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   25-MAY-2022, entry version 96.
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; DOI=10.1042/bj1100289;
RA   Reid K.B.M., Grant P.T., Youngson A.;
RT   "The sequence of amino acids in insulin isolated from islet tissue of the
RT   cod (Gadus callarias).";
RL   Biochem. J. 110:289-296(1968).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=4866431; DOI=10.1042/bj1060531;
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 increases
CC       cell permeability to monosaccharides, amino acids and fatty acids. It
CC       accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC       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   AlphaFoldDB; P01336; -.
DR   SMR; P01336; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04367; IlGF_insulin_like; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR11454; PTHR11454; 2.
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
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015811"
FT   PEPTIDE         31..51
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015812"
FT   DISULFID        8..37
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        20..50
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        36..41
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   51 AA;  5789 MW;  A51FD0C5D483705A CRC64;
     MAPPQHLCGS HLVDALYLVC GDRGFFYNPK GIVDQCCHRP CDIFDLQNYC N