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   25-MAY-2022, entry version 58.
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; Salmoniformes;
OC   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) insulin.";
RL   Biokhimiia 52:247-254(1987).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=2184990; DOI=10.1016/0305-0491(90)90006-f;
RA   Rusakov Y.I., Karasev V.S., Bondareva V.M., Pertseva M.N., Pankov Y.A.;
RT   "Isolation, primary structure, and biological and immunological properties
RT   of pink and chum salmon insulins.";
RL   Comp. Biochem. Physiol. 95B:477-482(1990).
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   PIR; S02203; INON.
DR   AlphaFoldDB; P68989; -.
DR   SMR; P68989; -.
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..29
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015861"
FT   PEPTIDE         30..50
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015862"
FT   DISULFID        7..36
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..49
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..40
FT                   /evidence="ECO:0000250"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   50 AA;  5576 MW;  D3D01633158CD95F CRC64;
     AAAQHLCGSH LVDALYLVCG EKGFFYNPKG IVEQCCHKPC NIFDLQNYCN