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   25-MAY-2022, entry version 91.
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 gene.";
RL   Comp. Biochem. Physiol. 121B:291-297(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 93-113.
RX   PubMed=7656183; DOI=10.1016/0742-8413(95)00023-z;
RA   Nguyen T.M., Wright J.R. Jr., Nielsen P.F., Conlon J.M.;
RT   "Characterization of the pancreatic hormones from the Brockmann body of the
RT   tilapia: implications for islet xenograft studies.";
RL   Comp. Biochem. Physiol. 111C:33-44(1995).
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   EMBL; AF038123; AAD22742.1; -; Genomic_DNA.
DR   AlphaFoldDB; P81025; -.
DR   STRING; 8128.ENSONIP00000000431; -.
DR   eggNOG; ENOG502S3FQ; Eukaryota.
DR   InParanoid; P81025; -.
DR   Proteomes; UP000005207; Unplaced.
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; 1.
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; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:7656183"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015865"
FT   PROPEP          56..90
FT                   /note="C peptide"
FT                   /id="PRO_0000015866"
FT   PEPTIDE         93..113
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015867"
FT   DISULFID        32..99
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..112
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..103
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  12480 MW;  C4719D5FC8920D3C CRC64;
     MAALWLQAFS LLVLMMVSWP GSQAVGGPQH LCGSHLVDAL YLVCGDRGFF YNPRRDVDPL
     LGFLPPKAGG AVVQGGENEV TFKDQMEMMV KRGIVEECCH KPCTIFDLQN YCN