ID   IAPP_OCTDE              Reviewed;          91 AA.
AC   P22889;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Islet amyloid polypeptide;
DE   AltName: Full=Amylin;
DE   Flags: Precursor;
GN   Name=IAPP;
OS   Octodon degus (Degu) (Sciurus degus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC   Octodon.
OX   NCBI_TaxID=10160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2293024; DOI=10.1210/mend-4-8-1192;
RA   Nishi M., Steiner D.F.;
RT   "Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin,
RT   and glucagon precursors from a New World rodent, the degu, Octodon degus.";
RL   Mol. Endocrinol. 4:1192-1198(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; M57669; AAA40589.1; -; mRNA.
DR   PIR; A36118; A36118.
DR   RefSeq; NP_001267801.1; NM_001280872.1.
DR   AlphaFoldDB; P22889; -.
DR   SMR; P22889; -.
DR   GeneID; 101563275; -.
DR   CTD; 3375; -.
DR   OMA; CATQRLT; -.
DR   OrthoDB; 1454612at2759; -.
DR   Proteomes; UP000515203; Unplaced.
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_0000004115"
FT   PEPTIDE         37..73
FT                   /note="Islet amyloid polypeptide"
FT                   /id="PRO_0000004116"
FT   PROPEP          77..91
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004117"
FT   MOD_RES         73
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..43
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   91 AA;  9925 MW;  42AB31AE1CE9EA99 CRC64;
     MCLLQLPVVL LLLSAALNTL KATPIASDTD HRVDKRKCNT ATCATQRLTN FLVRSSHNLG
     AALPPTKVGS NTYGRRNAEV VDVELLHYLP L