INS_SERQU
ID INS_SERQU Reviewed; 51 AA.
AC C0HJT9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 25-MAY-2022, entry version 11.
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 Seriola quinqueradiata (Five-ray yellowtail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=8161 {ECO:0000303|PubMed:26743346};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; C0HJT9; -.
DR SMR; C0HJT9; -.
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_0000438534"
FT PEPTIDE 31..51
FT /note="Insulin A chain"
FT /evidence="ECO:0000269|PubMed:26743346"
FT /id="PRO_0000438535"
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:0000305"
SQ SEQUENCE 51 AA; 5742 MW; A516B9A5CBAE605A CRC64;
VAPPQHLCGS HLVDALYLVC GDRGFFYNPK GIVEQCCHKP CNIFDLQNYC N