Reviewed, UniProtKB/Swiss-Prot P22062 (PIMT_RAT)

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

Name:

Pcmt1

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	Cytoplasm.
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.2 Inferred 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

	Sequence		Length	Mass (Da)
	P22062-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 833498527365E24F	FASTA	227	24,641
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)