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INS_ACIGU
ID   INS_ACIGU               Reviewed;          52 AA.
AC   P81423;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Acipenser gueldenstaedtii (Russian sturgeon) (Danube sturgeon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX   NCBI_TaxID=7902;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=9650713; DOI=10.1111/j.1399-3011.1998.tb00637.x;
RA   Rusakov Y.I., Moriyama S., Bondareva V.M., Kolychev A.P., Amemiya Y.,
RA   Yasuda A., Kawauchi H.;
RT   "Isolation and characterization of insulin in Russian sturgeon (Acipenser
RT   guldenstaedti).";
RL   J. Pept. Res. 51:395-400(1998).
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   AlphaFoldDB; P81423; -.
DR   SMR; P81423; -.
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 B chain"
FT                   /id="PRO_0000015738"
FT   PEPTIDE         32..52
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015739"
FT   DISULFID        7..38
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..51
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        37..42
FT   NON_CONS        31..32
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   52 AA;  5811 MW;  BD1D693998D41631 CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYTPNK VGIVEQCCHS PCSLYDLENY CN
 
 
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