ID   INS1_KATPE              Reviewed;          50 AA.
AC   C0HJI2;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Insulin-1 {ECO:0000303|Ref.1};
DE   Contains:
DE     RecName: Full=Insulin-1 B chain {ECO:0000303|Ref.1};
DE   Contains:
DE     RecName: Full=Insulin-1 A chain {ECO:0000303|Ref.1};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Andoh T.;
RT   "Primary structures of two insulins from Bonito (Katsuwonus pelamis).";
RL   Submitted (APR-2014) to UniProtKB.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000255}.
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DR   AlphaFoldDB; C0HJI2; -.
DR   SMR; C0HJI2; -.
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-1 B chain"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000429388"
FT   PEPTIDE         30..50
FT                   /note="Insulin-1 A chain"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000429389"
FT   DISULFID        7..36
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        19..49
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        35..40
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   50 AA;  5673 MW;  C92408F762625D03 CRC64;
     ISSQHLCGSH LVEALNLVCG DRGFFYNPRG IVEQCCHRPC SIFELENYCN