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   01-SEP-2009, entry version 62.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89345542; 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
RT   mammals 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   MEDLINE=87231921; 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
RT   in 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   MEDLINE=91006862; PubMed=2210054;
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
RT   amino acid residues of potential significance for islet amyloid
RT   formation.";
RL   Diabetes 39:118-122(1990).
CC   -!- FUNCTION: Selectively inhibits insulin-stimulated glucose
CC       utilization and glycogen deposition in muscle, while not affecting
CC       adipocyte glucose metabolism (By similarity).
CC   -!- SUBUNIT: Interacts with IDE and INS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- DOMAIN: The mature protein is largely unstructured in the absence
CC       of a cognate ligand, and has a strong tendency to form fibrillar
CC       aggregates (By similarity).
CC   -!- SIMILARITY: Belongs to the calcitonin family.
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DR   EMBL; M25388; AAA30813.1; -; mRNA.
DR   PIR; A33542; A33542.
DR   RefSeq; NP_001036803.1; -.
DR   GeneID; 751513; -.
DR   CTD; 751513; -.
DR   HOVERGEN; P12967; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001693; Calcitonin-like.
DR   InterPro; IPR018360; Calcitonin_CS.
DR   InterPro; IPR000443; Islet_amyloid_polypep.
DR   PANTHER; PTHR10505; Calcitonin-like; 1.
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; Secreted; Signal.
FT   SIGNAL        1     22       Potential.
FT   PROPEP       23     31
FT                                /FTId=PRO_0000004102.
FT   PEPTIDE      34     70       Islet amyloid polypeptide.
FT                                /FTId=PRO_0000004103.
FT   PROPEP       74     89
FT                                /FTId=PRO_0000004104.
FT   MOD_RES      70     70       Tyrosine amide (By similarity).
FT   DISULFID     35     40       By similarity.
SQ   SEQUENCE   89 AA;  9832 MW;  0834D783DEAD72A8 CRC64;
     MCLLKLPVVL IVLLVALHHL KATPIESNQV EKRKCNTATC ATQRLANFLI RSSNNLGAIL
     SPTNVGSNTY GKRSTVDILN REPLNYLPF
//