ID INS_KATPE Reviewed; 50 AA. AC P01340; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-FEB-2023, entry version 89. DE RecName: Full=Insulin; DE Contains: DE RecName: Full=Insulin B chain; DE Contains: DE RecName: Full=Insulin A chain; GN Name=ins; OS Katsuwonus pelamis (Skipjack tuna) (Bonito). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Pelagiaria; Scombriformes; Scombridae; Katsuwonus. OX NCBI_TaxID=8226; RN [1] RP PROTEIN SEQUENCE OF 1-29. RX PubMed=14035061; DOI=10.1093/oxfordjournals.jbchem.a127658; RA Kotaki A.; RT "Studies on insulin. V. On the structure of the glycyl chain of bonito RT insulin II."; RL J. Biochem. 53:61-70(1963). RN [2] RP PROTEIN SEQUENCE OF 30-50. RX PubMed=14036898; DOI=10.1093/oxfordjournals.jbchem.a127536; RA Kotaki A.; RT "Studies on insulin. III. On the structure of the alanyl chain of bonito RT insulin."; RL J. Biochem. 51:301-309(1962). 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; A01607; INBN2. 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 Gene3D; 1.10.100.10; 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:SF9; INSULIN; 1. DR PANTHER; PTHR11454; INSULIN/INSULIN GROWTH FACTOR; 1. DR Pfam; PF00049; Insulin; 2. DR PRINTS; PR00277; INSULIN. DR PRINTS; PR00276; INSULINFAMLY. DR SMART; SM00078; IlGF; 1. DR SUPFAM; SSF56994; Insulin-like; 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:14036898" FT /id="PRO_0000015826" FT PEPTIDE 30..50 FT /note="Insulin A chain" FT /id="PRO_0000015827" FT DISULFID 7..36 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250" FT DISULFID 19..49 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250" FT DISULFID 35..40 FT /evidence="ECO:0000250" FT NON_CONS 29..30 FT /evidence="ECO:0000305" SQ SEQUENCE 50 AA; 5698 MW; 3627578FE24CE92E CRC64; AANPHLCGSH LVEALYLVCG ERGFFYQPKG IHZZCCHKPC BIFZLZBYCN //