ID   IAPP_RABIT              Reviewed;          67 AA.
AC   Q07334; Q28741; Q9BED7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 3.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Islet amyloid polypeptide;
DE   AltName: Full=Amylin;
DE   Flags: Precursor; Fragment;
GN   Name=IAPP;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-66.
RA   van Dijk M.A.M., de Jong W.W.;
RT   "Indels indicate that rodents are monophyletic and lagomorphs are their
RT   sister group.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-67.
RA   Albrandt K., Sierzega M.E., Mull E., Brady E.M.G.;
RT   "PCR amplification of amylin 3-34 from genomic DNA.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-64.
RC   STRAIN=New Zealand white;
RX   PubMed=8462765; DOI=10.1007/bf00399947;
RA   Christmanson L., Betsholtz C., Leckstroem A., Engstroem U., Cortie C.,
RA   Johnson K.H., Adrian T.E., Westermark P.;
RT   "Islet amyloid polypeptide in the rabbit and European hare: studies on its
RT   relationship to amyloidogenesis.";
RL   Diabetologia 36:183-188(1993).
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; AJ286814; CAC28529.1; -; mRNA.
DR   EMBL; U62630; AAB05917.1; -; Genomic_DNA.
DR   EMBL; S57804; AAB26084.1; -; mRNA.
DR   PIR; I46934; I46934.
DR   AlphaFoldDB; Q07334; -.
DR   eggNOG; ENOG502S4AQ; Eukaryota.
DR   InParanoid; Q07334; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021117; Calcitonin-like.
DR   InterPro; IPR021116; Calcitonin/adrenomedullin.
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.
PE   2: Evidence at transcript level;
KW   Amyloid; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..31
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000004119"
FT   PEPTIDE         35..>67
FT                   /note="Islet amyloid polypeptide"
FT                   /id="PRO_0000004120"
FT   DISULFID        35..40
FT                   /evidence="ECO:0000250"
FT   NON_TER         67
SQ   SEQUENCE   67 AA;  7230 MW;  BF5FEC2064F69646 CRC64;
     MCILKLPIVL LVLSVAVNHL QASPVESHQV EKRKCNTVTC ATQRLANFLI HSSNNFGAIF
     SPPSVGS