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P22062 (PIMT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase

Short name=PIMT
EC=2.1.1.77
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl/D-aspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Gene names
Name:Pcmt1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasm.

Sequence similarities

Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.

Sequence caution

The sequence BAA02034.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 227226Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PRO_0000111878

Sites

Active site601 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict831L → P in AAA60742. Ref.1
Sequence conflict831L → P in BAA02034. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22062 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 833498527365E24F

FASTA22724,641
        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 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26686 mRNA. Translation: AAA60742.1.
D11475 mRNA. Translation: BAA02034.1. Different initiation.
BC088417 mRNA. Translation: AAH88417.1.
IPIIPI00555303.
PIRA32449.
RefSeqNP_037205.2. NM_013073.3.
UniGeneRn.86985.

3D structure databases

ProteinModelPortalP22062.
SMRP22062. Positions 3-226.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4589251.
STRINGP22062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25604.
KEGGrno:25604.

Organism-specific databases

CTD5110.
RGD3268. Pcmt1.

Phylogenomic databases

eggNOGroNOG07095.
GeneTreeENSGT00510000046974.
HOVERGENHBG004483.
InParanoidP22062.
OrthoDBEOG4NGGNK.

Gene expression databases

ArrayExpressP22062.
GenevestigatorP22062.
GermOnlineENSRNOG00000014330. Rattus norvegicus.

Family and domain databases

InterProIPR000682. PCMT.
[Graphical view]
KOK00573.
PANTHERPTHR11579. PCMT. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. Pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607327.

Entry information

Entry namePIMT_RAT
AccessionPrimary (citable) accession number: P22062
Secondary accession number(s): Q5M7V6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families