ID   INS_RODSP               Reviewed;         108 AA.
AC   P21563;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 94.
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   Rodentia sp.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; unclassified Rodentia.
OX   NCBI_TaxID=69158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2531072; DOI=10.1002/j.1460-2075.1989.tb08439.x;
RA   Robitzki A., Schroeder H.C., Ugarkovic D., Pfeifer K., Uhlenbruck G.,
RA   Mueller W.E.G.;
RT   "Demonstration of an endocrine signaling circuit for insulin in the sponge
RT   Geodia cydonium.";
RL   EMBO J. 8:2905-2909(1989).
RN   [2]
RP   DOUBTS ON VALIDITY OF SEQUENCE.
RA   Bairoch A., Duret L.;
RL   Unpublished observations (FEB-1996).
RN   [3]
RP   AGREEMENT WITH RODENT CONTAMINATION.
RA   Mueller W.E.G.;
RL   Unpublished observations (APR-1996).
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. Note=Stored in spherulous cells prior
CC       to secretion.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:2531072) thought to originate from the
CC       sponge Geodia cydonium, but, on the basis of phylogenetic studies
CC       (Ref.2) it seems very probable that the DNA sequence coding for this
CC       protein comes from a rodent as agreed by the original authors (Ref.3).
CC       It is also doubtful that this is a real active insulin.
CC       {ECO:0000305|PubMed:2531072}.
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DR   AlphaFoldDB; P21563; -.
DR   SMR; P21563; -.
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   PANTHER; PTHR11454; PTHR11454; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 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..23
FT   PEPTIDE         24..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015901"
FT   PROPEP          57..88
FT                   /note="C peptide"
FT                   /id="PRO_0000015902"
FT   PEPTIDE         90..108
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015903"
FT   DISULFID        30..94
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..107
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   108 AA;  11849 MW;  BF4B4826D2E30306 CRC64;
     MALWILLPLL ALLILWGPDP AQAFVNQHLC GSHLVEALYI LVCGERGFFY TPMSRREVED
     PQVGQVELGA GPGAGSEQTL ALEVARQARI VQQCTSGICS LYQENYCN