ID IAPP_RAT Reviewed; 93 AA. AC P12969; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 03-NOV-2009, entry version 73. DE RecName: Full=Islet amyloid polypeptide; DE AltName: Full=Amylin; DE AltName: Full=Diabetes-associated peptide; DE Short=DAP; DE Flags: Precursor; GN Name=Iapp; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; 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 NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89240689; PubMed=2654937; DOI=10.1073/pnas.86.9.3127; RA Leffert J.D., Newgard C.B., Okamoto H., Milburn J.L., Luskey K.L.; RT "Rat amylin: cloning and tissue-specific expression in pancreatic RT islets."; RL Proc. Natl. Acad. Sci. U.S.A. 86:3127-3130(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WAP; TISSUE=Liver; RX MEDLINE=91027936; PubMed=2223885; DOI=10.1016/0167-4781(90)90210-S; RA van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., RA van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.; RT "Islet amyloid polypeptide: structure and upstream sequences of the RT IAPP gene in rat and man."; RL Biochim. Biophys. Acta 1087:235-240(1990). RN [4] RP PROTEIN SEQUENCE OF 38-74. RX MEDLINE=90026410; PubMed=2679555; DOI=10.1016/0006-291X(89)91733-6; RA Asai J., Nakazato M., Kangawa K., Matsukura S., Matsuo H.; RT "Isolation and sequence determination of rat islet amyloid RT polypeptide."; RL Biochem. Biophys. Res. Commun. 164:400-405(1989). RN [5] RP PROTEIN SEQUENCE OF 38-74. RX MEDLINE=90290528; PubMed=2357234; DOI=10.1016/0006-291X(90)90400-H; RA Asai J., Nakazato M., Miyazato M., Kangawa K., Matsuo H., RA Matsukura S.; RT "Regional distribution and molecular forms of rat islet amyloid RT polypeptide."; RL Biochem. Biophys. Res. Commun. 169:788-795(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-74. RX MEDLINE=89325677; PubMed=2666169; DOI=10.1016/0014-5793(89)81467-X; RA Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., RA Johnson K.H., Westermark P.; RT "Sequence divergence in a specific region of islet amyloid polypeptide RT (IAPP) explains differences in islet amyloid formation between RT species."; RL FEBS Lett. 251:261-264(1989). RN [7] RP DOMAIN. RX PubMed=19360098; DOI=10.1371/journal.pcbi.1000357; RA Jiang P., Xu W., Mu Y.; RT "Amyloidogenesis abolished by proline substitutions but enhanced by RT lipid binding."; RL PLoS Comput. Biol. 5:E1000357-E1000357(2009). 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. CC -!- TISSUE SPECIFICITY: Abundant in the islets of Langerhans but is CC not present in the brain or seven other tissues examined. CC -!- DOMAIN: The mature protein is largely unstructured in the absence CC of a cognate ligand, but contrary to the human protein, it does CC not easily form fibrillar aggregates. CC -!- SIMILARITY: Belongs to the calcitonin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M25390; AAA41359.1; -; mRNA. DR EMBL; J04544; AAA40730.1; -; mRNA. DR EMBL; X52820; CAA37003.1; -; Genomic_DNA. DR EMBL; X52821; CAA37003.1; JOINED; Genomic_DNA. DR IPI; IPI00202679; -. DR PIR; S13566; TCRTIA. DR RefSeq; NP_036718.1; -. DR UniGene; Rn.11394; -. DR PDB; 2KJ7; NMR; -; A=38-74. DR PDBsum; 2KJ7; -. DR STRING; P12969; -. DR Ensembl; ENSRNOT00000016614; ENSRNOP00000016614; ENSRNOG00000012417; Rattus norvegicus. DR GeneID; 24476; -. DR KEGG; rno:24476; -. DR UCSC; NM_012586; rat. DR CTD; 24476; -. DR RGD; 2854; Iapp. DR HOVERGEN; P12969; -. DR OMA; NTYGKRN; -. DR NextBio; 603429; -. DR ArrayExpress; P12969; -. DR Genevestigator; P12969; -. DR GermOnline; ENSRNOG00000012417; Rattus norvegicus. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030141; C:secretory granule; TAS:RGD. DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW. DR GO; GO:0006006; P:glucose metabolic process; TAS:RGD. 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 3D-structure; Amidation; Amyloid; Cleavage on pair of basic residues; KW Direct protein sequencing; Disulfide bond; Hormone; Secreted; Signal. FT SIGNAL 1 23 Potential. FT PROPEP 24 35 FT /FTId=PRO_0000004121. FT PEPTIDE 38 74 Islet amyloid polypeptide. FT /FTId=PRO_0000004122. FT PROPEP 78 93 FT /FTId=PRO_0000004123. FT MOD_RES 74 74 Tyrosine amide. FT DISULFID 39 44 By similarity. SQ SEQUENCE 93 AA; 10015 MW; 5A76C92E624DA962 CRC64; MRCISRLPAV LLILSVALGH LRATPVGSGT NPQVDKRKCN TATCATQRLA NFLVRSSNNL GPVLPPTNVG SNTYGKRNVA EDPNRESLDF LLL //