INS2_MOUSE
ID INS2_MOUSE Reviewed; 110 AA.
AC P01326;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Insulin-2;
DE Contains:
DE RecName: Full=Insulin-2 B chain;
DE Contains:
DE RecName: Full=Insulin-2 A chain;
DE Flags: Precursor;
GN Name=Ins2; Synonyms=Ins-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3104603; DOI=10.1007/bf02100639;
RA Wentworth B.M., Schaefer I.M., Villa-Komaroff L., Chirgwin J.M.;
RT "Characterization of the two nonallelic genes encoding mouse
RT preproinsulin.";
RL J. Mol. Evol. 23:305-312(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NON;
RX PubMed=2397023; DOI=10.1677/jme.0.0050061;
RA Sawa T., Ohgaku S., Morioka H., Yano S.;
RT "Molecular cloning and DNA sequence analysis of preproinsulin genes in the
RT NON mouse, an animal model of human non-obese, non-insulin-dependent
RT diabetes mellitus.";
RL J. Mol. Endocrinol. 5:61-67(1990).
RN [3]
RP PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX PubMed=5063718; DOI=10.1515/bchm2.1972.353.1.451;
RA Buenzli H.F., Glatthaar B., Kunz P., Muelhaupt E., Humbel R.E.;
RT "Amino acid sequence of the two insulins from mouse (Maus musculus).";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:451-458(1972).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; X04724; CAA28433.1; -; Genomic_DNA.
DR CCDS; CCDS22034.1; -.
DR PIR; A26342; INMS2.
DR RefSeq; NP_001172012.1; NM_001185083.2.
DR RefSeq; NP_001172013.1; NM_001185084.2.
DR RefSeq; NP_032413.1; NM_008387.5.
DR AlphaFoldDB; P01326; -.
DR SMR; P01326; -.
DR STRING; 10090.ENSMUSP00000101553; -.
DR iPTMnet; P01326; -.
DR PhosphoSitePlus; P01326; -.
DR PaxDb; P01326; -.
DR PRIDE; P01326; -.
DR ProteomicsDB; 269317; -.
DR ABCD; P01326; 1 sequenced antibody.
DR DNASU; 16334; -.
DR Ensembl; ENSMUST00000000220; ENSMUSP00000000220; ENSMUSG00000000215.
DR Ensembl; ENSMUST00000105932; ENSMUSP00000101552; ENSMUSG00000000215.
DR Ensembl; ENSMUST00000105933; ENSMUSP00000101553; ENSMUSG00000000215.
DR Ensembl; ENSMUST00000105934; ENSMUSP00000101554; ENSMUSG00000000215.
DR Ensembl; ENSMUST00000210288; ENSMUSP00000147425; ENSMUSG00000000215.
DR GeneID; 16334; -.
DR KEGG; mmu:16334; -.
DR UCSC; uc009kof.2; mouse.
DR CTD; 16334; -.
DR MGI; MGI:96573; Ins2.
DR VEuPathDB; HostDB:ENSMUSG00000000215; -.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR GeneTree; ENSGT00390000015440; -.
DR InParanoid; P01326; -.
DR OMA; LANQHLC; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P01326; -.
DR TreeFam; TF332820; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-74713; IRS activation.
DR Reactome; R-MMU-74749; Signal attenuation.
DR Reactome; R-MMU-74751; Insulin receptor signalling cascade.
DR Reactome; R-MMU-74752; Signaling by Insulin receptor.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR BioGRID-ORCS; 16334; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ins2; mouse.
DR PRO; PR:P01326; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P01326; protein.
DR Bgee; ENSMUSG00000000215; Expressed in islet of Langerhans and 57 other tissues.
DR ExpressionAtlas; P01326; baseline and differential.
DR Genevisible; P01326; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0006983; P:ER overload response; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:1904659; P:glucose transmembrane transport; TAS:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IDA:MGI.
DR GO; GO:0007520; P:myoblast fusion; IGI:MGI.
DR GO; GO:0014902; P:myotube differentiation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0042325; P:regulation of phosphorylation; IDA:MGI.
DR GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
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:5063718"
FT PEPTIDE 25..54
FT /note="Insulin-2 B chain"
FT /evidence="ECO:0000269|PubMed:3104603"
FT /id="PRO_0000015845"
FT PROPEP 57..87
FT /note="C peptide"
FT /id="PRO_0000015846"
FT PEPTIDE 90..110
FT /note="Insulin-2 A chain"
FT /evidence="ECO:0000269|PubMed:3104603"
FT /id="PRO_0000015847"
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"
SQ SEQUENCE 110 AA; 12364 MW; 3554C8803D24FDAD CRC64;
MALWMRFLPL LALLFLWESH PTQAFVKQHL CGSHLVEALY LVCGERGFFY TPMSRREVED
PQVAQLELGG GPGAGDLQTL ALEVAQQKRG IVDQCCTSIC SLYQLENYCN
