ID   INS_PSAOB               Reviewed;         110 AA.
AC   Q62587;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Psammomys obesus (Fat sand rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Psammomys.
OX   NCBI_TaxID=48139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=9166665; DOI=10.2337/diab.46.6.953;
RA   Kaiser N., Bailyes E.M., Schneider B.S., Cerasi E., Steiner D.F.,
RA   Hutton J.C., Gross D.J.;
RT   "Characterization of the unusual insulin of Psammomys obesus, a rodent with
RT   nutrition-induced NIDDM-like syndrome.";
RL   Diabetes 46:953-957(1997).
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   EMBL; X98241; CAA66897.1; -; mRNA.
DR   AlphaFoldDB; Q62587; -.
DR   SMR; Q62587; -.
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; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015889"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015890"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015891"
FT   DISULFID        31..96
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..109
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   110 AA;  12324 MW;  A006738E20579CB0 CRC64;
     MALWMRLLPL LAFLILWEPS PAHAFVNQHL CGSHLVEALY LVCGERGFFY TPKFRRGVDD
     PQMPQLELGG SPGAGDLRAL ALEVARQKRG IVEQCCTGIC SLYQLENYCN