ID   INS2_HUSDA              Reviewed;          52 AA.
AC   C0HJI8;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Insulin-2 {ECO:0000303|PubMed:11150638};
DE   Contains:
DE     RecName: Full=Insulin-2 B chain {ECO:0000303|PubMed:11150638};
DE   Contains:
DE     RecName: Full=Insulin-2 A chain {ECO:0000303|PubMed:11150638};
OS   Huso dauricus (Kaluga sturgeon) (Acipenser dauricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Huso.
OX   NCBI_TaxID=55293;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas {ECO:0000269|PubMed:11150638};
RX   PubMed=11150638; DOI=10.1016/s0196-9781(00)00337-5;
RA   Andoh T., Nagasawa H., Matsubara T.;
RT   "Multiple molecular forms of glucagon and insulin in the kaluga sturgeon,
RT   Huso dauricus.";
RL   Peptides 21:1785-1792(2000).
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; C0HJI8; -.
DR   SMR; C0HJI8; -.
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..31
FT                   /note="Insulin-2 B chain"
FT                   /evidence="ECO:0000269|PubMed:11150638"
FT                   /id="PRO_0000429386"
FT   PEPTIDE         32..52
FT                   /note="Insulin-2 A chain"
FT                   /evidence="ECO:0000269|PubMed:11150638"
FT                   /id="PRO_0000429387"
FT   DISULFID        7..38
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        19..51
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   DISULFID        37..42
FT                   /evidence="ECO:0000250|UniProtKB:P01339"
FT   NON_CONS        31..32
FT                   /evidence="ECO:0000303|PubMed:11150638"
SQ   SEQUENCE   52 AA;  5795 MW;  BD1D692E2E0F6C31 CRC64;
     AANQHLCGAH LVEALYLVCG ERGFFYTPNK VGIVEQCCHS PCSLYDLENY CN