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   25-MAY-2022, 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   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 been
RT   conserved between the American eel, Anguilla rostrata and the European eel,
RT   Anguilla anguilla.";
RL   Gen. Comp. Endocrinol. 82:23-32(1991).
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; A61125; A61125.
DR   AlphaFoldDB; P42633; -.
DR   SMR; P42633; -.
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                   /evidence="ECO:0000269|PubMed:1874385"
FT                   /id="PRO_0000015751"
FT   PEPTIDE         31..51
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:1874385"
FT                   /id="PRO_0000015752"
FT   DISULFID        7..37
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..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;  5652 MW;  1999FD7EEA173CB2 CRC64;
     ASTQHLCGSH LVEALYLVCG SNGFFFNPKD GIVEQCCHKP CSIFDLQNYC N