ID   IAPP_BOVIN              Reviewed;          91 AA.
AC   Q28207;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Islet amyloid polypeptide;
DE   AltName: Full=Amylin;
DE   Flags: Precursor;
GN   Name=IAPP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-69.
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.
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; U62626; AAB05915.1; -; Genomic_DNA.
DR   RefSeq; NP_001181967.1; NM_001195038.1.
DR   AlphaFoldDB; Q28207; -.
DR   SMR; Q28207; -.
DR   STRING; 9913.ENSBTAP00000013921; -.
DR   PaxDb; Q28207; -.
DR   PRIDE; Q28207; -.
DR   GeneID; 100138011; -.
DR   KEGG; bta:100138011; -.
DR   CTD; 3375; -.
DR   eggNOG; ENOG502S4AQ; Eukaryota.
DR   HOGENOM; CLU_189304_0_0_1; -.
DR   InParanoid; Q28207; -.
DR   OrthoDB; 1454612at2759; -.
DR   TreeFam; TF330783; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 1.
DR   PANTHER; PTHR10505:SF4; PTHR10505:SF4; 1.
DR   Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR   PRINTS; PR00818; ISLETAMYLOID.
DR   SMART; SM00113; 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..33
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000269882"
FT   PEPTIDE         37..72
FT                   /note="Islet amyloid polypeptide"
FT                   /id="PRO_0000004095"
FT   PROPEP          78..91
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000269883"
FT   MOD_RES         72
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..42
FT                   /evidence="ECO:0000250"
FT   CONFLICT        46
FT                   /note="R -> C (in Ref. 2; AAB05915)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   91 AA;  9953 MW;  41CBAA3A0B9D099C CRC64;
     MGILKLPVVL IVLCVALNHL EGGGKPTESH QMEKRKCGTA TCETQRLANF LAPSSNKLGA
     IFSPTKMGSN TYGKRKKVEI LKREPLSYLP I