ID   INS_ACIGU               Reviewed;          52 AA.
AC   P81423;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   29-OCT-2014, entry version 64.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae;
OC   Acipenser.
OX   NCBI_TaxID=7902;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=9650713;
RA   Rusakov Y.I., Moriyama S., Bondareva V.M., Kolychev A.P., Amemiya Y.,
RA   Yasuda A., Kawauchi H.;
RT   "Isolation and characterization of insulin in Russian sturgeon
RT   (Acipenser guldenstaedti).";
RL   J. Pept. Res. 51:395-400(1998).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P81423; -.
DR   SMR; P81423; 3-28.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                /FTId=PRO_0000015738.
FT   PEPTIDE      32     52       Insulin A chain.
FT                                /FTId=PRO_0000015739.
FT   DISULFID      7     38       Interchain (between B and A chains).
FT   DISULFID     19     51       Interchain (between B and A chains).
FT   DISULFID     37     42
FT   NON_CONS     31     32       {ECO:0000305}.
SQ   SEQUENCE   52 AA;  5811 MW;  BD1D693998D41631 CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYTPNK VGIVEQCCHS PCSLYDLENY CN
//
ID   INS_ACOCA               Reviewed;          51 AA.
AC   P01324;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 79.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Acomys cahirinus (Cairo spiny mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Deomyinae; Acomys.
OX   NCBI_TaxID=10068;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE.
RX   PubMed=5028210;
RA   Buenzli H.F., Humbel R.E.;
RT   "Isolation and partial structural analysis of insulin from mouse (Mus
RT   musculus) and spiny mouse (Acomys cahirinus).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 353:444-450(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01591; INMSSP.
DR   ProteinModelPortal; P01324; -.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015740.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015741.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     50       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     36     41       {ECO:0000250}.
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5768 MW;  992BD8B629047D3D CRC64;
     FVBQHLCGSH LVEALYLVCG ERGFFYTPKS GIVDQCCTSI CSLYQLENYC N
//
ID   INS_ALLMI               Reviewed;          51 AA.
AC   P12703;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Crocodylia;
OC   Alligatoridae; Alligatorinae; Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6146554; DOI=10.1016/0016-6480(84)90135-7;
RA   Lance V., Hamilton J.W., Rouse J.B., Kimmel J.R., Pollock H.G.;
RT   "Isolation and characterization of reptilian insulin, glucagon, and
RT   pancreatic polypeptide: complete amino acid sequence of alligator
RT   (Alligator mississippiensis) insulin and pancreatic polypeptide.";
RL   Gen. Comp. Endocrinol. 55:112-124(1984).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S07210; INAQ.
DR   ProteinModelPortal; P12703; -.
DR   SMR; P12703; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015742.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015743.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5689 MW;  19079AE89879876A CRC64;
     AANQRLCGSH LVDALYLVCG ERGFFYSPKG GIVEQCCHNT CSLYQLENYC N
//
ID   INS_AMICA               Reviewed;          52 AA.
AC   P29335;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   29-OCT-2014, entry version 70.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Amia calva (Bowfin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Amiiformes; Amiidae; Amia.
OX   NCBI_TaxID=7924;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2039477;
RA   Conlon J.M., Youson J.H., Whittaker J.;
RT   "Structure and receptor-binding activity of insulin from a holostean
RT   fish, the bowfin (Amia calva).";
RL   Biochem. J. 276:261-264(1991).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S15426; S15426.
DR   ProteinModelPortal; P29335; -.
DR   SMR; P29335; 3-52.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                /FTId=PRO_0000015744.
FT   PEPTIDE      32     52       Insulin A chain.
FT                                /FTId=PRO_0000015745.
FT   DISULFID      7     38       Interchain (between B and A chains).
FT   DISULFID     19     51       Interchain (between B and A chains).
FT   DISULFID     37     42
FT   NON_CONS     31     32       {ECO:0000305}.
SQ   SEQUENCE   52 AA;  5777 MW;  A3F5955F9C263FB1 CRC64;
     AASQHLCGSH LVEALFLVCG ESGFFYNPNK SGIVEQCCLK PCTIYEMEKY CN
//
ID   INS_ANGAN               Reviewed;          53 AA.
AC   P41522;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-OCT-2014, entry version 66.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor; Fragment;
GN   Name=ins;
OS   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30.
RC   TISSUE=Pancreas;
RX   PubMed=2776429;
RA   Conlon J.M., Thim L.;
RT   "Isolation and primary structure of the C-peptide of proinsulin from
RT   the European eel (Anguilla anguilla).";
RL   Comp. Biochem. Physiol. 93B:359-362(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-53.
RC   TISSUE=Pancreas;
RX   PubMed=1874385; DOI=10.1016/0016-6480(91)90292-E;
RA   Conlon J.M., Andrews P.C., Thim L., Moon T.W.;
RT   "The primary structure of glucagon-like peptide but not insulin has
RT   been conserved between the American eel, Anguilla rostrata and the
RT   European eel, Anguilla anguilla.";
RL   Gen. Comp. Endocrinol. 82:23-32(1991).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 represent paired basic residues
CC       assumed by homology to be present in the precursor molecule.
CC       {ECO:0000305}.
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DR   PIR; JL0099; JL0099.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   Pfam; PF00049; Insulin; 1.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PROPEP        1     30       C peptide.
FT                                /FTId=PRO_0000015749.
FT   PEPTIDE      33     53       Insulin A chain.
FT                                /FTId=PRO_0000015750.
FT   DISULFID     38     43
FT   NON_TER       1      1
SQ   SEQUENCE   53 AA;  5955 MW;  DDD3F00B33144EAD CRC64;
     DVEPLLGFLS PKSGQENEVD DFPYKGQGEL XXGIVEQCCH KPCNIFDLQN YCN
//
ID   INS_ANGRO               Reviewed;          51 AA.
AC   P42633;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-OCT-2014, entry version 69.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Anguilla rostrata (American eel) (Muraena rostrata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7938;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=1874385; DOI=10.1016/0016-6480(91)90292-E;
RA   Conlon J.M., Andrews P.C., Thim L., Moon T.W.;
RT   "The primary structure of glucagon-like peptide but not insulin has
RT   been conserved between the American eel, Anguilla rostrata and the
RT   European eel, Anguilla anguilla.";
RL   Gen. Comp. Endocrinol. 82:23-32(1991).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A61125; A61125.
DR   ProteinModelPortal; P42633; -.
DR   SMR; P42633; 4-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                {ECO:0000269|PubMed:1874385}.
FT                                /FTId=PRO_0000015751.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                {ECO:0000269|PubMed:1874385}.
FT                                /FTId=PRO_0000015752.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5652 MW;  1999FD7EEA173CB2 CRC64;
     ASTQHLCGSH LVEALYLVCG SNGFFFNPKD GIVEQCCHKP CSIFDLQNYC N
//
ID   INS_ANAPL               Reviewed;          81 AA.
AC   P01333;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Anas platyrhynchos (Domestic duck) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Anseriformes; Anatidae;
OC   Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 61-81.
RX   PubMed=4763354;
RA   Markussen J., Sundby F.;
RT   "Duck insulin: isolation, crystallization and amino acid sequence.";
RL   Int. J. Pept. Protein Res. 5:37-48(1973).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-58.
RX   PubMed=4715652; DOI=10.1111/j.1432-1033.1973.tb02772.x;
RA   Markussen J., Sundby F.;
RT   "Isolation and amino-acid sequence of the C-peptide of duck
RT   proinsulin.";
RL   Eur. J. Biochem. 34:401-408(1973).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 and 59-60 represent paired basic
CC       residues assumed by homology to be present in the precursor
CC       molecule. {ECO:0000305}.
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DR   PIR; A01600; IPDK.
DR   ProteinModelPortal; P01333; -.
DR   SMR; P01333; 3-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Reference proteome;
KW   Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                {ECO:0000269|PubMed:4763354}.
FT                                /FTId=PRO_0000015746.
FT   PROPEP       33     58       C peptide.
FT                                /FTId=PRO_0000015747.
FT   PEPTIDE      61     81       Insulin A chain.
FT                                {ECO:0000269|PubMed:4763354}.
FT                                /FTId=PRO_0000015748.
FT   DISULFID      7     67       Interchain (between B and A chains).
FT   DISULFID     19     80       Interchain (between B and A chains).
FT   DISULFID     66     71
SQ   SEQUENCE   81 AA;  9105 MW;  6EA8A271F099DA91 CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKT XXDVEQPLVN GPLHGEVGEL PFQHEEYQXX
     GIVEQCCENP CSLYQLENYC N
//
ID   INS_ANSAN               Reviewed;          51 AA.
AC   P68245; P07454; Q10995;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   29-OCT-2014, entry version 43.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Anser anser anser (Western graylag goose).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Anseriformes; Anatidae;
OC   Anser.
OX   NCBI_TaxID=8844;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Xu Y., Lin N., Zhang Y., Zhang Y.;
RT   "Isolation and sequence determination of goose insulin.";
RL   Kexue Tongbao 28:966-968(1983).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; JC0007; INGS.
DR   ProteinModelPortal; P68245; -.
DR   SMR; P68245; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015753.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015754.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5716 MW;  976EFAED8C68386D CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKT GIVEQCCENP CSLYQLENYC N
//
ID   INS_AOTTR               Reviewed;         108 AA.
AC   P67972; P10604;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-OCT-2014, entry version 46.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Aotidae; Aotus.
OX   NCBI_TaxID=9505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3118367; DOI=10.1073/pnas.84.21.7423;
RA   Seino S., Steiner D.F., Bell G.I.;
RT   "Sequence of a New World primate insulin having low biological potency
RT   and immunoreactivity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:7423-7427(1987).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; J02989; AAA35374.1; -; Genomic_DNA.
DR   PIR; A39883; A39883.
DR   ProteinModelPortal; P67972; -.
DR   SMR; P67972; 25-108.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015755.
FT   PROPEP       57     85       C peptide.
FT                                /FTId=PRO_0000015756.
FT   PEPTIDE      88    108       Insulin A chain.
FT                                /FTId=PRO_0000015757.
FT   DISULFID     31     94       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    107       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     93     98       {ECO:0000250}.
SQ   SEQUENCE   108 AA;  11842 MW;  1869B8250099731F CRC64;
     MALWMHLLPL LALLALWGPE PAPAFVNQHL CGPHLVEALY LVCGERGFFY APKTRREAED
     LQVGQVELGG GSITGSLPPL EGPMQKRGVV DQCCTSICSL YQLQNYCN
//
ID   INS_ATRSP               Reviewed;          52 AA.
AC   P09476;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Atractosteus spatula (Alligator gar) (Lepisosteus spatula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Atractosteus.
OX   NCBI_TaxID=7917;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3311873; DOI=10.1016/0016-6480(87)90192-4;
RA   Pollock H.G., Kimmel J.R., Hamilton J.W., Rouse J.B., Ebner K.E.,
RA   Lance V., Rawitch A.B.;
RT   "Isolation and structures of alligator gar (Lepisosteus spatula)
RT   insulin and pancreatic polypeptide.";
RL   Gen. Comp. Endocrinol. 67:375-382(1987).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S09342; INGXA.
DR   ProteinModelPortal; P09476; -.
DR   SMR; P09476; 3-52.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                {ECO:0000269|PubMed:3311873}.
FT                                /FTId=PRO_0000015830.
FT   PEPTIDE      32     52       Insulin A chain.
FT                                {ECO:0000269|PubMed:3311873}.
FT                                /FTId=PRO_0000015831.
FT   DISULFID      7     38       Interchain (between B and A chains).
FT   DISULFID     19     51       Interchain (between B and A chains).
FT   DISULFID     37     42
FT   NON_CONS     31     32       {ECO:0000305}.
SQ   SEQUENCE   52 AA;  5865 MW;  6D61138386AC0F10 CRC64;
     AANQHLCGSH LVEALYLVCG EKGFFYNPNK VGIVEQCCHK PCTIYELENY CN
//
ID   INS_BALBO               Reviewed;          51 AA.
AC   P01314;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Balaenoptera borealis (Sei whale) (Pollack whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
OC   Mysticeti; Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=9768;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=13552701; DOI=10.1038/1811468b0;
RA   Ishihara Y., Saito T., Ito Y., Fujino M.;
RT   "Structure of sperm- and sei-whale insulins and their breakdown by
RT   whale pepsin.";
RL   Nature 181:1468-1469(1958).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01582; INWH1S.
DR   ProteinModelPortal; P01314; -.
DR   SMR; P01314; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015758.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015759.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5724 MW;  9007B50E400A7DDD CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCAST CSLYQLENYC N
//
ID   INS_BALPH               Reviewed;          51 AA.
AC   P67973; P01312;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 44.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Balaenoptera physalus (Finback whale) (Common rorqual).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
OC   Mysticeti; Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=9770;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=14228503;
RA   Hama H., Titani K., Sakaki S., Narita K.;
RT   "The amino acid sequence in fin-whale insulin.";
RL   J. Biochem. 56:285-293(1964).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A91918; INWHF.
DR   PDB; 1BZV; NMR; -; A=31-51.
DR   PDBsum; 1BZV; -.
DR   ProteinModelPortal; P67973; -.
DR   SMR; P67973; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   EvolutionaryTrace; P67973; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015760.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015761.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
FT   HELIX        33     36       {ECO:0000244|PDB:1BZV}.
FT   STRAND       37     39       {ECO:0000244|PDB:1BZV}.
FT   HELIX        43     46       {ECO:0000244|PDB:1BZV}.
FT   TURN         47     49       {ECO:0000244|PDB:1BZV}.
SQ   SEQUENCE   51 AA;  5766 MW;  9007B514691A7CDD CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCTSI CSLYQLENYC N
//
ID   INS_BOVIN               Reviewed;         105 AA.
AC   P01317;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   29-OCT-2014, entry version 147.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2456452; DOI=10.1210/mend-1-4-327;
RA   D'Agostino J., Younes M.A., White J.W., Besch P.K., Field J.B.,
RA   Frazier M.L.;
RT   "Cloning and nucleotide sequence analysis of complementary
RT   deoxyribonucleic acid for bovine preproinsulin.";
RL   Mol. Endocrinol. 1:327-331(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-105.
RX   PubMed=4928892;
RA   Nolan C., Margoliash E., Peterson J.D., Steiner D.F.;
RT   "The structure of bovine proinsulin.";
RL   J. Biol. Chem. 246:2780-2795(1971).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-54.
RX   PubMed=14886311;
RA   Sanger F., Tuppy H.;
RT   "The amino-acid sequence in the phenylalanyl chain of insulin. 2. The
RT   investigation of peptides from enzymic hydrolysates.";
RL   Biochem. J. 49:481-490(1951).
RN   [4]
RP   PROTEIN SEQUENCE OF 57-82.
RX   PubMed=5545080;
RA   Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D.,
RA   Rubenstein A.H.;
RT   "Isolation and characterization of proinsulin C-peptide from bovine
RT   pancreas.";
RL   J. Biol. Chem. 246:1365-1374(1971).
RN   [5]
RP   PROTEIN SEQUENCE OF 57-82.
RX   PubMed=5105368; DOI=10.1111/j.1432-1033.1971.tb01377.x;
RA   Salokangas A., Smyth D.G., Markussen J., Sundby F.;
RT   "Bovine proinsulin: amino acid sequence of the C-peptide isolated from
RT   pancreas.";
RL   Eur. J. Biochem. 20:183-189(1971).
RN   [6]
RP   PROTEIN SEQUENCE OF 85-105.
RX   PubMed=13032079;
RA   Sanger F., Thompson E.O.P.;
RT   "The amino-acid sequence in the glycyl chain of insulin. 2. The
RT   investigation of peptides from enzymic hydrolysates.";
RL   Biochem. J. 53:366-374(1953).
RN   [7]
RP   PROTEIN SEQUENCE OF 25-54 AND 85-105, AND DISULFIDE BONDS.
RX   PubMed=13249947;
RA   Ryle A.P., Sanger F., Smith L.F., Kitai R.;
RT   "The disulphide bonds of insulin.";
RL   Biochem. J. 60:541-556(1955).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-54.
RA   Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G.,
RA   Reynolds C.D.;
RT   "The structure of des-Phe b1 bovine insulin.";
RL   Acta Crystallogr. B 38:3028-3032(1982).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-49.
RX   PubMed=9141131;
RX   DOI=10.1002/(SICI)1097-0134(199704)27:4<507::AID-PROT4>3.3.CO;2-H;
RA   Brange J., Dodson G.G., Edwards D.J., Holden P.H., Whittingham J.L.;
RT   "A model of insulin fibrils derived from the X-ray crystal structure
RT   of a monomeric insulin (despentapeptide insulin).";
RL   Proteins 27:507-516(1997).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- INTERACTION:
CC       Self; NbExp=6; IntAct=EBI-3989070, EBI-3989070;
CC       P08069:IGF1R (xeno); NbExp=4; IntAct=EBI-3989070, EBI-475981;
CC       P06213:INSR (xeno); NbExp=5; IntAct=EBI-3989070, EBI-475899;
CC       A1S3N8:Sama_0787 (xeno); NbExp=2; IntAct=EBI-3989070, EBI-7016414;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
CC       century - Issue 9 of April 2001;
CC       URL="http://web.expasy.org/spotlight/back_issues/009";
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DR   EMBL; M54979; AAA30722.1; -; mRNA.
DR   PIR; A40909; IPBO.
DR   UniGene; Bt.453; -.
DR   PDB; 1APH; X-ray; 2.00 A; A=85-105, B=25-54.
DR   PDB; 1BPH; X-ray; 2.00 A; A=85-105, B=25-54.
DR   PDB; 1CPH; X-ray; 1.90 A; A=85-105, B=25-54.
DR   PDB; 1DPH; X-ray; 1.90 A; A=85-105, B=25-54.
DR   PDB; 1HO0; NMR; -; A=25-54.
DR   PDB; 1PID; X-ray; 1.30 A; A/C=85-105, B/D=25-49.
DR   PDB; 2A3G; X-ray; 2.25 A; A/C=85-105, B/D=25-54.
DR   PDB; 2BN1; X-ray; 1.40 A; A=85-105, B=25-54.
DR   PDB; 2BN3; X-ray; 1.40 A; A=85-105, B=25-54.
DR   PDB; 2INS; X-ray; 2.50 A; A/C=85-105, B/D=26-54.
DR   PDB; 2ZP6; X-ray; 2.56 A; A/C=85-105, B/D=25-54.
DR   PDB; 3W14; X-ray; 4.40 A; A/I=85-105, B/J=25-54.
DR   PDB; 4BS3; X-ray; 2.30 A; A=85-105, B=25-54.
DR   PDB; 4E7T; X-ray; 1.40 A; A/C=85-105, B/D=25-54.
DR   PDB; 4E7U; X-ray; 1.30 A; A/C=85-105, B/D=25-54.
DR   PDB; 4E7V; X-ray; 1.80 A; 1/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y=85-105, 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z=25-54.
DR   PDB; 4I5Y; X-ray; 1.80 A; A=85-105, B=25-54.
DR   PDB; 4I5Z; X-ray; 1.80 A; A=85-105, B=25-54.
DR   PDB; 4IDW; X-ray; 2.70 A; A/C=85-105, B/D=25-54.
DR   PDB; 4IHN; X-ray; 1.16 A; A=85-105, B=25-54.
DR   PDB; 4M4F; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR   PDB; 4M4H; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR   PDB; 4M4I; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR   PDB; 4M4J; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR   PDB; 4M4L; X-ray; 1.45 A; A/C=85-105, B/D=25-54.
DR   PDB; 4M4M; X-ray; 1.50 A; A/C=85-105, B/D=25-54.
DR   PDBsum; 1APH; -.
DR   PDBsum; 1BPH; -.
DR   PDBsum; 1CPH; -.
DR   PDBsum; 1DPH; -.
DR   PDBsum; 1HO0; -.
DR   PDBsum; 1PID; -.
DR   PDBsum; 2A3G; -.
DR   PDBsum; 2BN1; -.
DR   PDBsum; 2BN3; -.
DR   PDBsum; 2INS; -.
DR   PDBsum; 2ZP6; -.
DR   PDBsum; 3W14; -.
DR   PDBsum; 4BS3; -.
DR   PDBsum; 4E7T; -.
DR   PDBsum; 4E7U; -.
DR   PDBsum; 4E7V; -.
DR   PDBsum; 4I5Y; -.
DR   PDBsum; 4I5Z; -.
DR   PDBsum; 4IDW; -.
DR   PDBsum; 4IHN; -.
DR   PDBsum; 4M4F; -.
DR   PDBsum; 4M4H; -.
DR   PDBsum; 4M4I; -.
DR   PDBsum; 4M4J; -.
DR   PDBsum; 4M4L; -.
DR   PDBsum; 4M4M; -.
DR   ProteinModelPortal; P01317; -.
DR   SMR; P01317; 25-105.
DR   DIP; DIP-52901N; -.
DR   IntAct; P01317; 5.
DR   Allergome; 2118; Bos d Insulin.
DR   eggNOG; NOG45999; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01317; -.
DR   EvolutionaryTrace; P01317; -.
DR   NextBio; 20804979; -.
DR   PMAP-CutDB; P01317; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:13249947,
FT                                ECO:0000269|PubMed:14886311,
FT                                ECO:0000269|PubMed:4928892}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                {ECO:0000269|PubMed:2456452}.
FT                                /FTId=PRO_0000015764.
FT   PROPEP       57     82       C peptide.
FT                                /FTId=PRO_0000015765.
FT   PEPTIDE      85    105       Insulin A chain.
FT                                {ECO:0000269|PubMed:2456452}.
FT                                /FTId=PRO_0000015766.
FT   DISULFID     31     91       Interchain (between B and A chains).
FT                                {ECO:0000269|PubMed:13249947}.
FT   DISULFID     43    104       Interchain (between B and A chains).
FT                                {ECO:0000269|PubMed:13249947}.
FT   DISULFID     90     95       {ECO:0000269|PubMed:13249947,
FT                                ECO:0000269|PubMed:4928892}.
FT   HELIX        33     43
FT   HELIX        44     46
FT   STRAND       48     50
FT   HELIX        86     90
FT   TURN         91     94
FT   HELIX        97    101
SQ   SEQUENCE   105 AA;  11393 MW;  75307CF78E61C06A CRC64;
     MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG
     PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL ENYCN
//
ID   INS_CALMI               Reviewed;          89 AA.
AC   P13190; O42485;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   29-OCT-2014, entry version 84.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Callorhynchus milii (Elephant fish) (Australian ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-89.
RX   PubMed=9356216; DOI=10.1006/gcen.1997.6965;
RA   Gieseg M.A., Swarbrick P.A., Perko L., Powell R.J., Cutfield J.F.;
RT   "Elephantfish proinsulin possesses a monobasic processing site.";
RL   Gen. Comp. Endocrinol. 108:199-208(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-31 AND 69-89.
RX   PubMed=2690815;
RA   Berks B.C., Marshall C.J., Carne A., Galloway S.M., Cutfield J.F.;
RT   "Isolation and structural characterization of insulin and glucagon
RT   from the holocephalan species Callorhynchus milii (elephantfish).";
RL   Biochem. J. 263:261-266(1989).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; U82395; AAB64356.1; -; Genomic_DNA.
DR   PIR; S06128; INEN.
DR   ProteinModelPortal; P13190; -.
DR   SMR; P13190; 4-29.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 2.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                /FTId=PRO_0000015772.
FT   PROPEP       33     66       C peptide.
FT                                /FTId=PRO_0000015773.
FT   PEPTIDE      69     89       Insulin A chain.
FT                                /FTId=PRO_0000015774.
FT   DISULFID      7     75       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     88       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     74     79       {ECO:0000250}.
SQ   SEQUENCE   89 AA;  10147 MW;  F2E8B0030BFCA7E3 CRC64;
     VPTQRLCGSH LVDALYFVCG ERGFFYSPKQ IRDVGPLSAF RDLEPPLDTE MEDRFPYRQQ
     LAGSKMKRGI VEQCCHNTCS LVNLEGYCN
//
ID   INS_CAIMO               Reviewed;          51 AA.
AC   P68243; P07454; Q10995;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   29-OCT-2014, entry version 44.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Cairina moschata (Muscovy duck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Anseriformes; Anatidae;
OC   Cairina.
OX   NCBI_TaxID=8855;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8759296; DOI=10.1016/0305-0491(95)02118-3;
RA   Chevalier B., Anglade P., Derouet M., Molle D., Simon J.;
RT   "Isolation and characterization of Muscovy (Cairna moschata) duck
RT   insulin.";
RL   Comp. Biochem. Physiol. 114B:19-26(1996).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P68243; -.
DR   SMR; P68243; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015770.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015771.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5716 MW;  976EFAED8C68386D CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKT GIVEQCCENP CSLYQLENYC N
//
ID   INS_CAMDR               Reviewed;          51 AA.
AC   P01320;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 73.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda;
OC   Camelidae; Camelus.
OX   NCBI_TaxID=9838;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Danho W.O.;
RT   "The isolation and characterization of insulin of camel (Camelus
RT   dromedarius).";
RL   J. Fac. Med. Baghdad 14:16-28(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A92782; INCMA.
DR   ProteinModelPortal; P01320; -.
DR   SMR; P01320; 3-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015775.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015776.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5694 MW;  901E88BA085A7DDD CRC64;
     FANQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCASV CSLYQLENYC N
//
ID   INS_CANFA               Reviewed;         110 AA.
AC   P01321;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 103.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6296142;
RA   Kwok S.C.M., Chan S.J., Steiner D.F.;
RT   "Cloning and nucleotide sequence analysis of the dog insulin gene.
RT   Coded amino acid sequence of canine preproinsulin predicts an
RT   additional C-peptide fragment.";
RL   J. Biol. Chem. 258:2357-2363(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; V00179; CAA23475.1; -; Genomic_DNA.
DR   PIR; A92413; IPDG.
DR   RefSeq; NP_001123565.1; NM_001130093.1.
DR   UniGene; Cfa.18796; -.
DR   ProteinModelPortal; P01321; -.
DR   SMR; P01321; 25-110.
DR   STRING; 9615.ENSCAFP00000014836; -.
DR   Ensembl; ENSCAFT00000016041; ENSCAFP00000014836; ENSCAFG00000010092.
DR   GeneID; 483665; -.
DR   KEGG; cfa:483665; -.
DR   CTD; 3630; -.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01321; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   NextBio; 20858027; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:5949593}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015777.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015778.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015779.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
SQ   SEQUENCE   110 AA;  12190 MW;  A574791864A4FB98 CRC64;
     MALWMRLLPL LALLALWAPA PTRAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVED
     LQVRDVELAG APGEGGLQPL ALEGALQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_CAPHI               Reviewed;          51 AA.
AC   P01319;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01586; INGT.
DR   ProteinModelPortal; P01319; -.
DR   SMR; P01319; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015780.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015781.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5692 MW;  9007B50CDB4E7DDD CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCAGV CSLYQLENYC N
//
ID   INS_CAVPO               Reviewed;         110 AA.
AC   P01329;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   01-OCT-2014, entry version 97.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3839794;
RA   Watt V.M.;
RT   "Sequence and evolution of guinea pig preproinsulin DNA.";
RL   J. Biol. Chem. 260:10926-10929(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6591179; DOI=10.1073/pnas.81.16.5046;
RA   Chan S.J., Episkopou V., Zeitlin S., Karathanasis S.K., Mackrell A.,
RA   Steiner D.F., Efstratiadis A.;
RT   "Guinea pig preproinsulin gene: an evolutionary compromise?";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5046-5050(1984).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
RN   [4]
RP   SEQUENCE REVISION.
RA   Smith L.F.;
RT   "Amino acid sequences of insulins.";
RL   Diabetes 21 Suppl. 2:457-460(1972).
RN   [5]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=1158864;
RA   Massey D.E., Smyth D.G.;
RT   "Guinea pig proinsulin. Primary structure of the C-peptide isolated
RT   from pancreas.";
RL   J. Biol. Chem. 250:6288-6290(1975).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; K02233; AAA37041.1; -; Genomic_DNA.
DR   EMBL; M11713; AAA37042.1; -; mRNA.
DR   PIR; A25370; IPGP.
DR   RefSeq; NP_001166362.1; NM_001172891.1.
DR   ProteinModelPortal; P01329; -.
DR   SMR; P01329; 25-53.
DR   STRING; 10141.ENSCPOP00000019016; -.
DR   Ensembl; ENSCPOT00000025967; ENSCPOP00000019016; ENSCPOG00000008198.
DR   GeneID; 100379579; -.
DR   CTD; 3630; -.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01329; -.
DR   OMA; VEQCCHN; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   TreeFam; TF332820; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:5949593}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                {ECO:0000269|PubMed:6591179}.
FT                                /FTId=PRO_0000015782.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015783.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                {ECO:0000269|PubMed:6591179}.
FT                                /FTId=PRO_0000015784.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
FT   CONFLICT     22     22       G -> N (in Ref. 2; AAA37041).
FT                                {ECO:0000305}.
FT   CONFLICT     81     84       ALEM -> QG (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   110 AA;  12187 MW;  DB22FE4A9CC5266C CRC64;
     MALWMHLLTV LALLALWGPN TGQAFVSRHL CGSNLVETLY SVCQDDGFFY IPKDRRELED
     PQVEQTELGM GLGAGGLQPL ALEMALQKRG IVDQCCTGTC TRHQLQSYCN
//
ID   INS_CHICH               Reviewed;          86 AA.
AC   P01327;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   29-OCT-2014, entry version 82.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Chinchilla chinchilla (Short-tailed chinchilla) (Chinchilla
OS   brevicaudata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Chinchillidae; Chinchilla.
OX   NCBI_TaxID=10152;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 66-86.
RX   PubMed=1175610; DOI=10.1111/j.1432-1033.1975.tb02190.x;
RA   Wood S.P., Blundell T.L., Wollmer A., Lazarus N.R., Neville R.W.J.;
RT   "The relation of conformation and association of insulin to receptor
RT   binding; X-ray and circular-dichroism studies on bovine and
RT   hystricomorph insulins.";
RL   Eur. J. Biochem. 55:531-542(1975).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-63.
RX   PubMed=808541;
RA   Snell C.R., Smyth D.G.;
RT   "Proinsulin: a proposed three-dimensional structure.";
RL   J. Biol. Chem. 250:6291-6295(1975).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 and 64-65 represent paired basic
CC       residues assumed by homology to be present in the precursor
CC       molecule. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; A01593; INCB.
DR   ProteinModelPortal; P01327; -.
DR   SMR; P01327; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015788.
FT   PROPEP       33     63       C peptide.
FT                                /FTId=PRO_0000043180.
FT   PEPTIDE      66     86       Insulin A chain.
FT                                /FTId=PRO_0000015789.
FT   DISULFID      7     72       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     85       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     71     76       {ECO:0000250}.
SQ   SEQUENCE   86 AA;  9470 MW;  95A4DAA4C004B4E2 CRC64;
     FVNKHLCGSH LVDALYLVCG DRGFFYTPMA XXELEDPQVG QADPGVVPEA GRLQPLALEM
     TLQXXGIVDQ CCTSICTLYQ LENYCN
//
ID   INS_CHICK               Reviewed;         107 AA.
AC   P67970; P01332; Q53YX4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 68.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7388949; DOI=10.1016/0092-8674(80)90641-8;
RA   Perler F., Efstratiadis A., Lomedico P., Gilbert W., Kolodner R.,
RA   Dodgson J.B.;
RT   "The evolution of genes: the chicken preproinsulin gene.";
RL   Cell 20:555-566(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RA   Hasegawa S., Honda K., Nata K., Yonekura H., Okamoto H., Hikami Y.;
RT   "Isolation of a cDNA encoding chicken insulin precursor.";
RL   Anim. Sci. Technol. 62:867-869(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nie Q., Fang M., Sun B., Lei M., Zhang X.;
RT   "Complete coding region of chicken preproinsulin gene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 25-54 AND 87-107.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; V00416; CAA23707.1; -; Genomic_DNA.
DR   EMBL; V00418; CAA23708.1; -; Genomic_DNA.
DR   EMBL; X58993; CAA41738.1; -; mRNA.
DR   EMBL; AY438372; AAR13049.1; -; Genomic_DNA.
DR   PIR; A90796; IPCH.
DR   RefSeq; NP_990553.1; NM_205222.3.
DR   UniGene; Gga.673; -.
DR   ProteinModelPortal; P67970; -.
DR   SMR; P67970; 27-107.
DR   PaxDb; P67970; -.
DR   Ensembl; ENSGALT00000010581; ENSGALP00000010567; ENSGALG00000006552.
DR   GeneID; 396145; -.
DR   KEGG; gga:396145; -.
DR   CTD; 3630; -.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P67970; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   PhylomeDB; P67970; -.
DR   TreeFam; TF332820; -.
DR   Reactome; REACT_197049; Amyloids.
DR   NextBio; 20816202; -.
DR   PRO; PR:P67970; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:AgBase.
DR   GO; GO:0003407; P:neural retina development; TAS:AgBase.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:5949593}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015790.
FT   PROPEP       57     84       C peptide.
FT                                /FTId=PRO_0000015791.
FT   PEPTIDE      87    107       Insulin A chain.
FT                                /FTId=PRO_0000015792.
FT   DISULFID     31     93       Interchain (between B and A chains).
FT   DISULFID     43    106       Interchain (between B and A chains).
FT   DISULFID     92     97
SQ   SEQUENCE   107 AA;  11981 MW;  3D43C5D82B25DCDD CRC64;
     MALWIRSLPL LALLVFSGPG TSYAAANQHL CGSHLVEALY LVCGERGFFY SPKARRDVEQ
     PLVSSPLRGE AGVLPFQQEE YEKVKRGIVE QCCHNTCSLY QLENYCN
//
ID   INS_CHIMO               Reviewed;          59 AA.
AC   P68991; P09536;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 41.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Chimaera monstrosa (Rabbit fish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Chimaeridae; Chimaera.
OX   NCBI_TaxID=7871;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3053327; DOI=10.1016/0016-6480(88)90191-8;
RA   Conlon J.M., Andrews P.C., Falkmer S., Thim L.;
RT   "Isolation and structural characterization of insulin from the
RT   holocephalan fish, Chimaera monstrosa (rabbit fish).";
RL   Gen. Comp. Endocrinol. 72:154-160(1988).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Due to a substitution of the Arg in position 31 by
CC       an Ile, this insulin B chain is longer than most other B chains
CC       and is processed differently.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; S06420; INRQ.
DR   ProteinModelPortal; P68991; -.
DR   SMR; P68991; 4-59.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     38       Insulin B chain.
FT                                /FTId=PRO_0000015793.
FT   PEPTIDE      39     59       Insulin A chain.
FT                                /FTId=PRO_0000015794.
FT   DISULFID      7     45       Interchain (between B and A chains).
FT   DISULFID     19     58       Interchain (between B and A chains).
FT   DISULFID     44     49
FT   NON_CONS     38     39       {ECO:0000305}.
SQ   SEQUENCE   59 AA;  6606 MW;  8827A57A9ED6D4AC CRC64;
     VPTQRLCGSH LVDALYFVCG ERGFFYSPKP IRELEPLLGI VEQCCHNTCS LANLEGYCN
//
ID   INS_CHLAE               Reviewed;         110 AA.
AC   P30407; P01309;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   29-OCT-2014, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1560757;
RA   Seino S., Bell G.I., Li W.;
RT   "Sequences of primate insulin genes support the hypothesis of a slower
RT   rate of molecular evolution in humans and apes than in monkeys.";
RL   Mol. Biol. Evol. 9:193-203(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=4626369;
RA   Peterson J.D., Nehrlich S., Oyer P.E., Steiner D.F.;
RT   "Determination of the amino acid sequence of the monkey, sheep, and
RT   dog proinsulin C-peptides by a semi-micro Edman degradation
RT   procedure.";
RL   J. Biol. Chem. 247:4866-4871(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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CC   -----------------------------------------------------------------------
DR   EMBL; X61092; CAA43405.1; -; Genomic_DNA.
DR   PIR; B42179; B42179.
DR   ProteinModelPortal; P30407; -.
DR   SMR; P30407; 25-110.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015785.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015786.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015787.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
SQ   SEQUENCE   110 AA;  12019 MW;  95A1F54BE7B247F9 CRC64;
     MALWMRLLPL LALLALWGPD PVPAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     PQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_CRILO               Reviewed;         110 AA.
AC   P01313;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   29-OCT-2014, entry version 86.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese
OS   hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6365663; DOI=10.2337/diab.33.3.297;
RA   Bell G.I., Sanchez-Pescador R.;
RT   "Sequence of a cDNA encoding Syrian hamster preproinsulin.";
RL   Diabetes 33:297-300(1984).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RA   Neelon F.A., Delcher H.K., Steinman H., Lebovitz H.E.;
RT   "Structure of hamster insulin: comparison with a tumor insulin.";
RL   Fed. Proc. 32:300-300(1973).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; M26328; AAA37089.1; -; mRNA.
DR   ProteinModelPortal; P01313; -.
DR   SMR; P01313; 25-110.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|Ref.2}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015797.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015798.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015799.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
SQ   SEQUENCE   110 AA;  12268 MW;  219E92B85A535CEC CRC64;
     MTLWMRLLPL LTLLVLWEPN PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKSRRGVED
     PQVAQLELGG GPGADDLQTL ALEVAQQKRG IVDQCCTSIC SLYQLENYCN
//
ID   INS_CROAT               Reviewed;          51 AA.
AC   P01334;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=939409; DOI=10.1016/0016-6480(76)90184-2;
RA   Kimmel J.R., Maher M.J., Pollock H.G., Vensel W.H.;
RT   "Isolation and characterization of reptilian insulin: partial amino
RT   acid sequence of rattlesnake (Crotalus atrox) insulin.";
RL   Gen. Comp. Endocrinol. 28:320-333(1976).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01601; INRS.
DR   ProteinModelPortal; P01334; -.
DR   SMR; P01334; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                {ECO:0000269|PubMed:939409}.
FT                                /FTId=PRO_0000015800.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                {ECO:0000269|PubMed:939409}.
FT                                /FTId=PRO_0000015801.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5794 MW;  951C975CF426A7B6 CRC64;
     APNQRLCGSH LVEALFLICG ERGFYYSPRS GIVEQCCENT CSLYQLENYC N
//
ID   INS_CYPCA               Reviewed;         108 AA.
AC   P01335;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 84.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6306593; DOI=10.1093/nar/11.13.4541;
RA   Hahn V., Winkler J., Rapoport T.A., Liebscher D.-H., Coutelle C.,
RA   Rosenthal S.;
RT   "Carp preproinsulin cDNA sequence and evolution of insulin genes.";
RL   Nucleic Acids Res. 11:4541-4552(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-108.
RX   PubMed=7037403; DOI=10.1111/j.1432-1033.1982.tb05886.x;
RA   Makower A., Dettmer R., Rapoport T.A., Knospe S., Behlke J., Prehn S.,
RA   Franke P., Etzold G., Rosenthal S.;
RT   "Carp insulin: amino acid sequence, biological activity and structural
RT   properties.";
RL   Eur. J. Biochem. 122:339-345(1982).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X00989; CAA25496.1; -; mRNA.
DR   PIR; A01602; IPCA.
DR   ProteinModelPortal; P01335; -.
DR   SMR; P01335; 27-52.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000269|PubMed:7037403}.
FT   PEPTIDE      22     51       Insulin B chain.
FT                                /FTId=PRO_0000015802.
FT   PROPEP       54     85       C peptide.
FT                                /FTId=PRO_0000015803.
FT   PEPTIDE      88    108       Insulin A chain.
FT                                {ECO:0000269|PubMed:6306593}.
FT                                /FTId=PRO_0000015804.
FT   DISULFID     30     94       Interchain (between B and A chains).
FT   DISULFID     42    107       Interchain (between B and A chains).
FT   DISULFID     93     98
SQ   SEQUENCE   108 AA;  11821 MW;  8656D5A50B862C42 CRC64;
     MAVWIQAGAL LFLLAVSSVN ANAGAPQHLC GSHLVDALYL VCGPTGFFYN PKRDVDPPLG
     FLPPKSAQET EVADFAFKDH AEVIRKRGIV EQCCHKPCSI FELQNYCN
//
ID   INS_DANRE               Reviewed;         108 AA.
AC   O73727; Q504H9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   29-OCT-2014, entry version 103.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9492081; DOI=10.1210/en.139.3.1440;
RA   Milewski W.M., Duguay S.J., Chan S.J., Steiner D.F.;
RT   "Conservation of PDX-1 structure, function, and expression in
RT   zebrafish.";
RL   Endocrinology 139:1440-1449(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF036326; AAC41261.1; -; mRNA.
DR   EMBL; BC095013; AAH95013.1; -; mRNA.
DR   RefSeq; NP_571131.1; NM_131056.1.
DR   UniGene; Dr.75811; -.
DR   ProteinModelPortal; O73727; -.
DR   SMR; O73727; 27-52.
DR   Ensembl; ENSDART00000051222; ENSDARP00000051221; ENSDARG00000035350.
DR   GeneID; 30262; -.
DR   KEGG; dre:30262; -.
DR   CTD; 3630; -.
DR   ZFIN; ZDB-GENE-980526-110; ins.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; O73727; -.
DR   KO; K04526; -.
DR   OMA; PQHLCGS; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   TreeFam; TF332820; -.
DR   Reactome; REACT_223535; Amyloids.
DR   NextBio; 20806709; -.
DR   Bgee; O73727; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000250}.
FT   PEPTIDE      22     51       Insulin B chain.
FT                                /FTId=PRO_0000015767.
FT   PROPEP       54     84       C peptide.
FT                                /FTId=PRO_0000015768.
FT   PEPTIDE      88    108       Insulin A chain.
FT                                /FTId=PRO_0000015769.
FT   DISULFID     30     94       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     42    107       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     93     98       {ECO:0000250}.
SQ   SEQUENCE   108 AA;  11904 MW;  31D03CCF37BD2C22 CRC64;
     MAVWLQAGAL LVLLVVSSVS TNPGTPQHLC GSHLVDALYL VCGPTGFFYN PKRDVEPLLG
     FLPPKSAQET EVADFAFKDH AELIRKRGIV EQCCHKPCSI FELQNYCN
//
ID   INS_ELEMA               Reviewed;          51 AA.
AC   P01316;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 76.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Elephas maximus (Indian elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Elephas.
OX   NCBI_TaxID=9783;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: The species of elephant is not given, but it is
CC       most probably the indian elephant (Elephas maximus).
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P01316; -.
DR   SMR; P01316; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015807.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015808.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5752 MW;  9007B50CDB457D6D CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKT GIVEQCCTGV CSLYQLENYC N
//
ID   INS_DIDVI               Reviewed;          51 AA.
AC   P18109;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   29-OCT-2014, entry version 74.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS   virginiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX   NCBI_TaxID=9267;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=2695899; DOI=10.1016/0196-9781(89)90012-0;
RA   Yu J.-H., Eng J., Rattan S., Yalow R.S.;
RT   "Opossum insulin, glucagon and pancreatic polypeptide: amino acid
RT   sequences.";
RL   Peptides 10:1195-1197(1989).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; JQ0362; JQ0362.
DR   ProteinModelPortal; P18109; -.
DR   SMR; P18109; 2-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015805.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015806.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5732 MW;  9007B8BAE4BDEEDD CRC64;
     LVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCNSI CSLYQLETYC N
//
ID   INS_FELCA               Reviewed;         110 AA.
AC   P06306; Q8WNW6;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   29-OCT-2014, entry version 93.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RA   Okamoto S., Morimatsu M.;
RT   "Cat insulin.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=3518635; DOI=10.1016/0003-9861(86)90528-X;
RA   Hallden G., Gafvelin G., Mutt V., Joernvall H.;
RT   "Characterization of cat insulin.";
RL   Arch. Biochem. Biophys. 247:20-27(1986).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AB043535; BAB84110.1; -; mRNA.
DR   PIR; A01588; INCT.
DR   RefSeq; NP_001009272.1; NM_001009272.1.
DR   ProteinModelPortal; P06306; -.
DR   SMR; P06306; 25-110.
DR   Ensembl; ENSFCAT00000023517; ENSFCAP00000020961; ENSFCAG00000024114.
DR   GeneID; 493804; -.
DR   KEGG; fca:493804; -.
DR   CTD; 3630; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P06306; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:3518635}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015809.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000227016.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015810.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
SQ   SEQUENCE   110 AA;  12069 MW;  95FB6E170C7BECA4 CRC64;
     MAPWTRLLPL LALLSLWIPA PTRAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAED
     LQGKDAELGE APGAGGLQPS ALEAPLQKRG IVEQCCASVC SLYQLEHYCN
//
ID   INS_GADMC               Reviewed;          51 AA.
AC   P01336;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 82.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8053;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4881974;
RA   Reid K.B.M., Grant P.T., Youngson A.;
RT   "The sequence of amino acids in insulin isolated from islet tissue of
RT   the cod (Gadus callarias).";
RL   Biochem. J. 110:289-296(1968).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=4866431;
RA   Grant P.T., Reid K.B.M.;
RT   "Isolation and a partial amino acid sequence of insulin from the islet
RT   tissue of cod (Gadus callarias).";
RL   Biochem. J. 106:531-541(1968).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P01336; -.
DR   SMR; P01336; 5-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015811.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015812.
FT   DISULFID      8     37       Interchain (between B and A chains).
FT   DISULFID     20     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5789 MW;  A51FD0C5D483705A CRC64;
     MAPPQHLCGS HLVDALYLVC GDRGFFYNPK GIVDQCCHRP CDIFDLQNYC N
//
ID   INS_GORGO               Reviewed;         110 AA.
AC   Q6YK33;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-OCT-2014, entry version 61.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Gorilla gorilla gorilla (Lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY137500; AAN06935.1; -; Genomic_DNA.
DR   RefSeq; XP_004050475.1; XM_004050427.1.
DR   RefSeq; XP_004050476.1; XM_004050428.1.
DR   ProteinModelPortal; Q6YK33; -.
DR   SMR; Q6YK33; 25-110.
DR   Ensembl; ENSGGOT00000030259; ENSGGOP00000018194; ENSGGOG00000022826.
DR   GeneID; 101132604; -.
DR   KEGG; ggo:101132604; -.
DR   CTD; 3630; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; Q6YK33; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015813.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015814.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015815.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  11981 MW;  C2C3B23B85E520E5 CRC64;
     MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_HORSE               Reviewed;          86 AA.
AC   P01310;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 83.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 66-86.
RX   PubMed=13373434; DOI=10.1016/0003-9861(56)90203-X;
RA   Harris J.I., Sanger F., Naughton M.A.;
RT   "Species differences in insulin.";
RL   Arch. Biochem. Biophys. 65:427-438(1956).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-63.
RX   PubMed=4640931;
RA   Tager H.S., Steiner D.F.;
RT   "Primary structures of the proinsulin connecting peptides of the rat
RT   and the horse.";
RL   J. Biol. Chem. 247:7936-7940(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 and 64-65 represent paired basic
CC       residues assumed by homology to be present in the precursor
CC       molecule. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   PIR; A01580; IPHO.
DR   ProteinModelPortal; P01310; -.
DR   SMR; P01310; 1-30.
DR   STRING; 9796.ENSECAP00000022114; -.
DR   eggNOG; NOG45999; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01310; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Reference proteome;
KW   Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015816.
FT   PROPEP       33     63       C peptide.
FT                                /FTId=PRO_0000015817.
FT   PEPTIDE      66     86       Insulin A chain.
FT                                /FTId=PRO_0000015818.
FT   DISULFID      7     72       Interchain (between B and A chains).
FT   DISULFID     19     85       Interchain (between B and A chains).
FT   DISULFID     71     76
SQ   SEQUENCE   86 AA;  9147 MW;  A3E1E822711BDB46 CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA XXEAEDPQVG EVELGGGPGL GGLQPLALAG
     PQQXXGIVEQ CCTGICSLYQ LENYCN
//
ID   INS_HUMAN               Reviewed;         110 AA.
AC   P01308; Q5EEX2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 197.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6243748; DOI=10.1038/284026a0;
RA   Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E.,
RA   Goodman H.M.;
RT   "Sequence of the human insulin gene.";
RL   Nature 284:26-32(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6248962; DOI=10.1126/science.6248962;
RA   Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.;
RT   "Genetic variation in the human insulin gene.";
RL   Science 209:612-615(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=503234; DOI=10.1038/282525a0;
RA   Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M.,
RA   Rutter W.J.;
RT   "Nucleotide sequence of a cDNA clone encoding human preproinsulin.";
RL   Nature 282:525-527(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6927840; DOI=10.1126/science.6927840;
RA   Sures I., Goeddel D.V., Gray A., Ullrich A.;
RT   "Nucleotide sequence of human preproinsulin complementary DNA.";
RL   Science 208:57-59(1980).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8358440; DOI=10.1038/ng0793-305;
RA   Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P.,
RA   Lathrop M., Bell J.I.;
RT   "Susceptibility to insulin dependent diabetes mellitus maps to a 4.1
RT   kb segment of DNA spanning the insulin gene and associated VNTR.";
RL   Nat. Genet. 4:305-310(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15070567; DOI=10.1016/S0140-6736(04)15438-X;
RA   Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M.,
RA   Libutti S.K., Shalev A.;
RT   "Insulinomas and expression of an insulin splice variant.";
RL   Lancet 363:363-367(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC   TISSUE=Blood;
RA   Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.;
RT   "Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G)
RT   within the 5' region of insulin gene.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=14426955; DOI=10.1038/187483a0;
RA   Nicol D.S.H.W., Smith L.F.;
RT   "Amino-acid sequence of human insulin.";
RL   Nature 187:483-485(1960).
RN   [13]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=5101771;
RA   Oyer P.E., Cho S., Peterson J.D., Steiner D.F.;
RT   "Studies on human proinsulin. Isolation and amino acid sequence of the
RT   human pancreatic C-peptide.";
RL   J. Biol. Chem. 246:1375-1386(1971).
RN   [14]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=5560404; DOI=10.1111/j.1432-1033.1971.tb01378.x;
RA   Ko A., Smyth D.G., Markussen J., Sundby F.;
RT   "The amino acid sequence of the C-peptide of human proinsulin.";
RL   Eur. J. Biochem. 20:190-199(1971).
RN   [15]
RP   SYNTHESIS.
RX   PubMed=4443293; DOI=10.1002/hlca.19740570839;
RA   Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.;
RT   "Total synthesis of human insulin under directed formation of the
RT   disulfide bonds.";
RL   Helv. Chim. Acta 57:2617-2621(1974).
RN   [16]
RP   SYNTHESIS OF 57-87.
RX   PubMed=4803504;
RA   Naithani V.K.;
RT   "Studies on polypeptides, IV. The synthesis of C-peptide of human
RT   proinsulin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1973).
RN   [17]
RP   SYNTHESIS OF 65-69 AND 70-73.
RX   PubMed=4698555; DOI=10.1002/cber.19731060124;
RA   Geiger R., Volk A.;
RT   "Synthesis of peptides with the properties of human proinsulin C
RT   peptides (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of
RT   human proinsulin C peptides.";
RL   Chem. Ber. 106:199-205(1973).
RN   [18]
RP   SYNTHESIS OF 84-87.
RX   PubMed=4698553; DOI=10.1002/cber.19731060122;
RA   Geiger R., Jaeger G., Keonig W., Treuth G.;
RT   "Synthesis of peptides with the properties of human proinsulin C
RT   peptides (hC peptide). I. Scheme for the synthesis and preparation of
RT   the sequence 28-31 of human proinsulin C peptide.";
RL   Chem. Ber. 106:188-192(1973).
RN   [19]
RP   VARIANT LOS ANGELES SER-48.
RX   PubMed=6312455; DOI=10.1073/pnas.80.20.6366;
RA   Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.;
RT   "Studies on mutant human insulin genes: identification and sequence
RT   analysis of a gene encoding [SerB24]insulin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983).
RN   [20]
RP   VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49.
RX   PubMed=6424111; DOI=10.1073/pnas.80.24.7390;
RA   Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T.,
RA   Rubenstein A.H., Tager H.;
RT   "Identification of a mutant human insulin predicted to contain a
RT   serine-for-phenylalanine substitution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983).
RN   [21]
RP   VARIANT FHPRI ASP-34.
RX   PubMed=3470784; DOI=10.1073/pnas.84.8.2194;
RA   Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.;
RT   "A mutation in the B chain coding region is associated with impaired
RT   proinsulin conversion in a family with hyperproinsulinemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1987).
RN   [22]
RP   VARIANT WAKAYAMA LEU-92.
RX   PubMed=3537011; DOI=10.1172/JCI112760;
RA   Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.;
RT   "Structurally abnormal insulin in a diabetic patient. Characterization
RT   of the mutant insulin A3 (Val-->Leu) isolated from the pancreas.";
RL   J. Clin. Invest. 78:1666-1672(1986).
RN   [23]
RP   VARIANT FHPRI HIS-89.
RX   PubMed=2196279; DOI=10.1210/jcem-71-1-164;
RA   Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H.,
RA   Merenich J.A., Taylor S.I., Roth J.;
RT   "Two unrelated patients with familial hyperproinsulinemia due to a
RT   mutation substituting histidine for arginine at position 65 in the
RT   proinsulin molecule: identification of the mutation by direct
RT   sequencing of genomic deoxyribonucleic acid amplified by polymerase
RT   chain reaction.";
RL   J. Clin. Endocrinol. Metab. 71:164-169(1990).
RN   [24]
RP   VARIANT FHPRI HIS-89.
RX   PubMed=4019786; DOI=10.1172/JCI111973;
RA   Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.;
RT   "Posttranslational cleavage of proinsulin is blocked by a point
RT   mutation in familial hyperproinsulinemia.";
RL   J. Clin. Invest. 76:378-380(1985).
RN   [25]
RP   VARIANT FHPRI LEU-89.
RX   PubMed=1601997; DOI=10.1172/JCI115795;
RA   Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.;
RT   "A novel point mutation in the human insulin gene giving rise to
RT   hyperproinsulinemia (proinsulin Kyoto).";
RL   J. Clin. Invest. 89:1902-1907(1992).
RN   [26]
RP   STRUCTURE BY NMR.
RX   PubMed=2271664; DOI=10.1021/bi00498a018;
RA   Hua Q.-X., Weiss M.A.;
RT   "Toward the solution structure of human insulin: sequential 2D 1H NMR
RT   assignment of a des-pentapeptide analogue and comparison with crystal
RT   structure.";
RL   Biochemistry 29:10545-10555(1990).
RN   [27]
RP   STRUCTURE BY NMR.
RX   PubMed=2036420; DOI=10.1021/bi00236a025;
RA   Hua Q.-X., Weiss M.A.;
RT   "Comparative 2D NMR studies of human insulin and des-pentapeptide
RT   insulin: sequential resonance assignment and implications for protein
RT   dynamics and receptor recognition.";
RL   Biochemistry 30:5505-5515(1991).
RN   [28]
RP   STRUCTURE BY NMR.
RX   PubMed=1646635; DOI=10.1016/0167-4838(91)90098-K;
RA   Hua Q.-X., Weiss M.A.;
RT   "Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-
RT   specific resonance assignments and effects of solvent composition.";
RL   Biochim. Biophys. Acta 1078:101-110(1991).
RN   [29]
RP   STRUCTURE BY NMR.
RX   PubMed=1433291; DOI=10.1016/0022-2836(92)90527-Q;
RA   Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.;
RT   "Three-dimensional solution structure of an insulin dimer. A study of
RT   the B9(Asp) mutant of human insulin using nuclear magnetic resonance,
RT   distance geometry and restrained molecular dynamics.";
RL   J. Mol. Biol. 227:1146-1163(1992).
RN   [30]
RP   STRUCTURE BY NMR OF VARIANT LOS-ANGELES SER-48.
RX   PubMed=8421693; DOI=10.1073/pnas.90.2.582;
RA   Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.;
RT   "Paradoxical structure and function in a mutant human insulin
RT   associated with diabetes mellitus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993).
RN   [31]
RP   STRUCTURE BY NMR.
RX   PubMed=9235985; DOI=10.1021/bi9631069;
RA   Chang X., Joergensen A.M., Bardrum P., Led J.J.;
RT   "Solution structures of the R6 human insulin hexamer.";
RL   Biochemistry 36:9409-9422(1997).
RN   [32]
RP   VARIANTS PNDM ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89;
RP   CYS-90; TYR-96 AND CYS-108.
RX   PubMed=17855560; DOI=10.1073/pnas.0707291104;
RA   Stoy J., Edghill E.L., Flanagan S.E., Ye H., Paz V.P., Pluzhnikov A.,
RA   Below J.E., Hayes M.G., Cox N.J., Lipkind G.M., Lipton R.B.,
RA   Greeley S.A., Patch A.M., Ellard S., Steiner D.F., Hattersley A.T.,
RA   Philipson L.H., Bell G.I.;
RT   "Insulin gene mutations as a cause of permanent neonatal diabetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15040-15044(2007).
RN   [33]
RP   VARIANTS PNDM ASP-24; ASP-29; ARG-32; SER-32; PRO-35; GLY-43; VAL-47;
RP   CYS-48; ARG-84; CYS-89; CYS-90; SER-96; TYR-96; CYS-101; CYS-103 AND
RP   CYS-108, VARIANT MODY10 CYS-6, AND VARIANT MET-68.
RX   PubMed=18162506; DOI=10.2337/db07-1405;
RA   Edghill E.L., Flanagan S.E., Patch A.M., Boustred C., Parrish A.,
RA   Shields B., Shepherd M.H., Hussain K., Kapoor R.R., Malecki M.,
RA   MacDonald M.J., Stoy J., Steiner D.F., Philipson L.H., Bell G.I.,
RA   Hattersley A.T., Ellard S.;
RT   "Insulin mutation screening in 1,044 patients with diabetes: mutations
RT   in the INS gene are a common cause of neonatal diabetes but a rare
RT   cause of diabetes diagnosed in childhood or adulthood.";
RL   Diabetes 57:1034-1042(2008).
RN   [34]
RP   VARIANT MODY10 GLN-46, AND VARIANT IDDM2 CYS-55.
RX   PubMed=18192540; DOI=10.2337/db07-1467;
RA   Molven A., Ringdal M., Nordbo A.M., Raeder H., Stoy J., Lipkind G.M.,
RA   Steiner D.F., Philipson L.H., Bergmann I., Aarskog D., Undlien D.E.,
RA   Joner G., Sovik O., Bell G.I., Njolstad P.R.;
RT   "Mutations in the insulin gene can cause MODY and autoantibody-
RT   negative type 1 diabetes.";
RL   Diabetes 57:1131-1135(2008).
RN   [35]
RP   VARIANTS MODY10 HIS-6 AND GLN-46.
RX   PubMed=20226046; DOI=10.1186/1471-2350-11-42;
RA   Boesgaard T.W., Pruhova S., Andersson E.A., Cinek O., Obermannova B.,
RA   Lauenborg J., Damm P., Bergholdt R., Pociot F., Pisinger C.,
RA   Barbetti F., Lebl J., Pedersen O., Hansen T.;
RT   "Further evidence that mutations in INS can be a rare cause of
RT   Maturity-Onset Diabetes of the Young (MODY).";
RL   BMC Med. Genet. 11:42-42(2010).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- INTERACTION:
CC       Self; NbExp=16; IntAct=EBI-7090529, EBI-7090529;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P01308-1; Sequence=Displayed;
CC       Name=2; Synonyms=INS-IGF2;
CC         IsoId=F8WCM5-1; Sequence=External;
CC         Note=Based on a readthrough transcript which may produce an
CC         INS-IGF2 fusion protein.;
CC   -!- DISEASE: Hyperproinsulinemia, familial (FHPRI) [MIM:176730]: An
CC       autosomal dominant condition characterized by elevated levels of
CC       serum proinsulin-like material. {ECO:0000269|PubMed:1601997,
CC       ECO:0000269|PubMed:2196279, ECO:0000269|PubMed:3470784,
CC       ECO:0000269|PubMed:4019786}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Diabetes mellitus, insulin-dependent, 2 (IDDM2)
CC       [MIM:125852]: A multifactorial disorder of glucose homeostasis
CC       that is characterized by susceptibility to ketoacidosis in the
CC       absence of insulin therapy. Clinical features are polydipsia,
CC       polyphagia and polyuria which result from hyperglycemia-induced
CC       osmotic diuresis and secondary thirst. These derangements result
CC       in long-term complications that affect the eyes, kidneys, nerves,
CC       and blood vessels. {ECO:0000269|PubMed:18192540}. Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Diabetes mellitus, permanent neonatal (PNDM)
CC       [MIM:606176]: A rare form of diabetes distinct from childhood-
CC       onset autoimmune diabetes mellitus type 1. It is characterized by
CC       insulin-requiring hyperglycemia that is diagnosed within the first
CC       months of life. Permanent neonatal diabetes requires lifelong
CC       therapy. {ECO:0000269|PubMed:17855560,
CC       ECO:0000269|PubMed:18162506}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Maturity-onset diabetes of the young 10 (MODY10)
CC       [MIM:613370]: A form of diabetes that is characterized by an
CC       autosomal dominant mode of inheritance, onset in childhood or
CC       early adulthood (usually before 25 years of age), a primary defect
CC       in insulin secretion and frequent insulin-independence at the
CC       beginning of the disease. {ECO:0000269|PubMed:18162506,
CC       ECO:0000269|PubMed:18192540, ECO:0000269|PubMed:20226046}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- PHARMACEUTICAL: Available under the names Humulin or Humalog (Eli
CC       Lilly) and Novolin (Novo Nordisk). Used in the treatment of
CC       diabetes. Humalog is an insulin analog with 52-Lys-Pro-53 instead
CC       of 52-Pro-Lys-53.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA59179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Insulin at Eli Lilly; Note=Clinical information
CC       on Eli Lilly insulin products;
CC       URL="http://www.lillyDiabetes.com/Products/PatientInfo.cfm";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
CC       century - Issue 9 of April 2001;
CC       URL="http://web.expasy.org/spotlight/back_issues/009";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Insulin entry;
CC       URL="http://en.wikipedia.org/wiki/Insulin";
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DR   EMBL; V00565; CAA23828.1; -; Genomic_DNA.
DR   EMBL; M10039; AAA59173.1; -; Genomic_DNA.
DR   EMBL; J00265; AAA59172.1; -; Genomic_DNA.
DR   EMBL; X70508; CAA49913.1; -; mRNA.
DR   EMBL; L15440; AAA59179.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY899304; AAW83741.1; -; mRNA.
DR   EMBL; AY138590; AAN39451.1; -; Genomic_DNA.
DR   EMBL; BT006808; AAP35454.1; -; mRNA.
DR   EMBL; CH471158; EAX02488.1; -; Genomic_DNA.
DR   EMBL; BC005255; AAH05255.1; -; mRNA.
DR   EMBL; AJ009655; CAA08766.1; -; Genomic_DNA.
DR   CCDS; CCDS7729.1; -. [P01308-1]
DR   PIR; A93222; IPHU.
DR   RefSeq; NP_000198.1; NM_000207.2. [P01308-1]
DR   RefSeq; NP_001172026.1; NM_001185097.1. [P01308-1]
DR   RefSeq; NP_001172027.1; NM_001185098.1. [P01308-1]
DR   RefSeq; NP_001278826.1; NM_001291897.1. [P01308-1]
DR   UniGene; Hs.272259; -.
DR   PDB; 1A7F; NMR; -; A=90-110, B=25-53.
DR   PDB; 1AI0; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1B9E; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1BEN; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 1EFE; NMR; -; A=25-54, A=90-110.
DR   PDB; 1EV3; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
DR   PDB; 1EV6; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1EVR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1FU2; X-ray; 3.24 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1FUB; X-ray; 3.09 A; A/C=90-110, B/D=25-54.
DR   PDB; 1G7A; X-ray; 1.20 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1G7B; X-ray; 1.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1GUJ; X-ray; 1.62 A; A/C=90-110, B/D=25-54.
DR   PDB; 1HIQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HIS; NMR; -; A=90-110, B=25-49.
DR   PDB; 1HIT; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HLS; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HTV; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-51.
DR   PDB; 1HUI; NMR; -; A=90-110, B=26-53.
DR   PDB; 1IOG; NMR; -; A=90-110, B=25-53.
DR   PDB; 1IOH; NMR; -; A=90-110, B=25-53.
DR   PDB; 1J73; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1JCA; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1JCO; NMR; -; A=90-110, B=25-54.
DR   PDB; 1JK8; X-ray; 2.40 A; C=35-47.
DR   PDB; 1K3M; NMR; -; A=90-110, B=25-54.
DR   PDB; 1KMF; NMR; -; A=90-110, B=25-54.
DR   PDB; 1LKQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1LPH; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 1MHI; NMR; -; A=90-110, B=25-54.
DR   PDB; 1MHJ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1MSO; X-ray; 1.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1OS3; X-ray; 1.95 A; A/C=90-110, B/D=25-54.
DR   PDB; 1OS4; X-ray; 2.25 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1Q4V; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1QIY; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1QIZ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1QJ0; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 1RWE; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 1SF1; NMR; -; A=90-110, B=25-54.
DR   PDB; 1SJT; NMR; -; A=90-110, B=25-51.
DR   PDB; 1SJU; NMR; -; A=25-110.
DR   PDB; 1T0C; NMR; -; A=57-87.
DR   PDB; 1T1K; NMR; -; A=90-110, B=25-54.
DR   PDB; 1T1P; NMR; -; A=90-110, B=25-54.
DR   PDB; 1T1Q; NMR; -; A=90-110, B=25-54.
DR   PDB; 1TRZ; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 1TYL; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 1TYM; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 1UZ9; X-ray; 1.60 A; A=90-110, B=25-53.
DR   PDB; 1VKT; NMR; -; A=90-110, B=25-54.
DR   PDB; 1W8P; X-ray; 2.08 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1XDA; X-ray; 1.80 A; A/C/E/G=90-110, B/D/F/H=25-53.
DR   PDB; 1XGL; NMR; -; A=90-110, B=25-54.
DR   PDB; 1XW7; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZEG; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZEH; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZNJ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2C8Q; X-ray; 1.95 A; A=90-110, B=25-53.
DR   PDB; 2C8R; X-ray; 1.50 A; A=90-110, B=25-53.
DR   PDB; 2CEU; X-ray; 1.80 A; A/C=90-110, B/D=25-49.
DR   PDB; 2G54; X-ray; 2.25 A; C/D=25-54.
DR   PDB; 2G56; X-ray; 2.20 A; C/D=25-54.
DR   PDB; 2H67; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HH4; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HHO; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HIU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JMN; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUM; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUV; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JV1; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JZQ; NMR; -; A=25-54, A=90-110.
DR   PDB; 2K91; NMR; -; A=90-110, B=25-54.
DR   PDB; 2K9R; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KJJ; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KJU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KQP; NMR; -; A=25-110.
DR   PDB; 2KQQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KXK; NMR; -; A=90-110, B=25-54.
DR   PDB; 2L1Y; NMR; -; A=90-110, B=25-54.
DR   PDB; 2L1Z; NMR; -; A=90-110, B=25-54.
DR   PDB; 2LGB; NMR; -; A=90-110, B=25-55.
DR   PDB; 2LWZ; NMR; -; A=25-54, A=89-110.
DR   PDB; 2M1D; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M1E; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2M; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2N; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2O; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2P; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MLI; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MPG; NMR; -; A=90-110, B=25-54.
DR   PDB; 2OLY; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2OLZ; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2OM0; X-ray; 2.05 A; 1/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k=90-110, 2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l=25-54.
DR   PDB; 2OM1; X-ray; 1.97 A; 1/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k=90-110, 2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l=25-54.
DR   PDB; 2OMG; X-ray; 1.52 A; A/C/E=90-110, B/D/F=25-54.
DR   PDB; 2OMH; X-ray; 1.36 A; A/C/E=90-110, B/D/F=25-54.
DR   PDB; 2OMI; X-ray; 2.24 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2OMQ; X-ray; 2.00 A; A/B/C/D=36-41.
DR   PDB; 2QIU; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R34; X-ray; 2.25 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R35; X-ray; 2.08 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R36; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
DR   PDB; 2RN5; NMR; -; A=90-110, B=25-54.
DR   PDB; 2VJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 2VK0; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 2W44; X-ray; 2.00 A; A/C/E=94-110, B/D/F=25-53.
DR   PDB; 2WBY; X-ray; 2.60 A; C/E=90-109, D/F=25-43.
DR   PDB; 2WC0; X-ray; 2.80 A; C/E=90-110, D/F=25-54.
DR   PDB; 2WRU; X-ray; 1.57 A; A=90-110, B=25-50.
DR   PDB; 2WRV; X-ray; 2.15 A; A=90-110, B=25-50.
DR   PDB; 2WRW; X-ray; 2.41 A; A=90-110, B=25-50.
DR   PDB; 2WRX; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 2WS0; X-ray; 2.10 A; A=90-110, B=25-54.
DR   PDB; 2WS1; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 2WS4; X-ray; 1.90 A; A=90-110, B=25-50.
DR   PDB; 2WS6; X-ray; 1.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2WS7; X-ray; 2.59 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-50.
DR   PDB; 3AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3BRR; X-ray; 1.70 A; A/C=90-110, B/D=25-53.
DR   PDB; 3BXQ; X-ray; 1.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 3E7Y; X-ray; 1.60 A; A/C=90-110, B/D=25-53.
DR   PDB; 3E7Z; X-ray; 1.70 A; A/C=90-110, B/D=25-53.
DR   PDB; 3EXX; X-ray; 1.35 A; A/C=90-110, B/D=25-54.
DR   PDB; 3FQ9; X-ray; 1.35 A; A/C=91-110, B/D=25-54.
DR   PDB; 3HYD; X-ray; 1.00 A; A=35-41.
DR   PDB; 3I3Z; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 3I40; X-ray; 1.85 A; A=90-110, B=25-54.
DR   PDB; 3ILG; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 3INC; X-ray; 1.85 A; A/C=90-110, B/D=25-54.
DR   PDB; 3IR0; X-ray; 2.20 A; A/C/E/G/I/K/M/O/R/T/V/X=90-110, B/D/F/H/J/L/N/P/S/U/W/Y=25-54.
DR   PDB; 3JSD; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 3KQ6; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 3P2X; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 3P33; X-ray; 2.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 3Q6E; X-ray; 2.05 A; A/C=90-110, B/D=25-54.
DR   PDB; 3ROV; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3TT8; X-ray; 1.12 A; A/C=90-110, B/D=25-54.
DR   PDB; 3U4N; X-ray; 1.98 A; A=90-110, B=25-53.
DR   PDB; 3UTQ; X-ray; 1.67 A; C=15-24.
DR   PDB; 3UTS; X-ray; 2.71 A; C/H=15-24.
DR   PDB; 3UTT; X-ray; 2.60 A; C/H=15-24.
DR   PDB; 3V19; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 3V1G; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W11; X-ray; 3.90 A; A=90-110, B=25-54.
DR   PDB; 3W12; X-ray; 4.30 A; A=90-110, B=25-50.
DR   PDB; 3W13; X-ray; 4.30 A; A=90-110, B=25-50.
DR   PDB; 3W7Y; X-ray; 0.92 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W7Z; X-ray; 1.15 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W80; X-ray; 1.40 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 3ZI3; X-ray; 1.70 A; A=90-110, B=25-54.
DR   PDB; 3ZQR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3ZS2; X-ray; 1.97 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3ZU1; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 4AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 4AJX; X-ray; 1.20 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-53.
DR   PDB; 4AJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-53.
DR   PDB; 4AK0; X-ray; 2.28 A; A=90-110, B=25-53.
DR   PDB; 4AKJ; X-ray; 2.01 A; A/C=90-110, B/D=25-53.
DR   PDB; 4CXL; X-ray; 1.50 A; A=90-110, B=25-54.
DR   PDB; 4CXN; X-ray; 1.70 A; A=90-110, B=25-54.
DR   PDB; 4CY7; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EFX; X-ray; 1.98 A; A/C=90-110, B/D=25-52.
DR   PDB; 4EWW; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EWX; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EWZ; X-ray; 1.79 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EX0; X-ray; 1.86 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EX1; X-ray; 1.66 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EXX; X-ray; 1.55 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EY1; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EY9; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYD; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYN; X-ray; 1.53 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYP; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F0N; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F0O; X-ray; 1.67 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1A; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1B; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1C; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1D; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1G; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F4T; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F4V; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F51; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F8F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4FG3; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 4FKA; X-ray; 1.08 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBC; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBI; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBK; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBL; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBN; X-ray; 1.87 A; A/C=90-110, B/D=25-54.
DR   PDB; 4IUZ; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 4IYD; X-ray; 1.66 A; A=90-109, B=25-53.
DR   PDB; 4IYF; X-ray; 1.80 A; A=90-109, B=25-53.
DR   PDB; 4NIB; X-ray; 1.40 A; A=90-110, B=25-54.
DR   PDB; 4OGA; X-ray; 3.50 A; A=90-110, B=25-54.
DR   PDB; 5AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDBsum; 1A7F; -.
DR   PDBsum; 1AI0; -.
DR   PDBsum; 1AIY; -.
DR   PDBsum; 1B9E; -.
DR   PDBsum; 1BEN; -.
DR   PDBsum; 1EFE; -.
DR   PDBsum; 1EV3; -.
DR   PDBsum; 1EV6; -.
DR   PDBsum; 1EVR; -.
DR   PDBsum; 1FU2; -.
DR   PDBsum; 1FUB; -.
DR   PDBsum; 1G7A; -.
DR   PDBsum; 1G7B; -.
DR   PDBsum; 1GUJ; -.
DR   PDBsum; 1HIQ; -.
DR   PDBsum; 1HIS; -.
DR   PDBsum; 1HIT; -.
DR   PDBsum; 1HLS; -.
DR   PDBsum; 1HTV; -.
DR   PDBsum; 1HUI; -.
DR   PDBsum; 1IOG; -.
DR   PDBsum; 1IOH; -.
DR   PDBsum; 1J73; -.
DR   PDBsum; 1JCA; -.
DR   PDBsum; 1JCO; -.
DR   PDBsum; 1JK8; -.
DR   PDBsum; 1K3M; -.
DR   PDBsum; 1KMF; -.
DR   PDBsum; 1LKQ; -.
DR   PDBsum; 1LPH; -.
DR   PDBsum; 1MHI; -.
DR   PDBsum; 1MHJ; -.
DR   PDBsum; 1MSO; -.
DR   PDBsum; 1OS3; -.
DR   PDBsum; 1OS4; -.
DR   PDBsum; 1Q4V; -.
DR   PDBsum; 1QIY; -.
DR   PDBsum; 1QIZ; -.
DR   PDBsum; 1QJ0; -.
DR   PDBsum; 1RWE; -.
DR   PDBsum; 1SF1; -.
DR   PDBsum; 1SJT; -.
DR   PDBsum; 1SJU; -.
DR   PDBsum; 1T0C; -.
DR   PDBsum; 1T1K; -.
DR   PDBsum; 1T1P; -.
DR   PDBsum; 1T1Q; -.
DR   PDBsum; 1TRZ; -.
DR   PDBsum; 1TYL; -.
DR   PDBsum; 1TYM; -.
DR   PDBsum; 1UZ9; -.
DR   PDBsum; 1VKT; -.
DR   PDBsum; 1W8P; -.
DR   PDBsum; 1XDA; -.
DR   PDBsum; 1XGL; -.
DR   PDBsum; 1XW7; -.
DR   PDBsum; 1ZEG; -.
DR   PDBsum; 1ZEH; -.
DR   PDBsum; 1ZNJ; -.
DR   PDBsum; 2AIY; -.
DR   PDBsum; 2C8Q; -.
DR   PDBsum; 2C8R; -.
DR   PDBsum; 2CEU; -.
DR   PDBsum; 2G54; -.
DR   PDBsum; 2G56; -.
DR   PDBsum; 2H67; -.
DR   PDBsum; 2HH4; -.
DR   PDBsum; 2HHO; -.
DR   PDBsum; 2HIU; -.
DR   PDBsum; 2JMN; -.
DR   PDBsum; 2JUM; -.
DR   PDBsum; 2JUU; -.
DR   PDBsum; 2JUV; -.
DR   PDBsum; 2JV1; -.
DR   PDBsum; 2JZQ; -.
DR   PDBsum; 2K91; -.
DR   PDBsum; 2K9R; -.
DR   PDBsum; 2KJJ; -.
DR   PDBsum; 2KJU; -.
DR   PDBsum; 2KQP; -.
DR   PDBsum; 2KQQ; -.
DR   PDBsum; 2KXK; -.
DR   PDBsum; 2L1Y; -.
DR   PDBsum; 2L1Z; -.
DR   PDBsum; 2LGB; -.
DR   PDBsum; 2LWZ; -.
DR   PDBsum; 2M1D; -.
DR   PDBsum; 2M1E; -.
DR   PDBsum; 2M2M; -.
DR   PDBsum; 2M2N; -.
DR   PDBsum; 2M2O; -.
DR   PDBsum; 2M2P; -.
DR   PDBsum; 2MLI; -.
DR   PDBsum; 2MPG; -.
DR   PDBsum; 2OLY; -.
DR   PDBsum; 2OLZ; -.
DR   PDBsum; 2OM0; -.
DR   PDBsum; 2OM1; -.
DR   PDBsum; 2OMG; -.
DR   PDBsum; 2OMH; -.
DR   PDBsum; 2OMI; -.
DR   PDBsum; 2OMQ; -.
DR   PDBsum; 2QIU; -.
DR   PDBsum; 2R34; -.
DR   PDBsum; 2R35; -.
DR   PDBsum; 2R36; -.
DR   PDBsum; 2RN5; -.
DR   PDBsum; 2VJZ; -.
DR   PDBsum; 2VK0; -.
DR   PDBsum; 2W44; -.
DR   PDBsum; 2WBY; -.
DR   PDBsum; 2WC0; -.
DR   PDBsum; 2WRU; -.
DR   PDBsum; 2WRV; -.
DR   PDBsum; 2WRW; -.
DR   PDBsum; 2WRX; -.
DR   PDBsum; 2WS0; -.
DR   PDBsum; 2WS1; -.
DR   PDBsum; 2WS4; -.
DR   PDBsum; 2WS6; -.
DR   PDBsum; 2WS7; -.
DR   PDBsum; 3AIY; -.
DR   PDBsum; 3BRR; -.
DR   PDBsum; 3BXQ; -.
DR   PDBsum; 3E7Y; -.
DR   PDBsum; 3E7Z; -.
DR   PDBsum; 3EXX; -.
DR   PDBsum; 3FQ9; -.
DR   PDBsum; 3HYD; -.
DR   PDBsum; 3I3Z; -.
DR   PDBsum; 3I40; -.
DR   PDBsum; 3ILG; -.
DR   PDBsum; 3INC; -.
DR   PDBsum; 3IR0; -.
DR   PDBsum; 3JSD; -.
DR   PDBsum; 3KQ6; -.
DR   PDBsum; 3P2X; -.
DR   PDBsum; 3P33; -.
DR   PDBsum; 3Q6E; -.
DR   PDBsum; 3ROV; -.
DR   PDBsum; 3TT8; -.
DR   PDBsum; 3U4N; -.
DR   PDBsum; 3UTQ; -.
DR   PDBsum; 3UTS; -.
DR   PDBsum; 3UTT; -.
DR   PDBsum; 3V19; -.
DR   PDBsum; 3V1G; -.
DR   PDBsum; 3W11; -.
DR   PDBsum; 3W12; -.
DR   PDBsum; 3W13; -.
DR   PDBsum; 3W7Y; -.
DR   PDBsum; 3W7Z; -.
DR   PDBsum; 3W80; -.
DR   PDBsum; 3ZI3; -.
DR   PDBsum; 3ZQR; -.
DR   PDBsum; 3ZS2; -.
DR   PDBsum; 3ZU1; -.
DR   PDBsum; 4AIY; -.
DR   PDBsum; 4AJX; -.
DR   PDBsum; 4AJZ; -.
DR   PDBsum; 4AK0; -.
DR   PDBsum; 4AKJ; -.
DR   PDBsum; 4CXL; -.
DR   PDBsum; 4CXN; -.
DR   PDBsum; 4CY7; -.
DR   PDBsum; 4EFX; -.
DR   PDBsum; 4EWW; -.
DR   PDBsum; 4EWX; -.
DR   PDBsum; 4EWZ; -.
DR   PDBsum; 4EX0; -.
DR   PDBsum; 4EX1; -.
DR   PDBsum; 4EXX; -.
DR   PDBsum; 4EY1; -.
DR   PDBsum; 4EY9; -.
DR   PDBsum; 4EYD; -.
DR   PDBsum; 4EYN; -.
DR   PDBsum; 4EYP; -.
DR   PDBsum; 4F0N; -.
DR   PDBsum; 4F0O; -.
DR   PDBsum; 4F1A; -.
DR   PDBsum; 4F1B; -.
DR   PDBsum; 4F1C; -.
DR   PDBsum; 4F1D; -.
DR   PDBsum; 4F1F; -.
DR   PDBsum; 4F1G; -.
DR   PDBsum; 4F4T; -.
DR   PDBsum; 4F4V; -.
DR   PDBsum; 4F51; -.
DR   PDBsum; 4F8F; -.
DR   PDBsum; 4FG3; -.
DR   PDBsum; 4FKA; -.
DR   PDBsum; 4GBC; -.
DR   PDBsum; 4GBI; -.
DR   PDBsum; 4GBK; -.
DR   PDBsum; 4GBL; -.
DR   PDBsum; 4GBN; -.
DR   PDBsum; 4IUZ; -.
DR   PDBsum; 4IYD; -.
DR   PDBsum; 4IYF; -.
DR   PDBsum; 4NIB; -.
DR   PDBsum; 4OGA; -.
DR   PDBsum; 5AIY; -.
DR   ProteinModelPortal; P01308; -.
DR   SMR; P01308; 25-110.
DR   BioGrid; 109842; 10.
DR   DIP; DIP-6024N; -.
DR   IntAct; P01308; 3.
DR   MINT; MINT-106847; -.
DR   STRING; 9606.ENSP00000348986; -.
DR   ChEMBL; CHEMBL5881; -.
DR   Allergome; 2121; Hom s Insulin.
DR   PhosphoSite; P01308; -.
DR   DMDM; 124617; -.
DR   PaxDb; P01308; -.
DR   PeptideAtlas; P01308; -.
DR   PRIDE; P01308; -.
DR   DNASU; 3630; -.
DR   Ensembl; ENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
DR   Ensembl; ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
DR   Ensembl; ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
DR   GeneID; 3630; -.
DR   KEGG; hsa:3630; -.
DR   UCSC; uc001lvn.2; human. [P01308-1]
DR   CTD; 3630; -.
DR   GeneCards; GC11M002181; -.
DR   GeneReviews; INS; -.
DR   HGNC; HGNC:6081; INS.
DR   HPA; CAB000048; -.
DR   HPA; CAB012098; -.
DR   HPA; CAB053843; -.
DR   HPA; HPA004932; -.
DR   MIM; 125852; phenotype.
DR   MIM; 176730; gene+phenotype.
DR   MIM; 606176; phenotype.
DR   MIM; 613370; phenotype.
DR   neXtProt; NX_P01308; -.
DR   Orphanet; 552; MODY syndrome.
DR   Orphanet; 99885; Permanent neonatal diabetes mellitus.
DR   PharmGKB; PA201; -.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01308; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   PhylomeDB; P01308; -.
DR   TreeFam; TF332820; -.
DR   BioCyc; MetaCyc:MONOMER-16190; -.
DR   Reactome; REACT_1109; Insulin receptor recycling.
DR   Reactome; REACT_13819; Regulation of gene expression in beta cells.
DR   Reactome; REACT_15550; Insulin processing.
DR   Reactome; REACT_1661; SHC activation.
DR   Reactome; REACT_18325; Regulation of insulin secretion.
DR   Reactome; REACT_19189; Synthesis, secretion, and deacylation of Ghrelin.
DR   Reactome; REACT_498; Signaling by Insulin receptor.
DR   Reactome; REACT_508; Signal attenuation.
DR   Reactome; REACT_570; IRS activation.
DR   SignaLink; P01308; -.
DR   EvolutionaryTrace; P01308; -.
DR   GeneWiki; Insulin; -.
DR   GenomeRNAi; 3630; -.
DR   NextBio; 14203; -.
DR   PMAP-CutDB; P01308; -.
DR   PRO; PR:P01308; -.
DR   Bgee; P01308; -.
DR   ExpressionAtlas; P01308; baseline.
DR   Genevestigator; P01308; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
DR   GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IDA:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IC:UniProtKB.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
DR   GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR   GO; GO:0055089; P:fatty acid homeostasis; IMP:BHF-UCL.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IDA:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IDA:DFLAT.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; NAS:BHF-UCL.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IMP:BHF-UCL.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; NAS:BHF-UCL.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IDA:BHF-UCL.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; NAS:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IDA:UniProtKB.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0045908; P:negative regulation of vasodilation; NAS:UniProtKB.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; TAS:BHF-UCL.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; NAS:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; NAS:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IDA:BHF-UCL.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IDA:BHF-UCL.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; NAS:BHF-UCL.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0045840; P:positive regulation of mitosis; IDA:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; NAS:UniProtKB.
DR   GO; GO:0090277; P:positive regulation of peptide hormone secretion; TAS:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:BHF-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IDA:BHF-UCL.
DR   GO; GO:0045909; P:positive regulation of vasodilation; NAS:UniProtKB.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR   GO; GO:0050708; P:regulation of protein secretion; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Diabetes mellitus; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Glucose metabolism; Hormone; Pharmaceutical;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:14426955}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015819.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015820.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015821.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100       {ECO:0000269|PubMed:5101771}.
FT   VARIANT       6      6       R -> C (in MODY10; dbSNP:rs121908278).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063721.
FT   VARIANT       6      6       R -> H (in MODY10; dbSNP:rs121908259).
FT                                {ECO:0000269|PubMed:20226046}.
FT                                /FTId=VAR_063722.
FT   VARIANT      24     24       A -> D (in PNDM; dbSNP:rs80356663).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063723.
FT   VARIANT      29     29       H -> D (in PNDM; dbSNP:rs121908272).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063724.
FT   VARIANT      32     32       G -> R (in PNDM; dbSNP:rs80356664).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063725.
FT   VARIANT      32     32       G -> S (in PNDM; dbSNP:rs80356664).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063726.
FT   VARIANT      34     34       H -> D (in FHPRI; Providence).
FT                                {ECO:0000269|PubMed:3470784}.
FT                                /FTId=VAR_003971.
FT   VARIANT      35     35       L -> P (in PNDM; dbSNP:rs121908273).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063727.
FT   VARIANT      43     43       C -> G (in PNDM; dbSNP:rs80356666).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063728.
FT   VARIANT      46     46       R -> Q (in MODY10; dbSNP:rs121908260).
FT                                {ECO:0000269|PubMed:18192540,
FT                                ECO:0000269|PubMed:20226046}.
FT                                /FTId=VAR_063729.
FT   VARIANT      47     47       G -> V (in PNDM; dbSNP:rs80356667).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063730.
FT   VARIANT      48     48       F -> C (in PNDM; dbSNP:rs80356668).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063731.
FT   VARIANT      48     48       F -> S (associated with diabetes mellitus
FT                                type-II; Los-Angeles).
FT                                {ECO:0000269|PubMed:6312455,
FT                                ECO:0000269|PubMed:6424111}.
FT                                /FTId=VAR_003972.
FT   VARIANT      49     49       F -> L (in Chicago).
FT                                {ECO:0000269|PubMed:6424111}.
FT                                /FTId=VAR_003973.
FT   VARIANT      55     55       R -> C (in IDDM2; dbSNP:rs121908261).
FT                                {ECO:0000269|PubMed:18192540}.
FT                                /FTId=VAR_063732.
FT   VARIANT      68     68       L -> M (in dbSNP:rs121908279).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063733.
FT   VARIANT      84     84       G -> R (in PNDM; uncertain pathological
FT                                significance; dbSNP:rs121908274).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063734.
FT   VARIANT      89     89       R -> C (in PNDM; dbSNP:rs80356669).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063735.
FT   VARIANT      89     89       R -> H (in FHPRI; impairs
FT                                posttranslational cleavage;
FT                                dbSNP:rs28933985).
FT                                {ECO:0000269|PubMed:2196279,
FT                                ECO:0000269|PubMed:4019786}.
FT                                /FTId=VAR_003974.
FT   VARIANT      89     89       R -> L (in FHPRI; Kyoto).
FT                                {ECO:0000269|PubMed:1601997}.
FT                                /FTId=VAR_003975.
FT   VARIANT      90     90       G -> C (in PNDM; dbSNP:rs80356670).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063736.
FT   VARIANT      92     92       V -> L (in Wakayama).
FT                                {ECO:0000269|PubMed:3537011}.
FT                                /FTId=VAR_003976.
FT   VARIANT      96     96       C -> S (in PNDM; dbSNP:rs80356671).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063737.
FT   VARIANT      96     96       C -> Y (in PNDM; dbSNP:rs80356671).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063738.
FT   VARIANT     101    101       S -> C (in PNDM; dbSNP:rs121908276).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063739.
FT   VARIANT     103    103       Y -> C (in PNDM; dbSNP:rs121908277).
FT                                {ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063740.
FT   VARIANT     108    108       Y -> C (in PNDM; dbSNP:rs80356672).
FT                                {ECO:0000269|PubMed:17855560,
FT                                ECO:0000269|PubMed:18162506}.
FT                                /FTId=VAR_063741.
FT   STRAND       26     29
FT   HELIX        33     43
FT   HELIX        44     46
FT   STRAND       48     50
FT   TURN         59     66
FT   STRAND       74     76
FT   HELIX        79     81
FT   TURN         84     86
FT   HELIX        91     97
FT   STRAND       98    101
FT   HELIX       102    106
FT   TURN        107    109
SQ   SEQUENCE   110 AA;  11981 MW;  C2C3B23B85E520E5 CRC64;
     MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_HYDCO               Reviewed;          59 AA.
AC   P68992; P09536;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 42.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Hydrolagus colliei (Spotted ratfish) (Chimaera colliei).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Chimaeridae; Hydrolagus.
OX   NCBI_TaxID=7873;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3780981; DOI=10.1016/0014-5793(86)81066-3;
RA   Conlon J.M., Dafgard E., Falkmer S., Thim L.;
RT   "The primary structure of ratfish insulin reveals an unusual mode of
RT   proinsulin processing.";
RL   FEBS Lett. 208:445-450(1986).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=2646172; DOI=10.1016/0016-6480(89)90064-6;
RA   Conlon J.M., Goeke R., Andrews P.C., Thim L.;
RT   "Multiple molecular forms of insulin and glucagon-like peptide from
RT   the Pacific ratfish (Hydrolagus colliei).";
RL   Gen. Comp. Endocrinol. 73:136-146(1989).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Due to a substitution of the Arg in position 31 by
CC       an Ile, this insulin B chain is longer than most other B chains
CC       and is processed differently.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S06474; INFI.
DR   ProteinModelPortal; P68992; -.
DR   SMR; P68992; 4-59.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     38       Insulin B chain.
FT                                /FTId=PRO_0000015822.
FT   PEPTIDE      39     59       Insulin A chain.
FT                                /FTId=PRO_0000015823.
FT   DISULFID      7     45       Interchain (between B and A chains).
FT   DISULFID     19     58       Interchain (between B and A chains).
FT   DISULFID     44     49
FT   NON_CONS     38     39       {ECO:0000305}.
SQ   SEQUENCE   59 AA;  6606 MW;  8827A57A9ED6D4AC CRC64;
     VPTQRLCGSH LVDALYFVCG ERGFFYSPKP IRELEPLLGI VEQCCHNTCS LANLEGYCN
//
ID   INS_HYSCR               Reviewed;          51 AA.
AC   P01328;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 77.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Hystrix cristata (North African crested porcupine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Hystricidae; Hystrix.
OX   NCBI_TaxID=10137;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6995860; DOI=10.1038/286822a0;
RA   Horuk R., Blundell T.L., Lazarus N.R., Neville R.W.J., Stone D.,
RA   Wollmer A.;
RT   "A monomeric insulin from the porcupine (Hystrix cristata), an Old
RT   World hystricomorph.";
RL   Nature 286:822-824(1980).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; A01594; INPQ.
DR   ProteinModelPortal; P01328; -.
DR   SMR; P01328; 1-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015824.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015825.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     50       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     36     41       {ECO:0000250}.
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5706 MW;  6C36087CC689161B CRC64;
     FVNQHLCGSH LVEALYLVCG NDGFFYRPKA GIVDQCCTGV CSLYQLQNYC N
//
ID   INS_KATPE               Reviewed;          50 AA.
AC   P01340;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Katsuwonus pelamis (Skipjack tuna) (Bonito).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Katsuwonus.
OX   NCBI_TaxID=8226;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-29.
RX   PubMed=14035061;
RA   Kotaki A.;
RT   "Studies on insulin. V. On the structure of the glycyl chain of bonito
RT   insulin II.";
RL   J. Biochem. 53:61-70(1963).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-50.
RX   PubMed=14036898;
RA   Kotaki A.;
RT   "Studies on insulin. III. On the structure of the alanyl chain of
RT   bonito insulin.";
RL   J. Biochem. 51:301-309(1962).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01607; INBN2.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                {ECO:0000269|PubMed:14036898}.
FT                                /FTId=PRO_0000015826.
FT   PEPTIDE      30     50       Insulin A chain.
FT                                /FTId=PRO_0000015827.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     49       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     35     40       {ECO:0000250}.
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   50 AA;  5698 MW;  3627578FE24CE92E CRC64;
     AANPHLCGSH LVEALYLVCG ERGFFYQPKG IHZZCCHKPC BIFZLZBYCN
//
ID   INS_LAMFL               Reviewed;          57 AA.
AC   P68988; P14806; Q9PRR1; Q9PRR2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 41.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Lampetra fluviatilis (European river lamprey) (Petromyzon
OS   fluviatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Lampetra.
OX   NCBI_TaxID=7748;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=8575665; DOI=10.1006/gcen.1995.1138;
RA   Conlon J.M., Bondareva V., Rusakov Y., Plisetskaya E.M.,
RA   Mynarcik D.C., Whittaker J.;
RT   "Characterization of insulin, glucagon, and somatostatin from the
RT   river lamprey, Lampetra fluviatilis.";
RL   Gen. Comp. Endocrinol. 100:96-105(1995).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P68988; -.
DR   SMR; P68988; 10-57.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     36       Insulin B chain.
FT                                /FTId=PRO_0000015828.
FT   PEPTIDE      37     57       Insulin A chain.
FT                                /FTId=PRO_0000015829.
FT   DISULFID     12     43       Interchain (between B and A chains).
FT   DISULFID     24     56       Interchain (between B and A chains).
FT   DISULFID     42     47
FT   NON_CONS     36     37       {ECO:0000305}.
SQ   SEQUENCE   57 AA;  6207 MW;  64029669D2CDB337 CRC64;
     SALTGAGGTH LCGSHLVEAL YVVCGDRGFF YTPSKTGIVE QCCHRKCSIY DMENYCN
//
ID   INS_LOPAM               Reviewed;         116 AA.
AC   P69045; P01341;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 44.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Lophius americanus (American goosefish) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7001633; DOI=10.1126/science.7001633;
RA   Hobart P.M., Shen L.-P., Crawford R., Pictet R.L., Rutter W.J.;
RT   "Comparison of the nucleic acid sequence of anglerfish and mammalian
RT   insulin mRNA's from cloned cDNA's.";
RL   Science 210:1360-1363(1980).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; V00634; CAA23907.1; -; mRNA.
DR   PIR; A01608; IPAF.
DR   ProteinModelPortal; P69045; -.
DR   SMR; P69045; 29-54.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 2.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     53       Insulin B chain.
FT                                /FTId=PRO_0000015832.
FT   PROPEP       56     93       C peptide.
FT                                /FTId=PRO_0000015833.
FT   PEPTIDE      96    116       Insulin A chain.
FT                                /FTId=PRO_0000015834.
FT   DISULFID     32    102       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     44    115       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID    101    106       {ECO:0000250}.
SQ   SEQUENCE   116 AA;  12737 MW;  C686F8EF8183BEFE CRC64;
     MAALWLQSFS LLVLLVVSWP GSQAVAPAQH LCGSHLVDAL YLVCGDRGFF YNPKRDVDQL
     LGFLPPKSGG AAAAGADNEV AEFAFKDQME MMVKRGIVEQ CCHRPCNIFD LQNYCN
//
ID   INS_LOPPI               Reviewed;          51 AA.
AC   P69046; P01341;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 42.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Lophius piscatorius (Allmouth goosefish) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8074;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5389298;
RA   Neumann P.A., Koldenhof M., Humbel R.E.;
RT   "Amino acid sequence of insulin from the angler fish (Lophius
RT   piscatorius).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 350:1286-1288(1969).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A91644; INAFP.
DR   ProteinModelPortal; P69046; -.
DR   SMR; P69046; 5-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015835.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015836.
FT   DISULFID      8     37       Interchain (between B and A chains).
FT   DISULFID     20     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5744 MW;  CE7B12D5D493604E CRC64;
     VAPAQHLCGS HLVDALYLVC GDRGFFYNPK GIVEQCCHRP CNIFDLQNYC N
//
ID   INS_MACFA               Reviewed;         110 AA.
AC   P30406; P01309;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   29-OCT-2014, entry version 74.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6184262; DOI=10.1016/0378-1119(82)90004-X;
RA   Wetekam W., Groneberg J., Leineweber M., Wengenmayer F.,
RA   Winnacker E.-L.;
RT   "The nucleotide sequence of cDNA coding for preproinsulin from the
RT   primate Macaca fascicularis.";
RL   Gene 19:179-183(1982).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; J00336; AAA36849.1; -; mRNA.
DR   PIR; JQ0178; JQ0178.
DR   RefSeq; NP_001271848.1; NM_001284919.1.
DR   UniGene; Mfa.5396; -.
DR   ProteinModelPortal; P30406; -.
DR   SMR; P30406; 25-110.
DR   GeneID; 102133184; -.
DR   KEGG; mcf:102133184; -.
DR   CTD; 3630; -.
DR   HOVERGEN; HBG006137; -.
DR   KO; K04526; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015837.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015838.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015839.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  11991 MW;  83C6E33A80A420F9 CRC64;
     MALWMRLLPL LALLALWGPD PAPAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     PQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_MELGA               Reviewed;          51 AA.
AC   P67968; P01332;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-OCT-2014, entry version 47.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Meleagris gallopavo (Common turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5066110;
RA   Jentsch J.;
RT   "Structure and increased activity of insulin from the turkey
RT   (Meleagris gallopavo).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 353:980-986(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P67968; -.
DR   SMR; P67968; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P67968; -.
DR   NextBio; 20816202; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Reference proteome;
KW   Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015840.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015841.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5698 MW;  976EFAE8987D40DD CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKA GIVEQCCHNT CSLYQLENYC N
//
ID   INS_MYOCO               Reviewed;          51 AA.
AC   P01330;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 74.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Myocastor coypus (Coypu) (Nutria).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Myocastoridae; Myocastor.
OX   NCBI_TaxID=10157;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Smith L.F.;
RT   "Amino acid sequences of insulins.";
RL   Diabetes 21 Suppl. 2:457-460(1972).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=3541911;
RA   Bajaj M., Blundell T.L., Horuk R., Pitts J.E., Wood S.P., Gowan L.K.,
RA   Schwabe C., Wollmer A., Gliemann J., Gammeltoft S.;
RT   "Coypu insulin. Primary structure, conformation and biological
RT   properties of a hystricomorph rodent insulin.";
RL   Biochem. J. 238:345-351(1986).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01596; INCU.
DR   ProteinModelPortal; P01330; -.
DR   SMR; P01330; 1-50.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                /FTId=PRO_0000015848.
FT   PEPTIDE      30     51       Insulin A chain.
FT                                /FTId=PRO_0000015849.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT   DISULFID     19     49       Interchain (between B and A chains).
FT   DISULFID     35     40
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5897 MW;  0812CFD83BAD3ACF CRC64;
     YVSQRLCGSQ LVDTLYSVCR HRGFYRPNDG IVDQCCTNIC SRNQLMSYCN D
//
ID   INS_MYOSC               Reviewed;          50 AA.
AC   P07453;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Myoxocephalus scorpius (Shorthorn sculpin) (Cottus scorpius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Cottales; Cottidae;
OC   Myoxocephalus.
OX   NCBI_TaxID=8097;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3525155; DOI=10.1111/j.1432-1033.1986.tb09728.x;
RA   Cutfield J.F., Cutfield S.M., Carne A., Emdin S.O., Falkmer S.;
RT   "The isolation, purification and amino-acid sequence of insulin from
RT   the teleost fish Cottus scorpius (daddy sculpin).";
RL   Eur. J. Biochem. 158:117-123(1986).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   PIR; A25061; INFIS.
DR   ProteinModelPortal; P07453; -.
DR   SMR; P07453; 4-50.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                {ECO:0000269|PubMed:3525155}.
FT                                /FTId=PRO_0000015850.
FT   PEPTIDE      30     50       Insulin A chain.
FT                                {ECO:0000269|PubMed:3525155}.
FT                                /FTId=PRO_0000015851.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT   DISULFID     19     49       Interchain (between B and A chains).
FT   DISULFID     35     40
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   50 AA;  5683 MW;  0A600B9EBFE15827 CRC64;
     ADPQHLCGSH LVDALYLVCG DRGFFYNPKG IVEQCCHRPC NIRVLENYCN
//
ID   INS_MYXGL               Reviewed;         115 AA.
AC   P01342;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 85.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Myxine glutinosa (Atlantic hagfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperotreti; Myxiniformes; Myxinidae; Myxininae; Myxine.
OX   NCBI_TaxID=7769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6265453;
RA   Chan S.J., Emdin S.O., Kwok S.C.M., Kramer J.M., Falkmer S.,
RA   Steiner D.F.;
RT   "Messenger RNA sequence and primary structure of preproinsulin in a
RT   primitive vertebrate, the Atlantic hagfish.";
RL   J. Biol. Chem. 256:7595-7602(1981).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-57 AND 95-115.
RX   PubMed=1097441;
RA   Peterson J.D., Steiner D.F., Emdin S.O., Falkmer S.;
RT   "The amino acid sequence of the insulin from a primitive vertebrate,
RT   the atlantic hagfish (Myxine glutinosa).";
RL   J. Biol. Chem. 250:5183-5191(1975).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 AND 6.0 ANGSTROMS).
RX   PubMed=4418746; DOI=10.1038/251239a0;
RA   Peterson J.D., Coulter C.L., Steiner D.F., Emdin S.O., Falkmer S.;
RT   "Structural and crystallographic observations on hagfish insulin.";
RL   Nature 251:239-240(1974).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX   PubMed=4427361; DOI=10.1016/0022-2836(74)90557-9;
RA   Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Sabesan M.N.;
RT   "Low resolution crystal structure of hagfish insulin.";
RL   J. Mol. Biol. 87:23-30(1974).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; V00649; CAA23993.1; -; mRNA.
DR   PIR; A01609; IPHF.
DR   ProteinModelPortal; P01342; -.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 2.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     26       {ECO:0000269|PubMed:1097441}.
FT   PEPTIDE      27     57       Insulin B chain.
FT                                {ECO:0000269|PubMed:1097441}.
FT                                /FTId=PRO_0000015852.
FT   PROPEP       60     92       C peptide.
FT                                /FTId=PRO_0000015853.
FT   PEPTIDE      95    115       Insulin A chain.
FT                                {ECO:0000269|PubMed:1097441}.
FT                                /FTId=PRO_0000015854.
FT   DISULFID     33    101       Interchain (between B and A chains).
FT   DISULFID     45    114       Interchain (between B and A chains).
FT   DISULFID    100    105
FT   CONFLICT    109    109       D -> N (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    111    111       E -> Q (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   115 AA;  12615 MW;  C6E3352B0C27581A CRC64;
     MALSPFLAAV IPLVLLLSRA PPSADTRTTG HLCGKDLVNA LYIACGVRGF FYDPTKMKRD
     TGALAAFLPL AYAEDNESQD DESIGINEVL KSKRGIVEQC CHKRCSIYDL ENYCN
//
ID   INS_OCTDE               Reviewed;         109 AA.
AC   P17715;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   29-OCT-2014, entry version 81.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Octodon degus (Degu) (Sciurus degus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Octodontidae; Octodon.
OX   NCBI_TaxID=10160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2293024; DOI=10.1210/mend-4-8-1192;
RA   Nishi M., Steiner D.F.;
RT   "Cloning of complementary DNAs encoding islet amyloid polypeptide,
RT   insulin, and glucagon precursors from a New World rodent, the degu,
RT   Octodon degus.";
RL   Mol. Endocrinol. 4:1192-1198(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-53 AND 87-109.
RX   PubMed=2192710; DOI=10.1016/0006-291X(90)90369-X;
RA   Hellman U., Wernstedt C., Westermark P., O'Brien T.D., Rathbun W.B.,
RA   Johnson K.H.;
RT   "Amino acid sequence from degu islet amyloid-derived insulin shows
RT   unique sequence characteristics.";
RL   Biochem. Biophys. Res. Commun. 169:571-577(1990).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; M57671; AAA40590.1; -; mRNA.
DR   PIR; B36118; IPRTDU.
DR   RefSeq; XP_004627141.1; XM_004627084.1.
DR   ProteinModelPortal; P17715; -.
DR   GeneID; 101571541; -.
DR   CTD; 3630; -.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:2192710}.
FT   PEPTIDE      25     53       Insulin B chain.
FT                                {ECO:0000269|PubMed:2192710}.
FT                                /FTId=PRO_0000015855.
FT   PROPEP       56     84       C peptide.
FT                                /FTId=PRO_0000015856.
FT   PEPTIDE      87    109       Insulin A chain.
FT                                {ECO:0000269|PubMed:2192710}.
FT                                /FTId=PRO_0000015857.
FT   DISULFID     31     93       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    106       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     92     97       {ECO:0000250}.
SQ   SEQUENCE   109 AA;  12197 MW;  845CCE631A9A54D7 CRC64;
     MAPWMHLLTV LALLALWGPN SVQAYSSQHL CGSNLVEALY MTCGRSGFYR PHDRRELEDL
     QVEQAELGLE AGGLQPSALE MILQKRGIVD QCCNNICTFN QLQNYCNVP
//
ID   INS_ONCGO               Reviewed;          50 AA.
AC   P68989; P23187;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 45.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Oncorhynchus gorbuscha (Pink salmon) (Salmo gorbuscha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8017;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Rusakov Y.I., Karasev V.S., Pertseva M.N., Pankov Y.A.;
RT   "Amino acid sequence of humpback salmon (Oncorhynchus gorbuscha)
RT   insulin.";
RL   Biokhimiia 52:247-254(1987).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=2184990;
RA   Rusakov Y.I., Karasev V.S., Bondareva V.M., Pertseva M.N.,
RA   Pankov Y.A.;
RT   "Isolation, primary structure, and biological and immunological
RT   properties of pink and chum salmon insulins.";
RL   Comp. Biochem. Physiol. 95B:477-482(1990).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   PIR; S02203; INON.
DR   ProteinModelPortal; P68989; -.
DR   SMR; P68989; 4-50.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                /FTId=PRO_0000015861.
FT   PEPTIDE      30     50       Insulin A chain.
FT                                /FTId=PRO_0000015862.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     49       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     35     40       {ECO:0000250}.
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   50 AA;  5576 MW;  D3D01633158CD95F CRC64;
     AAAQHLCGSH LVDALYLVCG EKGFFYNPKG IVEQCCHKPC NIFDLQNYCN
//
ID   INS_ONCKE               Reviewed;         105 AA.
AC   P04667; Q91477; Q91478; Q91479;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   29-OCT-2014, entry version 87.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Sperm;
RX   PubMed=2757686; DOI=10.1093/nar/17.4.1758;
RA   Koval A.P., Petrenko A.I., Kavsan V.M.;
RT   "Sequence of the salmon (Oncorhynchus keta) preproinsulin gene.";
RL   Nucleic Acids Res. 17:1758-1758(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sorokin A.V., Skoblov Y.S., Mironov A.A., Zlochevskii M.L.,
RA   Dem'Yanova N.G., Rebentish B.A., Kozlov Y.I., Kavsan V.M., Sova V.V.,
RA   Debabov V.G.;
RT   "Nucleotide sequence of cloned insulin cDNA of Oncorhyncus keta.";
RL   Dokl. Biochem. 269:80-83(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6897724; DOI=10.1016/0378-1119(82)90205-0;
RA   Sorokin A.V., Petrenko A.I., Kavsan V.M., Kozlov Y.I., Debabov V.G.,
RA   Zlochevskii M.L.;
RT   "Nucleotide sequence analysis of the cloned salmon preproinsulin
RT   cDNA.";
RL   Gene 20:367-376(1982).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 26-51.
RX   AGRICOLA=IND81114320;
RA   Dem'Yanova N.G., Zlochevskii M.L., Kavsan V.M., Kozlov Y.I.,
RA   Petrenko A.I., Polyakova N.E., Prokopenko I.V., Rebentish B.A.,
RA   Ryndich A.V., Skoblov Y.S., Sova V.V., Yurin V.L., Yankovskii N.K.,
RA   Debabov V.G.;
RT   "Cloning of the insulin gene of a fish (Oncorhynchus keta) in
RT   Escherichia coli.";
RL   Dokl. Biochem. 256:35-38(1981).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-50 AND 85-105.
RX   PubMed=3314270;
RA   Rusakov Y.I., Karasev V.S., Pertseva M.N., Pankov Y.A.;
RT   "Amino acid sequence of the insulin of the dog salmon Oncorhynchus
RT   keta.";
RL   Zh. Evol. Biokhim. Fiziol. 23:473-480(1987).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X00148; CAA24983.1; ALT_SEQ; mRNA.
DR   EMBL; J00936; AAA49414.1; ALT_SEQ; mRNA.
DR   EMBL; K01655; AAA49417.1; -; mRNA.
DR   EMBL; X13559; CAA31910.1; -; Genomic_DNA.
DR   PIR; S02722; IPON.
DR   ProteinModelPortal; P04667; -.
DR   SMR; P04667; 26-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:3314270}.
FT   PEPTIDE      23     50       Insulin B chain.
FT                                /FTId=PRO_0000015858.
FT   PROPEP       53     82       C peptide.
FT                                /FTId=PRO_0000015859.
FT   PEPTIDE      85    105       Insulin A chain.
FT                                {ECO:0000269|PubMed:6897724}.
FT                                /FTId=PRO_0000015860.
FT   DISULFID     29     91       Interchain (between B and A chains).
FT   DISULFID     41    104       Interchain (between B and A chains).
FT   DISULFID     90     95
FT   CONFLICT     27     27       Missing (in Ref. 4). {ECO:0000305}.
FT   CONFLICT     49     49       T -> N (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
SQ   SEQUENCE   105 AA;  11714 MW;  A928FDD5CFFDA7A6 CRC64;
     MAFWLQAASL LVLLALSPGV DAAAAQHLCG SHLVDALYLV CGEKGFFYTP KRDVDPLIGF
     LSPKSAKENE EYPFKDQTEM MVKRGIVEQC CHKPCNIFDL QNYCN
//
ID   INS_ONCKI               Reviewed;          50 AA.
AC   P68990; P23187;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 45.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8019;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3898237; DOI=10.1016/0167-0115(85)90071-0;
RA   Plisetskaya E., Pollock H.G., Rouse J.B., Hamilton J.W., Kimmel J.R.,
RA   Gorbman A.;
RT   "Characterization of coho salmon (Oncorhynchus kisutch) insulin.";
RL   Regul. Pept. 11:105-116(1985).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A60322; INONC.
DR   ProteinModelPortal; P68990; -.
DR   SMR; P68990; 4-50.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                /FTId=PRO_0000015863.
FT   PEPTIDE      30     50       Insulin A chain.
FT                                /FTId=PRO_0000015864.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     49       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     35     40       {ECO:0000250}.
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   50 AA;  5576 MW;  D3D01633158CD95F CRC64;
     AAAQHLCGSH LVDALYLVCG EKGFFYNPKG IVEQCCHKPC NIFDLQNYCN
//
ID   INS_ORENI               Reviewed;         113 AA.
AC   P81025; Q9W653;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   29-OCT-2014, entry version 71.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9972302; DOI=10.1016/S0305-0491(98)10102-5;
RA   Mansour M., Wright J.R. Jr., Pohajdak B.;
RT   "Cloning, sequencing and characterization of the tilapia insulin
RT   gene.";
RL   Comp. Biochem. Physiol. 121B:291-297(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 93-113.
RX   PubMed=7656183;
RA   Nguyen T.M., Wright J.R. Jr., Nielsen P.F., Conlon J.M.;
RT   "Characterization of the pancreatic hormones from the Brockmann body
RT   of the tilapia: implications for islet xenograft studies.";
RL   Comp. Biochem. Physiol. 111C:33-44(1995).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF038123; AAD22742.1; -; Genomic_DNA.
DR   ProteinModelPortal; P81025; -.
DR   SMR; P81025; 29-54.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P81025; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:7656183}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015865.
FT   PROPEP       56     90       C peptide.
FT                                /FTId=PRO_0000015866.
FT   PEPTIDE      93    113       Insulin A chain.
FT                                /FTId=PRO_0000015867.
FT   DISULFID     32     99       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     44    112       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     98    103       {ECO:0000250}.
SQ   SEQUENCE   113 AA;  12480 MW;  C4719D5FC8920D3C CRC64;
     MAALWLQAFS LLVLMMVSWP GSQAVGGPQH LCGSHLVDAL YLVCGDRGFF YNPRRDVDPL
     LGFLPPKAGG AVVQGGENEV TFKDQMEMMV KRGIVEECCH KPCTIFDLQN YCN
//
ID   INS_ORNAN               Reviewed;          51 AA.
AC   Q9TQY7; Q9TQY8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   29-OCT-2014, entry version 60.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=8868070; DOI=10.1515/bchm3.1996.377.2.147;
RA   Nourse A., Treacy G.B., Shaw D.C., Jeffrey P.D.;
RT   "Platypus insulin: indications from the amino acid sequence of
RT   significant differences in structure from porcine insulin.";
RL   Biol. Chem. Hoppe-Seyler 377:147-153(1996).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S63591; S63590.
DR   ProteinModelPortal; Q9TQY7; -.
DR   SMR; Q9TQY7; 1-51.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; Q9TQY7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Reference proteome;
KW   Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015868.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015869.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5854 MW;  0E4D30265D77EAA3 CRC64;
     FPNQHLCGSH LVEALYLVCG EKGFYYIPRM GIVEECCKGV CSMYQLENYC N
//
ID   INS_PANBU               Reviewed;         110 AA.
AC   Q98TA8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   29-OCT-2014, entry version 54.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Pantodon buchholzi (Freshwater butterflyfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Pantodontidae; Pantodon.
OX   NCBI_TaxID=8276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11306171; DOI=10.1016/S0303-7207(00)00449-4;
RA   Al-Mahrouki A.A., Irwin D.M., Graham L.C., Youson J.H.;
RT   "Molecular cloning of preproinsulin cDNAs from several
RT   osteoglossomorphs and a cyprinid.";
RL   Mol. Cell. Endocrinol. 174:51-58(2001).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF199588; AAK28712.1; -; mRNA.
DR   ProteinModelPortal; Q98TA8; -.
DR   SMR; Q98TA8; 26-53.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   PEPTIDE      24     53       Insulin B chain.
FT                                /FTId=PRO_0000042212.
FT   PROPEP       56     87       C peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000042213.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000042214.
FT   DISULFID     30     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     42    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  12324 MW;  BDECCD659D872E06 CRC64;
     MALWLQAFTL LVLLVLSSPG AQSASSQHLC GSHLVDALYM VCGEKGFFYQ PKTKRDVDPL
     LGFLSPKSAQ ENEADEYPYK DQGDLKVKRG IVEQCCHHPC NIFDLQNYCN
//
ID   INS_PANTR               Reviewed;         110 AA.
AC   P30410;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   29-OCT-2014, entry version 103.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1560757;
RA   Seino S., Bell G.I., Li W.;
RT   "Sequences of primate insulin genes support the hypothesis of a slower
RT   rate of molecular evolution in humans and apes than in monkeys.";
RL   Mol. Biol. Evol. 9:193-203(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X61089; CAA43403.1; -; Genomic_DNA.
DR   EMBL; AY137497; AAN06933.1; -; Genomic_DNA.
DR   PIR; A42179; A42179.
DR   RefSeq; NP_001008996.1; NM_001008996.2.
DR   UniGene; Ptr.6479; -.
DR   PDB; 1BZV; NMR; -; B=25-49.
DR   PDBsum; 1BZV; -.
DR   ProteinModelPortal; P30410; -.
DR   SMR; P30410; 25-110.
DR   STRING; 9598.ENSPTRP00000057962; -.
DR   Ensembl; ENSPTRT00000006075; ENSPTRP00000005606; ENSPTRG00000003172.
DR   GeneID; 449570; -.
DR   KEGG; ptr:449570; -.
DR   CTD; 3630; -.
DR   eggNOG; NOG45999; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P30410; -.
DR   KO; K04526; -.
DR   OMA; HAKAIHA; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   TreeFam; TF332820; -.
DR   EvolutionaryTrace; P30410; -.
DR   NextBio; 20832685; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015870.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015871.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015872.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
FT   HELIX        33     43
FT   STRAND       44     46
SQ   SEQUENCE   110 AA;  12025 MW;  41EB8DF79837CEF5 CRC64;
     MALWMRLLPL LVLLALWGPD PASAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_PETMA               Reviewed;          57 AA.
AC   P68987; P14806; Q9PRR1; Q9PRR2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 45.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3282977; DOI=10.1016/0016-6480(88)90051-2;
RA   Plisetskaya E.M., Pollock H.G., Elliott W.M., Youson J.H.,
RA   Andrews P.C.;
RT   "Isolation and structure of lamprey (Petromyzon marinus) insulin.";
RL   Gen. Comp. Endocrinol. 69:46-55(1988).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S06338; INLMS.
DR   ProteinModelPortal; P68987; -.
DR   SMR; P68987; 10-57.
DR   Ensembl; ENSPMAT00000009915; ENSPMAP00000009873; ENSPMAG00000008971.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOVERGEN; HBG006137; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     36       Insulin B chain.
FT                                /FTId=PRO_0000015873.
FT   PEPTIDE      37     57       Insulin A chain.
FT                                /FTId=PRO_0000015874.
FT   DISULFID     12     43       Interchain (between B and A chains).
FT   DISULFID     24     56       Interchain (between B and A chains).
FT   DISULFID     42     47
FT   NON_CONS     36     37       {ECO:0000305}.
SQ   SEQUENCE   57 AA;  6207 MW;  64029669D2CDB337 CRC64;
     SALTGAGGTH LCGSHLVEAL YVVCGDRGFF YTPSKTGIVE QCCHRKCSIY DMENYCN
//
ID   INS_PIAME               Reviewed;          52 AA.
AC   P81881;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   29-OCT-2014, entry version 65.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Piaractus mesopotamicus (Pacu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Piaractus.
OX   NCBI_TaxID=42528;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=10327603; DOI=10.1016/S0305-0491(98)10164-5;
RA   de Lima J.A., Oliveira B., Conlon J.M.;
RT   "Purification and characterization of insulin and peptides derived
RT   from proglucagon and prosomatostatin from the fruit-eating fish, the
RT   pacu Piaractus mesopotamicus.";
RL   Comp. Biochem. Physiol. 122B:127-135(1999).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   ProteinModelPortal; P81881; -.
DR   SMR; P81881; 6-52.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                /FTId=PRO_0000015877.
FT   PEPTIDE      32     52       Insulin A chain.
FT                                /FTId=PRO_0000015878.
FT   DISULFID      9     38       Interchain (between B and A chains).
FT   DISULFID     21     51       Interchain (between B and A chains).
FT   DISULFID     37     42
FT   NON_CONS     31     32       {ECO:0000305}.
SQ   SEQUENCE   52 AA;  5673 MW;  B8A37293739276AE CRC64;
     NAGAPQHLCG SHLVDALYLV CGPSGFFYNP KGIVEQCCHK PCSIFDLQNY CN
//
ID   INS_PHYCD               Reviewed;          51 AA.
AC   P67974; P01312;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 48.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Physeter catodon (Sperm whale) (Physeter macrocephalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
OC   Odontoceti; Physeteridae; Physeter.
OX   NCBI_TaxID=9755;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=13373434; DOI=10.1016/0003-9861(56)90203-X;
RA   Harris J.I., Sanger F., Naughton M.A.;
RT   "Species differences in insulin.";
RL   Arch. Biochem. Biophys. 65:427-438(1956).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=13552701; DOI=10.1038/1811468b0;
RA   Ishihara Y., Saito T., Ito Y., Fujino M.;
RT   "Structure of sperm- and sei-whale insulins and their breakdown by
RT   whale pepsin.";
RL   Nature 181:1468-1469(1958).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; A93142; INWHP.
DR   ProteinModelPortal; P67974; -.
DR   SMR; P67974; 1-30.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015875.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015876.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5766 MW;  9007B514691A7CDD CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCTSI CSLYQLENYC N
//
ID   INS_PIG                 Reviewed;         108 AA.
AC   P01315; Q9TSJ5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   29-OCT-2014, entry version 138.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Han X.G., Tuch B.E.;
RT   "Complete porcine preproinsulin cDNA sequence.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Large white;
RX   PubMed=12140686; DOI=10.1007/s00335-001-3059-x;
RA   Amarger V., Nguyen M., Van Laere A.-S., Braunschweig M., Nezer C.,
RA   Georges M., Andersson L.;
RT   "Comparative sequence analysis of the INS-IGF2-H19 gene cluster in
RT   pigs.";
RL   Mamm. Genome 13:388-398(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=European wild boar, Hampshire, Japanese wild boar, Landrace,
RC   Large white, Meishan, and Pietrain;
RX   PubMed=14574411; DOI=10.1038/nature02064;
RA   Van Laere A.-S., Nguyen M., Braunschweig M., Nezer C., Collette C.,
RA   Moreau L., Archibald A.L., Haley C., Buys N., Tally M., Andersson G.,
RA   Georges M., Andersson L.;
RT   "A regulatory mutation in IGF2 causes a major QTL effect on muscle
RT   growth in the pig.";
RL   Nature 425:832-836(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-108.
RX   PubMed=5657063; DOI=10.1126/science.161.3837.165;
RA   Chance R.E., Ellis R.M., Bromer W.W.;
RT   "Porcine proinsulin: characterization and amino acid sequence.";
RL   Science 161:165-167(1968).
RN   [5]
RP   SEQUENCE REVISION TO 59.
RA   Chance R.E.;
RL   Submitted (JUL-1970) to the PIR data bank.
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RA   Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.;
RT   "Insulin. The structure in the crystal and its reflection in chemistry
RT   and biology.";
RL   Adv. Protein Chem. 26:279-402(1972).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RA   Isaacs N.W., Agarwal R.C.;
RT   "Experience with fast Fourier least squares in the refinement of the
RT   crystal structure of rhombohedral 2-zinc insulin at 1.5-A
RT   resolution.";
RL   Acta Crystallogr. A 34:782-791(1978).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=2905485; DOI=10.1098/rstb.1988.0058;
RA   Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J.,
RA   Dodson G.G., Crowfoot Hodgkin D.M., Hubbard R.E., Isaacs N.W.,
RA   Reynolds C.D., Sakabe K., Sakabe N., Vijayan N.M.;
RT   "The structure of 2Zn pig insulin crystals at 1.5-A resolution.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 319:369-456(1988).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=1772633; DOI=10.1107/S010876819100842X;
RA   Balschmidt P., Hansen F.B., Dodson E., Dodson G., Korber F.;
RT   "Structure of porcine insulin cocrystallized with clupeine Z.";
RL   Acta Crystallogr. B 47:975-986(1991).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=2025410; DOI=10.1107/S0108768190009570;
RA   Badger J., Harris M.R., Reynolds C.D., Evans A.C., Dodson E.J.,
RA   Dodson G.G., North A.C.T.;
RT   "Structure of the pig insulin dimer in the cubic crystal.";
RL   Acta Crystallogr. B 47:127-136(1991).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   PubMed=15299880; DOI=10.1107/S0907444997004034;
RA   Diao J.-S., Wan Z.-L., Chang W.-R., Liang D.-C.;
RT   "Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30)
RT   insulin at 1.65-A resolution.";
RL   Acta Crystallogr. D 53:507-512(1997).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-8437944, EBI-8437944;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC77920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
CC       century - Issue 9 of April 2001;
CC       URL="http://web.expasy.org/spotlight/back_issues/009";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF064555; AAC77920.1; ALT_INIT; mRNA.
DR   EMBL; AY044828; AAL69550.1; -; Genomic_DNA.
DR   EMBL; AY242098; AAQ00952.1; -; Genomic_DNA.
DR   EMBL; AY242099; AAQ00954.1; -; Genomic_DNA.
DR   EMBL; AY242100; AAQ00957.1; -; Genomic_DNA.
DR   EMBL; AY242101; AAQ00960.1; -; Genomic_DNA.
DR   EMBL; AY242102; AAQ00963.1; -; Genomic_DNA.
DR   EMBL; AY242103; AAQ00966.1; -; Genomic_DNA.
DR   EMBL; AY242104; AAQ00969.1; -; Genomic_DNA.
DR   EMBL; AY242105; AAQ00972.1; -; Genomic_DNA.
DR   EMBL; AY242106; AAQ00975.1; -; Genomic_DNA.
DR   EMBL; AY242107; AAQ00978.1; -; Genomic_DNA.
DR   EMBL; AY242108; AAQ00981.1; -; Genomic_DNA.
DR   EMBL; AY242109; AAQ00983.1; -; Genomic_DNA.
DR   EMBL; AY242110; AAQ00985.1; -; Genomic_DNA.
DR   EMBL; AY242111; AAQ00987.1; -; Genomic_DNA.
DR   EMBL; AY242112; AAQ00990.1; -; Genomic_DNA.
DR   PIR; A01583; IPPG.
DR   RefSeq; NP_001103242.1; NM_001109772.1.
DR   UniGene; Ssc.583; -.
DR   PDB; 1B17; X-ray; 1.70 A; A=88-108, B=25-54.
DR   PDB; 1B18; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 1B19; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 1B2A; X-ray; 1.70 A; A=88-108, B=25-54.
DR   PDB; 1B2B; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 1B2C; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 1B2D; X-ray; 1.70 A; A=88-108, B=25-54.
DR   PDB; 1B2E; X-ray; 1.90 A; A=88-108, B=25-54.
DR   PDB; 1B2F; X-ray; 1.90 A; A=88-108, B=25-54.
DR   PDB; 1B2G; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 1DEI; X-ray; 1.60 A; A/C=88-108, B/D=25-47.
DR   PDB; 1IZA; X-ray; 2.50 A; A/C=88-108, B/D=25-53.
DR   PDB; 1IZB; X-ray; 2.00 A; A/C=88-108, B/D=25-53.
DR   PDB; 1M5A; X-ray; 1.20 A; A/C=88-108, B/D=25-54.
DR   PDB; 1MPJ; X-ray; 2.30 A; A/C=88-108, B/D=25-54.
DR   PDB; 1SDB; X-ray; 1.65 A; A=88-108, B=27-49.
DR   PDB; 1WAV; X-ray; 2.50 A; A/C/E/G/I/K=88-108, B/D/F/H/J/L=25-54.
DR   PDB; 1ZEI; X-ray; 1.90 A; A/B/C/D/E/F=25-54, A/B/C/D/E/F=88-108.
DR   PDB; 1ZNI; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR   PDB; 2EFA; Neutron; 2.70 A; A=88-108, B=25-54.
DR   PDB; 2G4M; X-ray; 1.80 A; A=88-108, B=25-54.
DR   PDB; 2TCI; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR   PDB; 2ZPP; Neutron; 2.50 A; A=88-108, B=25-54.
DR   PDB; 3FHP; Neutron; 2.00 A; A/C=88-108, B/D=25-54.
DR   PDB; 3GKY; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR   PDB; 3INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR   PDB; 3MTH; X-ray; 1.90 A; A/C=88-108, B/D=25-54.
DR   PDB; 3RTO; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
DR   PDB; 3T2A; X-ray; 2.10 A; A=88-108, B=25-54.
DR   PDB; 4A7E; X-ray; 1.86 A; A=88-108, B=25-54.
DR   PDB; 4INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
DR   PDB; 6INS; X-ray; 2.00 A; E/F=25-108.
DR   PDB; 7INS; X-ray; 2.00 A; A/C/E=88-108, B/D/F=25-54.
DR   PDB; 9INS; X-ray; 1.70 A; A=88-108, B=25-54.
DR   PDBsum; 1B17; -.
DR   PDBsum; 1B18; -.
DR   PDBsum; 1B19; -.
DR   PDBsum; 1B2A; -.
DR   PDBsum; 1B2B; -.
DR   PDBsum; 1B2C; -.
DR   PDBsum; 1B2D; -.
DR   PDBsum; 1B2E; -.
DR   PDBsum; 1B2F; -.
DR   PDBsum; 1B2G; -.
DR   PDBsum; 1DEI; -.
DR   PDBsum; 1IZA; -.
DR   PDBsum; 1IZB; -.
DR   PDBsum; 1M5A; -.
DR   PDBsum; 1MPJ; -.
DR   PDBsum; 1SDB; -.
DR   PDBsum; 1WAV; -.
DR   PDBsum; 1ZEI; -.
DR   PDBsum; 1ZNI; -.
DR   PDBsum; 2EFA; -.
DR   PDBsum; 2G4M; -.
DR   PDBsum; 2TCI; -.
DR   PDBsum; 2ZPP; -.
DR   PDBsum; 3FHP; -.
DR   PDBsum; 3GKY; -.
DR   PDBsum; 3INS; -.
DR   PDBsum; 3MTH; -.
DR   PDBsum; 3RTO; -.
DR   PDBsum; 3T2A; -.
DR   PDBsum; 4A7E; -.
DR   PDBsum; 4INS; -.
DR   PDBsum; 6INS; -.
DR   PDBsum; 7INS; -.
DR   PDBsum; 9INS; -.
DR   ProteinModelPortal; P01315; -.
DR   SMR; P01315; 25-108.
DR   IntAct; P01315; 1.
DR   MINT; MINT-1505666; -.
DR   Allergome; 2122; Sus s Insulin.
DR   GeneID; 397415; -.
DR   KEGG; ssc:397415; -.
DR   CTD; 3630; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01315; -.
DR   KO; K04526; -.
DR   EvolutionaryTrace; P01315; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism;
KW   Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:5657063}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015879.
FT   PROPEP       57     85       C peptide.
FT                                /FTId=PRO_0000015880.
FT   PEPTIDE      88    108       Insulin A chain.
FT                                /FTId=PRO_0000015881.
FT   DISULFID     31     94       Interchain (between B and A chains).
FT   DISULFID     43    107       Interchain (between B and A chains).
FT   DISULFID     93     98
FT   HELIX        33     43
FT   HELIX        44     46
FT   STRAND       48     50
FT   HELIX        89     95
FT   HELIX       100    103
FT   HELIX       104    106
SQ   SEQUENCE   108 AA;  11672 MW;  CB4491B429858EBE CRC64;
     MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAEN
     PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL YQLENYCN
//
ID   INS_PLAFE               Reviewed;          51 AA.
AC   P09477;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-OCT-2014, entry version 81.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Platichthys flesus (European flounder) (Pleuronectes flesus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Platichthys.
OX   NCBI_TaxID=8260;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3556313; DOI=10.1016/0016-6480(87)90268-1;
RA   Conlon J.M., Davis M.S., Thim L.;
RT   "Primary structure of insulin and glucagon from the flounder
RT   (Platichthys flesus).";
RL   Gen. Comp. Endocrinol. 66:203-209(1987).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S07213; INFLE.
DR   ProteinModelPortal; P09477; -.
DR   SMR; P09477; 5-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015882.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015883.
FT   DISULFID      8     37       Interchain (between B and A chains).
FT   DISULFID     20     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5755 MW;  04A232C873FF705B CRC64;
     VVPPQHLCGA HLVDALYLVC GERGFFYTPK GIVEQCCHKP CNIFDLQNYC N
//
ID   INS_POLSE               Reviewed;          52 AA.
AC   P0C236;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   29-OCT-2014, entry version 29.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Polypterus senegalus (Senegal bichir).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX   NCBI_TaxID=55291;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=9446726; DOI=10.1006/gcen.1997.7007;
RA   Conlon J.M., Fan H.-Y., Fritzsch B.;
RT   "Purification and structural characterization of insulin and glucagon
RT   from the bichir Polypterus senegalis (Actinopterygii:
RT   Polypteriformes).";
RL   Gen. Comp. Endocrinol. 109:86-93(1998).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P0C236; -.
DR   SMR; P0C236; 3-52.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     31       Insulin B chain.
FT                                /FTId=PRO_0000261314.
FT   PEPTIDE      32     52       Insulin A chain.
FT                                /FTId=PRO_0000261315.
FT   DISULFID      7     38       Interchain (between B and A chains).
FT   DISULFID     19     51       Interchain (between B and A chains).
FT   DISULFID     37     42
FT   NON_CONS     31     32       {ECO:0000305}.
SQ   SEQUENCE   52 AA;  5817 MW;  EB7D85400E016B3F CRC64;
     AANRHLCGSH LVEALYLVCG NRGFFYIPSK MGIVEQCCDT PCSLYDPENY CN
//
ID   INS_PONPY               Reviewed;         110 AA.
AC   Q8HXV2;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-OCT-2014, entry version 55.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AY137503; AAN06937.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8HXV2; -.
DR   SMR; Q8HXV2; 25-110.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015884.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015885.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015886.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  12038 MW;  22D2B32B94F520F8 CRC64;
     MALWMRLLPL LALLALWGPD PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_PROGU               Reviewed;          50 AA.
AC   P01331;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 74.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Proechimys guairae (Guaira spiny rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Echimyidae; Proechimys.
OX   NCBI_TaxID=10163;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=16068186; DOI=10.1038/279439a0;
RA   Horuk R., Goodwin P., O'Connor K., Neville R.W.J., Lazarus N.R.,
RA   Stone D.;
RT   "Evolutionary change in the insulin receptors of hystricomorph
RT   rodents.";
RL   Nature 279:439-440(1979).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A01597; INKS.
DR   ProteinModelPortal; P01331; -.
DR   SMR; P01331; 1-50.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     29       Insulin B chain.
FT                                /FTId=PRO_0000015887.
FT   PEPTIDE      30     50       Insulin A chain.
FT                                /FTId=PRO_0000015888.
FT   DISULFID      7     36       Interchain (between B and A chains).
FT   DISULFID     19     49       Interchain (between B and A chains).
FT   DISULFID     35     40
FT   NON_CONS     29     30       {ECO:0000305}.
SQ   SEQUENCE   50 AA;  5707 MW;  BD24AEFFBC8B1961 CRC64;
     YVGQRLCGSQ LVDTLYSVCK HRGFYRPSEG IVDQCCTNIC SRNQLLTYCN
//
ID   INS_PSAOB               Reviewed;         110 AA.
AC   Q62587;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-OCT-2014, entry version 69.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Psammomys obesus (Fat sand rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Gerbillinae; Psammomys.
OX   NCBI_TaxID=48139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=9166665; DOI=10.2337/diab.46.6.953;
RA   Kaiser N., Bailyes E.M., Schneider B.S., Cerasi E., Steiner D.F.,
RA   Hutton J.C., Gross D.J.;
RT   "Characterization of the unusual insulin of Psammomys obesus, a rodent
RT   with nutrition-induced NIDDM-like syndrome.";
RL   Diabetes 46:953-957(1997).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X98241; CAA66897.1; -; mRNA.
DR   ProteinModelPortal; Q62587; -.
DR   SMR; Q62587; 25-110.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015889.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015890.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015891.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  12324 MW;  A006738E20579CB0 CRC64;
     MALWMRLLPL LAFLILWEPS PAHAFVNQHL CGSHLVEALY LVCGERGFFY TPKFRRGVDD
     PQMPQLELGG SPGAGDLRAL ALEVARQKRG IVEQCCTGIC SLYQLENYCN
//
ID   INS_RABIT               Reviewed;         110 AA.
AC   P01311;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-OCT-2014, entry version 99.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Pancreas;
RX   PubMed=8132571;
RA   Devaskar S.U., Giddings S.J., Rajakumar P.A., Carnaghi L.R.,
RA   Menon R.K., Zahm D.S.;
RT   "Insulin gene expression and insulin synthesis in mammalian neuronal
RT   cells.";
RL   J. Biol. Chem. 269:8445-8454(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-110.
RA   Giddings S.J., Carnaghi L.R., Devaskar S.U.;
RL   Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; U03610; AAA19033.1; -; mRNA.
DR   EMBL; M61153; AAA17540.1; -; mRNA.
DR   PIR; A53438; INRB.
DR   RefSeq; NP_001075804.1; NM_001082335.1.
DR   UniGene; Ocu.1810; -.
DR   ProteinModelPortal; P01311; -.
DR   SMR; P01311; 25-110.
DR   GeneID; 100009181; -.
DR   CTD; 3630; -.
DR   eggNOG; NOG45999; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; P01311; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:5949593}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                {ECO:0000269|PubMed:8132571}.
FT                                /FTId=PRO_0000015892.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015893.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                {ECO:0000269|PubMed:8132571}.
FT                                /FTId=PRO_0000015894.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
FT   CONFLICT     83     83       E -> Y (in Ref. 3; AAA17540).
FT                                {ECO:0000305}.
SQ   SEQUENCE   110 AA;  11838 MW;  82D2975B85D77FA8 CRC64;
     MASLAALLPL LALLVLCRLD PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKSRREVEE
     LQVGQAELGG GPGAGGLQPS ALELALQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_PTYDH               Reviewed;          51 AA.
AC   P12708;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Ptyas dhumnades (Big-eyed ratsnake) (Zaocys dhumnades).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Colubridae; Colubrinae; Ptyas.
OX   NCBI_TaxID=8587;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7029709;
RA   Zhang Y.S., Cao Q.-P., Zhang Y.S.;
RT   "The primary structure of snake (Zaocys dhumnades dhumnades, Cantor)
RT   insulin.";
RL   Sci. Sin. 24:1585-1589(1981).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; JQ0359; JQ0359.
DR   ProteinModelPortal; P12708; -.
DR   SMR; P12708; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015935.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015936.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5809 MW;  951C975CF423BA26 CRC64;
     APNQRLCGSH LVEALFLICG ERGFYYSPRT GIVEQCCENT CSLYELENYC N
//
ID   INS_RODSP               Reviewed;         108 AA.
AC   P21563;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   29-OCT-2014, entry version 79.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Rodentia sp.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   unclassified Rodentia.
OX   NCBI_TaxID=69158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2531072;
RA   Robitzki A., Schroeder H.C., Ugarkovic D., Pfeifer K., Uhlenbruck G.,
RA   Mueller W.E.G.;
RT   "Demonstration of an endocrine signaling circuit for insulin in the
RT   sponge Geodia cydonium.";
RL   EMBO J. 8:2905-2909(1989).
RN   [2]
RP   DOUBTS ON VALIDITY OF SEQUENCE.
RA   Bairoch A., Duret L.;
RL   Unpublished observations (FEB-1996).
RN   [3]
RP   AGREEMENT WITH RODENT CONTAMINATION.
RA   Mueller W.E.G.;
RL   Unpublished observations (APR-1996).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Stored in spherulous cells
CC       prior to secretion.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:2531072) thought to originate from
CC       the sponge Geodia cydonium, but, on the basis of phylogenetic
CC       studies (Ref.2) it seems very probable that the DNA sequence
CC       coding for this protein comes from a rodent as agreed by the
CC       original authors (Ref.3). It is also doubtful that this is a real
CC       active insulin. {ECO:0000305|PubMed:2531072}.
CC   -----------------------------------------------------------------------
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DR   ProteinModelPortal; P21563; -.
DR   SMR; P21563; 24-54.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     23
FT   PEPTIDE      24     54       Insulin B chain.
FT                                /FTId=PRO_0000015901.
FT   PROPEP       57     88       C peptide.
FT                                /FTId=PRO_0000015902.
FT   PEPTIDE      90    108       Insulin A chain.
FT                                /FTId=PRO_0000015903.
FT   DISULFID     30     94       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    107       Interchain (between B and A chains).
FT                                {ECO:0000250}.
SQ   SEQUENCE   108 AA;  11849 MW;  BF4B4826D2E30306 CRC64;
     MALWILLPLL ALLILWGPDP AQAFVNQHLC GSHLVEALYI LVCGERGFFY TPMSRREVED
     PQVGQVELGA GPGAGSEQTL ALEVARQARI VQQCTSGICS LYQENYCN
//
ID   INS_SAISC               Reviewed;          51 AA.
AC   P67971; P10604;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-OCT-2014, entry version 45.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Saimiri sciureus (Common squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Saimiriinae; Saimiri.
OX   NCBI_TaxID=9521;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2263627; DOI=10.1073/pnas.87.24.9766;
RA   Yu J.-H., Eng J., Yalow R.S.;
RT   "Isolation and amino acid sequences of squirrel monkey (Saimiri
RT   sciurea) insulin and glucagon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9766-9768(1990).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   ProteinModelPortal; P67971; -.
DR   SMR; P67971; 1-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015904.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015905.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5747 MW;  84572881D72E7D6D CRC64;
     FVNQHLCGPH LVEALYLVCG ERGFFYAPKT GVVDQCCTSI CSLYQLQNYC N
//
ID   INS_SELRF               Reviewed;         103 AA.
AC   P51463;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   29-OCT-2014, entry version 67.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor; Fragment;
GN   Name=INS;
OS   Selasphorus rufus (Rufous hummingbird) (Trochilus rufus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Trochiliformes;
OC   Trochilidae; Selasphorus.
OX   NCBI_TaxID=29060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8405887; DOI=10.1006/gcen.1993.1100;
RA   Fan L., Gardner P., Chan S.J., Steiner D.F.;
RT   "Cloning and analysis of the gene encoding hummingbird proinsulin.";
RL   Gen. Comp. Endocrinol. 91:25-30(1993).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AH006925; AAC64211.1; -; Genomic_DNA.
DR   PIR; I51221; I51221.
DR   ProteinModelPortal; P51463; -.
DR   SMR; P51463; 22-103.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL       <1     20       {ECO:0000250}.
FT   PEPTIDE      21     50       Insulin B chain.
FT                                /FTId=PRO_0000015906.
FT   PROPEP       53     80       C peptide.
FT                                /FTId=PRO_0000015907.
FT   PEPTIDE      83    103       Insulin A chain.
FT                                /FTId=PRO_0000015908.
FT   DISULFID     27     89       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     39    102       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     88     93       {ECO:0000250}.
FT   NON_TER       1      1
SQ   SEQUENCE   103 AA;  11378 MW;  6598520B28F5BB9C CRC64;
     IQSLPLLALL ALSGPGTSHA AVNQHLCGSH LVEALYLVCG ERGFFYSPKA RRDAEHPLVN
     GPLHGEVGDL PFQQEEFEKV KRGIVEQCCH NTCSLYQLEN YCN
//
ID   INS_SHEEP               Reviewed;         105 AA.
AC   P01318;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   29-OCT-2014, entry version 82.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8011164; DOI=10.1089/dna.1994.13.377;
RA   Ohlsen S.M., Lugenbeel K.A., Wong E.A.;
RT   "Characterization of the linked ovine insulin and insulin-like growth
RT   factor-II genes.";
RL   DNA Cell Biol. 13:377-388(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 85-105.
RX   PubMed=13249948;
RA   Brown H., Sanger F., Kitai R.;
RT   "The structure of pig and sheep insulins.";
RL   Biochem. J. 60:556-565(1955).
RN   [3]
RP   PROTEIN SEQUENCE OF 57-82.
RX   PubMed=4626369;
RA   Peterson J.D., Nehrlich S., Oyer P.E., Steiner D.F.;
RT   "Determination of the amino acid sequence of the monkey, sheep, and
RT   dog proinsulin C-peptides by a semi-micro Edman degradation
RT   procedure.";
RL   J. Biol. Chem. 247:4866-4871(1972).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; U00659; AAB60625.1; -; Genomic_DNA.
DR   PIR; S16430; INSH.
DR   ProteinModelPortal; P01318; -.
DR   SMR; P01318; 25-105.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:13249948}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015909.
FT   PROPEP       57     82       C peptide.
FT                                /FTId=PRO_0000015910.
FT   PEPTIDE      85    105       Insulin A chain.
FT                                /FTId=PRO_0000015911.
FT   DISULFID     31     91       Interchain (between B and A chains).
FT   DISULFID     43    104       Interchain (between B and A chains).
FT   DISULFID     90     95
SQ   SEQUENCE   105 AA;  11235 MW;  8B27C7FB9922BC7A CRC64;
     MALWTRLVPL LALLALWAPA PAHAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG
     PQVGALELAG GPGAGGLEGP PQKRGIVEQC CAGVCSLYQL ENYCN
//
ID   INS_SPETR               Reviewed;         110 AA.
AC   Q91XI3;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   29-OCT-2014, entry version 66.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Spermophilus tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Ictidomys tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RA   Tredrea M.M., Buck M.J., Guhaniyogi J., Squire T.L., Andrews M.T.;
RT   "Regulation of PDK4 expression in a hibernating mammal.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY038604; AAK72558.1; -; mRNA.
DR   RefSeq; NP_001269184.1; NM_001282255.1.
DR   ProteinModelPortal; Q91XI3; -.
DR   SMR; Q91XI3; 25-110.
DR   Ensembl; ENSSTOT00000022326; ENSSTOP00000017025; ENSSTOG00000026937.
DR   GeneID; 101966207; -.
DR   CTD; 3630; -.
DR   GeneTree; ENSGT00390000015440; -.
DR   HOVERGEN; HBG006137; -.
DR   InParanoid; Q91XI3; -.
DR   OMA; VEQCCHN; -.
DR   OrthoDB; EOG7TF7CG; -.
DR   TreeFam; TF332820; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0015758; P:glucose transport; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015912.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015913.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015914.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     43    109       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     95    100       {ECO:0000250}.
SQ   SEQUENCE   110 AA;  12004 MW;  4511768D6622BEE5 CRC64;
     MALWTRLLPL LALLALLGPD PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKSRREVEE
     QQGGQVELGG GPGAGLPQPL ALEMALQKRG IVEQCCTSIC SLYQLENYCN
//
ID   INS_STRCA               Reviewed;          51 AA.
AC   P67969; P01332;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-OCT-2014, entry version 43.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Struthio camelus (Ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Palaeognathae; Struthioniformes;
OC   Struthionidae; Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3045031;
RA   Evans T.K., Litthauer D., Oelofsen W.;
RT   "Purification and primary structure of ostrich insulin.";
RL   Int. J. Pept. Protein Res. 31:454-462(1988).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   ProteinModelPortal; P67969; -.
DR   SMR; P67969; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015917.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015918.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT   DISULFID     19     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5698 MW;  976EFAE8987D40DD CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKA GIVEQCCHNT CSLYQLENYC N
//
ID   INS_SQUAC               Reviewed;          54 AA.
AC   P12704;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   29-OCT-2014, entry version 76.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Squalus acanthias (Spiny dogfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Squalimorphii; Squaliformes; Squalidae; Squalus.
OX   NCBI_TaxID=7797;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6352261; DOI=10.1111/j.1432-1033.1983.tb07685.x;
RA   Bajaj J., Blundell T.L., Pitts J.E., Wood S.P., Tatnell M.A.,
RA   Falkmer S., Emdin S.O., Gowan L.K., Crow H., Schwabe C., Wollmer A.,
RA   Strassburger W.;
RT   "Dogfish insulin. Primary structure, conformation and biological
RT   properties of an elasmobranchial insulin.";
RL   Eur. J. Biochem. 135:535-542(1983).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S07220; INDF.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     32       Insulin B chain.
FT                                /FTId=PRO_0000015915.
FT   PEPTIDE      33     54       Insulin A chain.
FT                                {ECO:0000269|PubMed:6352261}.
FT                                /FTId=PRO_0000015916.
FT   DISULFID      7     39       Interchain (between B and A chains).
FT   DISULFID     19     52       Interchain (between B and A chains).
FT   DISULFID     38     43
FT   NON_CONS     32     33       {ECO:0000305}.
SQ   SEQUENCE   54 AA;  6094 MW;  BC768929BE82F36B CRC64;
     LPSQHLCGSH LVEALYFVCG PKGFYYLPKB ZVGIVEHCCH NTCSLYDLEG YCNQ
//
ID   INS_THUTH               Reviewed;          51 AA.
AC   P01339;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-OCT-2014, entry version 81.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Thunnus thynnus (Atlantic bluefin tuna) (Scomber thynnus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8237;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5406482;
RA   Neumann P.A., Humbel R.E.;
RT   "Isolation of a single component of fish insulin from a bonito-tuna-
RT   swordfish insulin mixture and its complete amino-acid sequence.";
RL   Int. J. Protein Res. 1:125-140(1969).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   ProteinModelPortal; P01339; -.
DR   SMR; P01339; 5-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015919.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015920.
FT   DISULFID      8     37       Interchain (between B and A chains).
FT   DISULFID     20     50       Interchain (between B and A chains).
FT   DISULFID     36     41
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5742 MW;  A516B9A5CBAE605A CRC64;
     VAPPQHLCGS HLVDALYLVC GDRGFFYNPK GIVEQCCHKP CNIFDLQNYC N
//
ID   INS_TORMA               Reviewed;          70 AA.
AC   P12705;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   29-OCT-2014, entry version 78.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor; Fragments;
GN   Name=ins;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3549433; DOI=10.1016/0016-6480(86)90004-3;
RA   Conlon J.M., Thim L.;
RT   "Primary structure of insulin and a truncated C-peptide from an
RT   elasmobranchian fish, Torpedo marmorata.";
RL   Gen. Comp. Endocrinol. 64:199-205(1986).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 represent paired basic residues
CC       assumed by homology to be present in the precursor molecule.
CC       {ECO:0000305}.
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DR   PIR; S07212; IPRYM.
DR   ProteinModelPortal; P12705; -.
DR   SMR; P12705; 3-30.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015921.
FT   PROPEP       33    >49       C peptide.
FT                                /FTId=PRO_0000015922.
FT   PEPTIDE      50     70       Insulin A chain.
FT                                /FTId=PRO_0000015923.
FT   DISULFID      7     56       Interchain (between B and A chains).
FT   DISULFID     19     69       Interchain (between B and A chains).
FT   DISULFID     55     60
FT   NON_CONS     49     50       {ECO:0000305}.
SQ   SEQUENCE   70 AA;  7663 MW;  049C833B36146A9C CRC64;
     LPSQHLCGSH LVEALYFVCG PKGFYYLPKA XXFVDSLAGY SKHQNGGISG IVEHCCHNTC
     SLFDLEGYCN
//
ID   INS_TRADO               Reviewed;          51 AA.
AC   P69047; P31887;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 45.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Trachemys dorbigni (Black-bellied slider turtle) (Chrysemys dorbigni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Testudines; Cryptodira; Testudinoidea;
OC   Emydidae; Trachemys.
OX   NCBI_TaxID=31137;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1808015; DOI=10.1016/0016-6480(91)90081-G;
RA   Cascone O., Turyn D., Dellacha J.M., Machado V.L.A., Marques M.,
RA   Vita N., Cassan C., Ferrara P., Guillemot J.-C.;
RT   "Isolation, purification and primary structure of insulin from the
RT   turtle Chrysemys dorbigni.";
RL   Gen. Comp. Endocrinol. 84:355-359(1991).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A61129; A61129.
DR   ProteinModelPortal; P69047; -.
DR   SMR; P69047; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015795.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015796.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     50       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     36     41       {ECO:0000250}.
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5698 MW;  976EFAE8987D40DD CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKA GIVEQCCHNT CSLYQLENYC N
//
ID   INS_TRASC               Reviewed;          51 AA.
AC   P69048; P31887;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   29-OCT-2014, entry version 41.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Trachemys scripta (Red-eared slider turtle) (Pseudemys scripta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Testudines; Cryptodira; Testudinoidea;
OC   Emydidae; Trachemys.
OX   NCBI_TaxID=34903;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1974347; DOI=10.1016/0196-9781(90)90043-5;
RA   Conlon J.M., Hicks J.W.;
RT   "Isolation and structural characterization of insulin, glucagon and
RT   somatostatin from the turtle, Pseudemys scripta.";
RL   Peptides 11:461-466(1990).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; A60414; A60414.
DR   ProteinModelPortal; P69048; -.
DR   SMR; P69048; 3-51.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE       1     30       Insulin B chain.
FT                                /FTId=PRO_0000015924.
FT   PEPTIDE      31     51       Insulin A chain.
FT                                /FTId=PRO_0000015925.
FT   DISULFID      7     37       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     19     50       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     36     41       {ECO:0000250}.
FT   NON_CONS     30     31       {ECO:0000305}.
SQ   SEQUENCE   51 AA;  5698 MW;  976EFAE8987D40DD CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKA GIVEQCCHNT CSLYQLENYC N
//
ID   INS_VERMO               Reviewed;         115 AA.
AC   Q9W7R2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   29-OCT-2014, entry version 62.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Verasper moseri (Barfin flounder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Verasper.
OX   NCBI_TaxID=98923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Andoh T., Nagasawa H.;
RT   "Two molecular forms of insulin from barfin flounder, Verasper moseri,
RT   are derived from a single gene.";
RL   Zool. Sci. 15:931-937(1998).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AB029318; BAA82315.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9W7R2; -.
DR   SMR; Q9W7R2; 29-54.
DR   HOVERGEN; HBG006137; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 2.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000250}.
FT   PEPTIDE      23     53       Insulin B chain.
FT                                /FTId=PRO_0000015926.
FT   PROPEP       56     92       C peptide.
FT                                /FTId=PRO_0000015927.
FT   PEPTIDE      95    115       Insulin A chain.
FT                                /FTId=PRO_0000015928.
FT   DISULFID     32    101       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID     44    114       Interchain (between B and A chains).
FT                                {ECO:0000250}.
FT   DISULFID    100    105       {ECO:0000250}.
SQ   SEQUENCE   115 AA;  12608 MW;  7EA2A5B568DEDDBB CRC64;
     MAALWLQSVS LLVLMLVSWS GSQAVLPPQH LCGAHLVDAL YLVCGERGFF YTPKRDVDPL
     LGFLPAKSGG AAAGGENEVA EFAFKDQMEM MVKRGIVEQC CHKPCNIFDL QNYCN
//
