Reviewed,
UniProtKB/Swiss-Prot P12969 (IAPP_RAT)
Last modified
February 9, 2010.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Islet amyloid polypeptide Alternative name(s): Amylin Diabetes-associated peptide Short name=DAP | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 93 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism By similarity. |
| Subunit structure | Interacts with IDE and INS By similarity. |
| Subcellular location | |
| Tissue specificity | Abundant in the islets of Langerhans but is not present in the brain or seven other tissues examined. |
| Domain | The mature protein is largely unstructured in the absence of a cognate ligand, but contrary to the human protein, it does not easily form fibrillar aggregates. Ref.7 |
| Sequence similarities | Belongs to the calcitonin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Amyloid Secreted |
| Domain | Signal |
| Molecular function | Hormone |
| PTM | Amidation Cleavage on pair of basic residues Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Traceable author statement. Source: RGD |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Ref.1Traceable author statement. Source: RGD |
| Molecular function | hormone activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||
Molecule processing | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | |||||||||
| Propeptide | 24 – 35 | 12 | PRO_0000004121 | |||||||||
| Peptide | 38 – 74 | 37 | Islet amyloid polypeptide Ref.4 Ref.5 | PRO_0000004122 | ||||||||
| Propeptide | 78 – 93 | 16 | PRO_0000004123 | |||||||||
Amino acid modifications | ||||||||||||
| Modified residue | 74 | 1 | Tyrosine amide Ref.4 | |||||||||
| Disulfide bond | 39 ↔ 44 | Ref.8 | ||||||||||
Secondary structure | ||||||||||||
Helix Strand Turn | ||||||||||||
| Helix | 42 – 54 | 13 | ||||||||||
| Helix | 55 – 58 | 4 | ||||||||||
Sequences
References
| [1] | "Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone." Nishi M., Chan S.J., Nagamatsu S., Bell G.I., Steiner D.F. Proc. Natl. Acad. Sci. U.S.A. 86:5738-5742(1989) [PubMed: 2668946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Rat amylin: cloning and tissue-specific expression in pancreatic islets." Leffert J.D., Newgard C.B., Okamoto H., Milburn J.L., Luskey K.L. Proc. Natl. Acad. Sci. U.S.A. 86:3127-3130(1989) [PubMed: 2654937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man." van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S. Biochim. Biophys. Acta 1087:235-240(1990) [PubMed: 2223885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WAP. Tissue: Liver. |
| [4] | "Isolation and sequence determination of rat islet amyloid polypeptide." Asai J., Nakazato M., Kangawa K., Matsukura S., Matsuo H. Biochem. Biophys. Res. Commun. 164:400-405(1989) [PubMed: 2679555] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-74. |
| [5] | "Regional distribution and molecular forms of rat islet amyloid polypeptide." Asai J., Nakazato M., Miyazato M., Kangawa K., Matsuo H., Matsukura S. Biochem. Biophys. Res. Commun. 169:788-795(1990) [PubMed: 2357234] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-74. |
| [6] | "Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species." Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., Johnson K.H., Westermark P. FEBS Lett. 251:261-264(1989) [PubMed: 2666169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-74. |
| [7] | "Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding." Jiang P., Xu W., Mu Y. PLoS Comput. Biol. 5:E1000357-E1000357(2009) [PubMed: 19360098] [Abstract] Cited for: DOMAIN. |
| [8] | "Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy." Nanga R.P., Brender J.R., Xu J., Hartman K., Subramanian V., Ramamoorthy A. J. Am. Chem. Soc. 131:8252-8261(2009) [PubMed: 19456151] [Abstract] Cited for: STRUCTURE BY NMR OF 38-74, DISULFIDE BOND. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M25390 mRNA. Translation: AAA41359.1. J04544 mRNA. Translation: AAA40730.1. X52820, X52821 Genomic DNA. Translation: CAA37003.1. | ||||||||||||
| IPI | IPI00202679. | ||||||||||||
| PIR | TCRTIA. S13566. | ||||||||||||
| RefSeq | NP_036718.1. | ||||||||||||
| UniGene | Rn.11394 | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | P12969. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000016614; ENSRNOP00000016614; ENSRNOG00000012417; Rattus norvegicus. [Genome view] | ||||||||||||
| GeneID | 24476. | ||||||||||||
| KEGG | rno:24476. | ||||||||||||
| UCSC | NM_012586. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 24476. | ||||||||||||
| RGD | 2854. Iapp. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | roNOG17456. | ||||||||||||
| HOVERGEN | P12969. | ||||||||||||
| InParanoid | P12969. | ||||||||||||
| OMA | VEKRKCN. | ||||||||||||
| OrthoDB | EOG9F4VX1. | ||||||||||||
| PhylomeDB | P12969. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P12969. | ||||||||||||
| Genevestigator | P12969. | ||||||||||||
| GermOnline | ENSRNOG00000012417. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR018360. Calcitonin_CS. IPR001693. Calcitonin_peptide-like. IPR000443. Pro-islet_amyloid_polypep. IPR021117. Procalcitonin-like. IPR021116. Procalcitonin/adrenomedullin. [Graphical view] | ||||||||||||
| PANTHER | PTHR10505. Calcitonin-like. 1 hit. PTHR10505:SF4. Pro-islet_amyloid_polypep. 1 hit. | ||||||||||||
| Pfam | PF00214. Calc_CGRP_IAPP. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00818. ISLETAMYLOID. | ||||||||||||
| SMART | SM00113. CALCITONIN. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00258. CALCITONIN. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 603429. | ||||||||||||
Entry information
| Entry name | IAPP_RAT | ||||||||
| Accession | Primary (citable) accession number: P12969 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


