INS_MYOSC
ID INS_MYOSC Reviewed; 50 AA.
AC P07453;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Insulin;
DE Contains:
DE RecName: Full=Insulin B chain;
DE Contains:
DE RecName: Full=Insulin A chain;
GN Name=ins;
OS Myoxocephalus scorpius (Shorthorn sculpin) (Cottus scorpius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Cottidae; Myoxocephalus.
OX NCBI_TaxID=8097;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3525155; DOI=10.1111/j.1432-1033.1986.tb09728.x;
RA Cutfield J.F., Cutfield S.M., Carne A., Emdin S.O., Falkmer S.;
RT "The isolation, purification and amino-acid sequence of insulin from the
RT teleost fish Cottus scorpius (daddy sculpin).";
RL Eur. J. Biochem. 158:117-123(1986).
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}.
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 PIR; A25061; INFIS.
DR AlphaFoldDB; P07453; -.
DR SMR; P07453; -.
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 /evidence="ECO:0000269|PubMed:3525155"
FT /id="PRO_0000015850"
FT PEPTIDE 30..50
FT /note="Insulin A chain"
FT /evidence="ECO:0000269|PubMed:3525155"
FT /id="PRO_0000015851"
FT DISULFID 7..36
FT /note="Interchain (between B and A chains)"
FT DISULFID 19..49
FT /note="Interchain (between B and A chains)"
FT DISULFID 35..40
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
SQ SEQUENCE 50 AA; 5683 MW; 0A600B9EBFE15827 CRC64;
ADPQHLCGSH LVDALYLVCG DRGFFYNPKG IVEQCCHRPC NIRVLENYCN