IAPP_MOUSE
ID IAPP_MOUSE Reviewed; 93 AA.
AC P12968;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Islet amyloid polypeptide;
DE AltName: Full=Amylin;
DE AltName: Full=Diabetes-associated peptide;
DE Short=DAP;
DE Flags: Precursor;
GN Name=Iapp;
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 [MRNA].
RX PubMed=2668946; DOI=10.1073/pnas.86.15.5738;
RA Nishi M., Chan S.J., Nagamatsu S., Bell G.I., Steiner D.F.;
RT "Conservation of the sequence of islet amyloid polypeptide in five mammals
RT is consistent with its putative role as an islet hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5738-5742(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=9278863; DOI=10.1677/jme.0.0190079;
RA Ekawa K., Nishi M., Ohagi S., Sanke T., Nanjo K.;
RT "Cloning of mouse islet amyloid polypeptide gene and characterization of
RT its promoter.";
RL J. Mol. Endocrinol. 19:79-86(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-74.
RX PubMed=2666169; DOI=10.1016/0014-5793(89)81467-x;
RA Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V.,
RA Johnson K.H., Westermark P.;
RT "Sequence divergence in a specific region of islet amyloid polypeptide
RT (IAPP) explains differences in islet amyloid formation between species.";
RL FEBS Lett. 251:261-264(1989).
CC -!- FUNCTION: Selectively inhibits insulin-stimulated glucose utilization
CC and glycogen deposition in muscle, while not affecting adipocyte
CC glucose metabolism.
CC -!- SUBUNIT: Interacts with IDE and INS. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The mature protein is largely unstructured in the absence of a
CC cognate ligand, but contrary to the human protein, it does not easily
CC form fibrillar aggregates.
CC -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR EMBL; M25389; AAA37874.1; -; mRNA.
DR EMBL; D31820; BAA22051.1; -; Genomic_DNA.
DR EMBL; BC027527; AAH27527.1; -; mRNA.
DR CCDS; CCDS39694.1; -.
DR PIR; C33542; C33542.
DR RefSeq; NP_034621.1; NM_010491.2.
DR AlphaFoldDB; P12968; -.
DR BMRB; P12968; -.
DR SMR; P12968; -.
DR IntAct; P12968; 2.
DR STRING; 10090.ENSMUSP00000043956; -.
DR iPTMnet; P12968; -.
DR PhosphoSitePlus; P12968; -.
DR PaxDb; P12968; -.
DR PRIDE; P12968; -.
DR ProteomicsDB; 273084; -.
DR Antibodypedia; 4370; 428 antibodies from 35 providers.
DR DNASU; 15874; -.
DR Ensembl; ENSMUST00000041993; ENSMUSP00000043956; ENSMUSG00000041681.
DR GeneID; 15874; -.
DR KEGG; mmu:15874; -.
DR UCSC; uc009epb.2; mouse.
DR CTD; 3375; -.
DR MGI; MGI:96382; Iapp.
DR VEuPathDB; HostDB:ENSMUSG00000041681; -.
DR eggNOG; ENOG502S4AQ; Eukaryota.
DR GeneTree; ENSGT00510000048671; -.
DR HOGENOM; CLU_189304_0_0_1; -.
DR InParanoid; P12968; -.
DR OMA; CATQRLT; -.
DR OrthoDB; 1454612at2759; -.
DR PhylomeDB; P12968; -.
DR TreeFam; TF330783; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-419812; Calcitonin-like ligand receptors.
DR BioGRID-ORCS; 15874; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Iapp; mouse.
DR PRO; PR:P12968; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P12968; protein.
DR Bgee; ENSMUSG00000041681; Expressed in islet of Langerhans and 76 other tissues.
DR Genevisible; P12968; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0097647; P:amylin receptor signaling pathway; ISO:MGI.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR InterPro; IPR021117; Calcitonin-like.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR018360; Calcitonin_CS.
DR InterPro; IPR001693; Calcitonin_peptide-like.
DR InterPro; IPR000443; IAPP.
DR PANTHER; PTHR10505; PTHR10505; 2.
DR PANTHER; PTHR10505:SF4; PTHR10505:SF4; 2.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00818; ISLETAMYLOID.
DR SMART; SM00113; CALCITONIN; 1.
DR PROSITE; PS00258; CALCITONIN; 1.
PE 3: Inferred from homology;
KW Amidation; Amyloid; Cleavage on pair of basic residues; Disulfide bond;
KW Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..35
FT /id="PRO_0000004112"
FT PEPTIDE 38..74
FT /note="Islet amyloid polypeptide"
FT /id="PRO_0000004113"
FT PROPEP 78..93
FT /id="PRO_0000004114"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Tyrosine amide"
FT /evidence="ECO:0000250"
FT DISULFID 39..44
FT /evidence="ECO:0000250"
SQ SEQUENCE 93 AA; 10022 MW; B135DBBC81475B15 CRC64;
MMCISKLPAV LLILSVALNH LRATPVRSGS NPQMDKRKCN TATCATQRLA NFLVRSSNNL
GPVLPPTNVG SNTYGKRNAA GDPNRESLDF LLV
