INS_CAVPO
ID INS_CAVPO Reviewed; 110 AA.
AC P01329;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 143.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3839794; DOI=10.1016/s0021-9258(17)39123-8;
RA Watt V.M.;
RT "Sequence and evolution of guinea pig preproinsulin DNA.";
RL J. Biol. Chem. 260:10926-10929(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6591179; DOI=10.1073/pnas.81.16.5046;
RA Chan S.J., Episkopou V., Zeitlin S., Karathanasis S.K., Mackrell A.,
RA Steiner D.F., Efstratiadis A.;
RT "Guinea pig preproinsulin gene: an evolutionary compromise?";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5046-5050(1984).
RN [3]
RP PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA Smith L.F.;
RT "Species variation in the amino acid sequence of insulin.";
RL Am. J. Med. 40:662-666(1966).
RN [4]
RP SEQUENCE REVISION.
RA Smith L.F.;
RT "Amino acid sequences of insulins.";
RL Diabetes 21 Suppl. 2:457-460(1972).
RN [5]
RP PROTEIN SEQUENCE OF 57-87.
RX PubMed=1158864; DOI=10.1016/s0021-9258(19)41064-8;
RA Massey D.E., Smyth D.G.;
RT "Guinea pig proinsulin. Primary structure of the C-peptide isolated from
RT pancreas.";
RL J. Biol. Chem. 250:6288-6290(1975).
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. {ECO:0000250|UniProtKB:P01308}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; K02233; AAA37041.1; -; Genomic_DNA.
DR EMBL; M11713; AAA37042.1; -; mRNA.
DR PIR; A25370; IPGP.
DR RefSeq; NP_001166362.1; NM_001172891.1.
DR RefSeq; XP_013006103.1; XM_013150649.1.
DR AlphaFoldDB; P01329; -.
DR SMR; P01329; -.
DR STRING; 10141.ENSCPOP00000019016; -.
DR Ensembl; ENSCPOT00000044344; ENSCPOP00000026989; ENSCPOG00000031250.
DR GeneID; 100379579; -.
DR KEGG; cpoc:100379579; -.
DR CTD; 3630; -.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR GeneTree; ENSGT00390000015440; -.
DR HOGENOM; CLU_140421_1_0_1; -.
DR InParanoid; P01329; -.
DR OMA; LANQHLC; -.
DR OrthoDB; 1644517at2759; -.
DR TreeFam; TF332820; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000031250; Expressed in liver.
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:5949593"
FT PEPTIDE 25..54
FT /note="Insulin B chain"
FT /evidence="ECO:0000269|PubMed:6591179"
FT /id="PRO_0000015782"
FT PROPEP 57..87
FT /note="C peptide"
FT /id="PRO_0000015783"
FT PEPTIDE 90..110
FT /note="Insulin A chain"
FT /evidence="ECO:0000269|PubMed:6591179"
FT /id="PRO_0000015784"
FT DISULFID 31..96
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 43..109
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 95..100
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT CONFLICT 22
FT /note="G -> N (in Ref. 2; AAA37041)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..84
FT /note="ALEM -> QG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12187 MW; DB22FE4A9CC5266C CRC64;
MALWMHLLTV LALLALWGPN TGQAFVSRHL CGSNLVETLY SVCQDDGFFY IPKDRRELED
PQVEQTELGM GLGAGGLQPL ALEMALQKRG IVDQCCTGTC TRHQLQSYCN
