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Q4R5H0 (PIMT_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 34. 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
ORF Names:QnpA-11118
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence caution

The sequence BAE01655.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 227226Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PRO_0000253633

Sites

Active site601 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4R5H0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8EAAA2EC606402A8

FASTA22724,637
        10         20         30         40         50         60 
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AECNPYMDSP QSIGFQATIS 

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

       130        140        150        160        170        180 
NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI 

       190        200        210        220 
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK 

« Hide

References

[1]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Parietal cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB169573 mRNA. Translation: BAE01655.1. Different initiation.

3D structure databases

HSSPHSSP built from PDB template 1I1N based on UniProtKB P22061.
ProteinModelPortalQ4R5H0.
SMRQ4R5H0. Positions 3-226.
ModBaseSearch...

Proteomic databases

PRIDEQ4R5H0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004483.

Family and domain databases

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

Entry information

Entry namePIMT_MACFA
AccessionPrimary (citable) accession number: Q4R5H0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 23, 2007
Last modified: October 19, 2011
This is version 34 of the entry and version 3 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