IAPP_CAVPO
ID IAPP_CAVPO Reviewed; 92 AA.
AC P12966;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Islet amyloid polypeptide;
DE AltName: Full=Amylin;
DE Flags: Precursor;
GN Name=IAPP;
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=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).
CC -!- FUNCTION: Selectively inhibits insulin-stimulated glucose utilization
CC and glycogen deposition in muscle, while not affecting adipocyte
CC glucose metabolism. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IDE and INS. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: The mature protein is largely unstructured in the absence of a
CC cognate ligand. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR EMBL; M25387; AAA37040.1; -; mRNA.
DR PIR; D33542; D33542.
DR RefSeq; NP_001166436.1; NM_001172965.2.
DR AlphaFoldDB; P12966; -.
DR SMR; P12966; -.
DR STRING; 10141.ENSCPOP00000008717; -.
DR Ensembl; ENSCPOT00000009798; ENSCPOP00000008717; ENSCPOG00000009711.
DR GeneID; 100135550; -.
DR KEGG; cpoc:100135550; -.
DR CTD; 3375; -.
DR eggNOG; ENOG502S4AQ; Eukaryota.
DR GeneTree; ENSGT00510000048671; -.
DR HOGENOM; CLU_189304_0_0_1; -.
DR InParanoid; P12966; -.
DR OMA; CATQRLT; -.
DR TreeFam; TF330783; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000009711; Expressed in thyroid gland.
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:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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; 1.
DR PANTHER; PTHR10505:SF4; PTHR10505:SF4; 1.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..34
FT /evidence="ECO:0000250"
FT /id="PRO_0000004099"
FT PEPTIDE 37..73
FT /note="Islet amyloid polypeptide"
FT /id="PRO_0000004100"
FT PROPEP 77..92
FT /evidence="ECO:0000250"
FT /id="PRO_0000004101"
FT MOD_RES 73
FT /note="Tyrosine amide"
FT /evidence="ECO:0000250"
FT DISULFID 38..43
FT /evidence="ECO:0000250"
SQ SEQUENCE 92 AA; 9989 MW; 67F3629014BF3F9C CRC64;
MCLLRLPVTL LVLCVALNEL KATSIASDTG HQVGKRKCNT ATCATQRLTN FLVRSSHNLG
AALLPTDVGS NTYGKRNAPQ ISDRELLHYL PL
