ID   INS_OCTDE               Reviewed;         109 AA.
AC   P17715;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   25-MAY-2022, entry version 116.
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   Octodon degus (Degu) (Sciurus degus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC   Octodon.
OX   NCBI_TaxID=10160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2293024; DOI=10.1210/mend-4-8-1192;
RA   Nishi M., Steiner D.F.;
RT   "Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin,
RT   and glucagon precursors from a New World rodent, the degu, Octodon degus.";
RL   Mol. Endocrinol. 4:1192-1198(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-53 AND 87-109.
RX   PubMed=2192710; DOI=10.1016/0006-291x(90)90369-x;
RA   Hellman U., Wernstedt C., Westermark P., O'Brien T.D., Rathbun W.B.,
RA   Johnson K.H.;
RT   "Amino acid sequence from degu islet amyloid-derived insulin shows unique
RT   sequence characteristics.";
RL   Biochem. Biophys. Res. Commun. 169:571-577(1990).
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; M57671; AAA40590.1; -; mRNA.
DR   PIR; B36118; IPRTDU.
DR   RefSeq; XP_004627141.1; XM_004627084.1.
DR   AlphaFoldDB; P17715; -.
DR   SMR; P17715; -.
DR   GeneID; 101571541; -.
DR   CTD; 3630; -.
DR   OMA; IVEQCCN; -.
DR   OrthoDB; 1644517at2759; -.
DR   Proteomes; UP000515203; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
DR   GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IEA:Ensembl.
DR   GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2192710"
FT   PEPTIDE         25..53
FT                   /note="Insulin B chain"
FT                   /evidence="ECO:0000269|PubMed:2192710"
FT                   /id="PRO_0000015855"
FT   PROPEP          56..84
FT                   /note="C peptide"
FT                   /id="PRO_0000015856"
FT   PEPTIDE         87..109
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:2192710"
FT                   /id="PRO_0000015857"
FT   DISULFID        31..93
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..106
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..97
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   109 AA;  12197 MW;  845CCE631A9A54D7 CRC64;
     MAPWMHLLTV LALLALWGPN SVQAYSSQHL CGSNLVEALY MTCGRSGFYR PHDRRELEDL
     QVEQAELGLE AGGLQPSALE MILQKRGIVD QCCNNICTFN QLQNYCNVP