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UniProtKB/Swiss-Prot entry P22062


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIMT_RAT
Primary accession number P22062
Secondary accession number Q5M7V6
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Synonyms PIMT
EC 2.1.1.77
Protein-beta-aspartate methyltransferase
Protein L-isoaspartyl/D-aspartyl methyltransferase
L-isoaspartyl protein carboxyl methyltransferase
Gene name
Name: Pcmt1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/0006-291X(89)91602-1; PubMed=2730663 [NCBI, ExPASy, EBI, Israel, Japan]
Sato M., Yoshida T., Tuboi S.;
"Primary structure of rat brain protein carboxyl methyltransferase deduced from cDNA sequence.";
Biochem. Biophys. Res. Commun. 161:342-347(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8263531 [NCBI, ExPASy, EBI, Israel, Japan]
Mizobuchi M., Murao K., Takeda R., Kakimoto Y.;
"Tissue-specific expression of isoaspartyl protein carboxyl methyltransferase gene in rat brain and testis.";
J. Neurochem. 62:322-328(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 5-18; 28-37; 82-98; 106-135; 179-197 AND 205-219, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
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: Monomer.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M26686; AAA60742.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D11475; BAA02034.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC088417; AAH88417.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32449; A32449.
RefSeq NP_037205.2; -.
UniGene Rn.86985
3D structure databases
HSSP P22061; 1I1N. [HSSP ENTRY / PDB]
SMR P22062; 3-226.
ModBase P22062.
Organism-specific databases
RGD 3268; Pcmt1.
Gene expression databases
ArrayExpress P22062; -.
GermOnline ENSRNOG00000014330; Rattus norvegicus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004719; Molecular function: protein-L-isoaspartate (D-aspartate) O-methyltransferase activity (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000682; PCMT.
Graphical view of domain structure.
PANTHER PTHR11579; PCMT; 1.
Pfam PF01135; PCMT; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00080; pimt; 1.
PROSITE PS01279; PCMT; 1.
ProtoNet P22062.
Genome annotation databases
Ensembl ENSRNOG00000014330; Rattus norvegicus. [Contig view]
GeneID 25604; -.
KEGG rno:25604; -.
Phylogenomic databases
HOVERGEN P22062; -.
Other
NextBio 607327; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   227  226     Protein-L-isoaspartate(D-aspartate) O-methyltransferase. PRO_0000111878
ACT_SITE   60    60        By similarity. 
MOD_RES   2     2        N-acetylalanine (By similarity). 
CONFLICT   83    83        L -> P (in Ref. 1; AAA60742 and 2; BAA02034). 
Sequence information
Length: 227 AA [This is the length of the unprocessed precursor] Molecular weight: 24641 Da [This is the MW of the unprocessed precursor] CRC64: 833498527365E24F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKSNPYMDSP QSIGFQATIS 

        70         80         90        100        110        120 
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GHSGKVIGID HIKELVDDSI 

       130        140        150        160        170        180 
TNVKKDDPML LSSGRVRLVV GDGRMGFAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI 

       190        200        210        220 
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK 

P22062 in FASTA format

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