ID   INS2_KATPE              Reviewed;          51 AA.
AC   C0HJI3;
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-2 {ECO:0000303|Ref.1};
DE   Contains:
DE     RecName: Full=Insulin-2 B chain {ECO:0000303|Ref.1};
DE   Contains:
DE     RecName: Full=Insulin-2 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; C0HJI3; -.
DR   SMR; C0HJI3; -.
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-2 B chain"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000429390"
FT   PEPTIDE         31..51
FT                   /note="Insulin-2 A chain"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000429391"
FT   DISULFID        8..37
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        20..50
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        36..41
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   51 AA;  5728 MW;  A516A0987D6D204B CRC64;
     AAPPQHLCGS HLVDALYLVC GERGFFYNPK GIVEQCCHKP CNIFDLQNYC N