ID   IAPP_CANLF              Reviewed;          89 AA.
AC   P17716;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Islet amyloid polypeptide;
DE   AltName: Full=Amylin;
DE   Flags: Precursor;
GN   Name=IAPP;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1543754; DOI=10.1016/0167-4781(92)90470-k;
RA   Albrandt K., Mull E., Cooper G.J.S., Johnson M.J.;
RT   "Nucleotide sequence of a cDNA for canine amylin.";
RL   Biochim. Biophys. Acta 1130:97-99(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 43-68.
RX   PubMed=2192709; DOI=10.1016/0006-291x(90)90359-u;
RA   Jordan K., Murtaugh M.P., O'Brien T.D., Westermark P., Betsholtz C.,
RA   Johnson K.H.;
RT   "Canine IAPP cDNA sequence provides important clues regarding
RT   diabetogenesis and amyloidogenesis in type 2 diabetes.";
RL   Biochem. Biophys. Res. Commun. 169:502-508(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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
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DR   EMBL; X59998; CAA42616.1; -; mRNA.
DR   EMBL; M37720; AAA30849.1; -; mRNA.
DR   PIR; S22344; S22344.
DR   RefSeq; NP_001003233.1; NM_001003233.2.
DR   AlphaFoldDB; P17716; -.
DR   STRING; 9612.ENSCAFP00000039036; -.
DR   TCDB; 1.C.49.1.1; the cytotoxic amylin (amylin) family.
DR   PaxDb; P17716; -.
DR   Ensembl; ENSCAFT00030043237; ENSCAFP00030037734; ENSCAFG00030023537.
DR   Ensembl; ENSCAFT00040032072; ENSCAFP00040027877; ENSCAFG00040017373.
DR   Ensembl; ENSCAFT00845027673; ENSCAFP00845021778; ENSCAFG00845015514.
DR   GeneID; 403909; -.
DR   KEGG; cfa:403909; -.
DR   CTD; 3375; -.
DR   VEuPathDB; HostDB:ENSCAFG00845015514; -.
DR   eggNOG; ENOG502S4AQ; Eukaryota.
DR   GeneTree; ENSGT00510000048671; -.
DR   HOGENOM; CLU_189304_0_0_1; -.
DR   InParanoid; P17716; -.
DR   OMA; CATQRLT; -.
DR   TreeFam; TF330783; -.
DR   Reactome; R-CFA-418555; G alpha (s) signalling events.
DR   Reactome; R-CFA-419812; Calcitonin-like ligand receptors.
DR   Proteomes; UP000002254; Chromosome 27.
DR   Bgee; ENSCAFG00000029872; Expressed in pancreas and 15 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   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..31
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004096"
FT   PEPTIDE         35..70
FT                   /note="Islet amyloid polypeptide"
FT                   /id="PRO_0000004097"
FT   PROPEP          74..89
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004098"
FT   MOD_RES         70
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..40
FT                   /evidence="ECO:0000250"
FT   CONFLICT        67
FT                   /note="S -> T (in Ref. 2; AAA30849)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  9800 MW;  9BF757E1C1493EEF CRC64;
     MCLLKLPVVL IILSVALNHL KATPIKSHQM EKRKCNTATC ATQRLANFLV RTSNNLGAIL
     SPTNVGSNTY GKRNTIEILN RGPLNYLPL