ID   IAPP_FELCA              Reviewed;          89 AA.
AC   P12967;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Islet amyloid polypeptide;
DE   AltName: Full=Amylin;
DE   Flags: Precursor;
GN   Name=IAPP;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
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   PROTEIN SEQUENCE OF 34-60.
RX   PubMed=3035556; DOI=10.1073/pnas.84.11.3881;
RA   Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D.,
RA   Johnson K.H.;
RT   "Amyloid fibrils in human insulinoma and islets of Langerhans of the
RT   diabetic cat are derived from a neuropeptide-like protein also present in
RT   normal islet cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 34-70.
RX   PubMed=2210054; DOI=10.2337/diacare.39.1.118;
RA   Betsholtz C., Christmanson L., Engstrom U., Rorsman F., Jordan K.,
RA   O'Brien T.D., Murtaugh M., Johnson K.H., Westermark P.;
RT   "Structure of cat islet amyloid polypeptide and identification of amino
RT   acid residues of potential significance for islet amyloid formation.";
RL   Diabetes 39:118-122(1990).
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, and has a strong tendency to form fibrillar aggregates.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   EMBL; M25388; AAA30813.1; -; mRNA.
DR   PIR; A33542; A33542.
DR   RefSeq; NP_001036803.1; NM_001043338.1.
DR   RefSeq; XP_019689424.1; XM_019833865.1.
DR   AlphaFoldDB; P12967; -.
DR   STRING; 9685.ENSFCAP00000020627; -.
DR   Ensembl; ENSFCAT00000024980; ENSFCAP00000020627; ENSFCAG00000029193.
DR   GeneID; 751513; -.
DR   KEGG; fca:751513; -.
DR   CTD; 3375; -.
DR   VGNC; VGNC:84035; IAPP.
DR   eggNOG; ENOG502S4AQ; Eukaryota.
DR   GeneTree; ENSGT00510000048671; -.
DR   HOGENOM; CLU_189304_0_0_1; -.
DR   InParanoid; P12967; -.
DR   OMA; CATQRLT; -.
DR   OrthoDB; 1454612at2759; -.
DR   Proteomes; UP000011712; Chromosome B4.
DR   Bgee; ENSFCAG00000029193; Expressed in adult mammalian kidney and 6 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 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   1: Evidence at protein level;
KW   Amidation; Amyloid; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Hormone; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..31
FT                   /id="PRO_0000004102"
FT   PEPTIDE         34..70
FT                   /note="Islet amyloid polypeptide"
FT                   /id="PRO_0000004103"
FT   PROPEP          74..89
FT                   /id="PRO_0000004104"
FT   MOD_RES         70
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..40
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   89 AA;  9832 MW;  0834D783DEAD72A8 CRC64;
     MCLLKLPVVL IVLLVALHHL KATPIESNQV EKRKCNTATC ATQRLANFLI RSSNNLGAIL
     SPTNVGSNTY GKRSTVDILN REPLNYLPF