ID   INS_PLATA               Reviewed;          51 AA.
AC   C0HJU0;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Insulin {ECO:0000303|PubMed:26743346};
DE   Contains:
DE     RecName: Full=Insulin B chain {ECO:0000303|PubMed:26743346};
DE   Contains:
DE     RecName: Full=Insulin A chain {ECO:0000303|PubMed:26743346};
GN   Name=ins {ECO:0000305};
OS   Platax teira (Longfin batfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Ephippiformes; Ephippidae; Platax.
OX   NCBI_TaxID=334891;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Endocrine gland {ECO:0000303|PubMed:26743346};
RX   PubMed=26743346; DOI=10.1016/j.ygcen.2015.12.025;
RA   Andoh T.;
RT   "Development of a widely applicable immunoassay for insulin in marine
RT   teleosts that regulates cross-reactivity using biotinylation and inhibits
RT   interference by plasma components.";
RL   Gen. Comp. Endocrinol. 226:72-81(2016).
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. {ECO:0000305}.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000250|UniProtKB:P01317}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26743346}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HJU0; -.
DR   SMR; C0HJU0; -.
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:26743346"
FT                   /id="PRO_0000438532"
FT   PEPTIDE         31..51
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:26743346"
FT                   /id="PRO_0000438533"
FT   DISULFID        8..37
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01317"
FT   DISULFID        20..50
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01317"
FT   DISULFID        36..41
FT                   /evidence="ECO:0000250|UniProtKB:P01317"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|PubMed:26743346"
SQ   SEQUENCE   51 AA;  5770 MW;  A516B9A5D493605A CRC64;
     VAPPQHLCGS HLVDALYLVC GDRGFFYNPK GIVEQCCHRP CNIFDLQNYC N