Reviewed,
UniProtKB/Swiss-Prot P22062 (PIMT_RAT)
Last modified
June 16, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein-L-isoaspartate(D-aspartate) O-methyltransferase Short name=PIMT EC=2.1.1.77 Alternative name(s): Protein-beta-aspartate methyltransferase Protein L-isoaspartyl/D-aspartyl methyltransferase L-isoaspartyl protein carboxyl methyltransferase | ||
| 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 | 227 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 | Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein By similarity. |
| Catalytic activity | S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | S-adenosylhomocysteine metabolic process Ref.2 Inferred from direct assay. Source: RGD S-adenosylmethionine metabolic process Ref.2Inferred from direct assay. Source: RGD |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Ref.2 Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 227 | 226 | Protein-L-isoaspartate(D-aspartate) O-methyltransferase | PRO_0000111878 | |||||
Sites | |||||||||
| Active site | 60 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 83 | 1 | L → P in AAA60742. Ref.1 | ||||||
| Sequence conflict | 83 | 1 | L → P in BAA02034. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary structure of rat brain protein carboxyl methyltransferase deduced from cDNA sequence." Sato M., Yoshida T., Tuboi S. Biochem. Biophys. Res. Commun. 161:342-347(1989) [PubMed: 2730663] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [2] | "Tissue-specific expression of isoaspartyl protein carboxyl methyltransferase gene in rat brain and testis." Mizobuchi M., Murao K., Takeda R., Kakimoto Y. J. Neurochem. 62:322-328(1994) [PubMed: 8263531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung. |
| [4] | Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 5-18; 28-37; 82-98; 106-135; 179-197 AND 205-219, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| M26686 mRNA. Translation: AAA60742.1. D11475 mRNA. Translation: BAA02034.1. Different initiation. BC088417 mRNA. Translation: AAH88417.1. | |
| IPI | IPI00555303. |
| PIR | A32449. |
| RefSeq | NP_037205.2. |
| UniGene | Rn.86985 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1I1N based on UniProtKB P22061. |
| SMR | P22062. Positions 3-226. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000014330. Rattus norvegicus. [Contig view] |
| GeneID | 25604. |
| KEGG | rno:25604. |
Organism-specific databases | |
| RGD | 3268. Pcmt1. |
Phylogenomic databases | |
| HOVERGEN | P22062. |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.77. 248. |
Gene expression databases | |
| ArrayExpress | P22062. |
| GermOnline | ENSRNOG00000014330. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000682. PCMT. [Graphical view] |
| PANTHER | PTHR11579. PCMT. 1 hit. |
| Pfam | PF01135. PCMT. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00080. pimt. 1 hit. |
| PROSITE | PS01279. PCMT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 607327. |
Entry information
| Entry name | PIMT_RAT | ||||||||
| Accession | Primary (citable) accession number: P22062 Secondary accession number(s): Q5M7V6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


