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   02-DEC-2020, entry version 87.
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}.
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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   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: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