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Q08388 (PEMT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. 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:
Phosphatidylethanolamine N-methyltransferase

Short name=PEAMT
Short name=PEMT
EC=2.1.1.17
Gene names
Name:Pemt
Synonyms:Pempt
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes three sequential methylation of phosphatidylethanolamine (PE) by AdoMet, thus producing phosphatidylcholine (PC).

Catalytic activity

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Mitochondrion membrane; Multi-pass membrane protein Potential.

Tissue specificity

Liver.

Sequence similarities

Belongs to the PEMT/PEM2 methyltransferase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
   DomainTransmembrane
Transmembrane helix
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processS-adenosylhomocysteine metabolic process

Inferred from direct assay Ref.1. Source: RGD

S-adenosylmethionine metabolic process

Inferred from direct assay Ref.1. Source: RGD

negative regulation of cell proliferation

Inferred from mutant phenotype. Source: RGD

phosphatidylcholine biosynthetic process

Inferred from direct assay Ref.1. Source: RGD

positive regulation of lipoprotein metabolic process

Inferred from mutant phenotype. Source: RGD

response to amino acid stimulus

Inferred from expression pattern. Source: RGD

response to drug

Inferred from direct assay. Source: RGD

response to ethanol

Inferred from expression pattern. Source: RGD

response to vitamin

Inferred from direct assay. Source: RGD

   Cellular componentbrush border membrane

Inferred from direct assay. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fraction

Inferred from direct assay Ref.1. Source: RGD

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay. Source: RGD

   Molecular functionphosphatidylethanolamine N-methyltransferase activity

Inferred from direct assay Ref.1. Source: RGD

phosphatidylethanolamine binding

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 199198Phosphatidylethanolamine N-methyltransferase
PRO_0000193922

Regions

Transmembrane13 – 3321Helical; Potential
Transmembrane46 – 6621Helical; Potential
Transmembrane91 – 11121Helical; Potential
Transmembrane159 – 17921Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q08388 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8F1A938ED883B0FA

FASTA19922,486
        10         20         30         40         50         60 
MSWLLGYVDP TEPSFVAAVL TIVFNPLFWN VVARWEQRTR KLSRAFGSPY LACYSLGSII 

        70         80         90        100        110        120 
LLLNILRSHC FTQAMMSQPK MEGLDSHTIY FLGLALLGWG LVFVLSSFYA LGFTGTFLGD 

       130        140        150        160        170        180 
YFGILKESRV TTFPFSVLDN PMYWGSTANY LGWALMHASP TGLLLTVLVA LVYVVALLFE 

       190 
EPFTAEIYRR KATRLHKRS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a novel phosphatidylethanolamine N-methyltransferase. A specific biochemical and cytological marker for a unique membrane fraction in rat liver."
Cui Z., Vance J.E., Chen M.H., Voelker D.R., Vance D.E.
J. Biol. Chem. 268:16655-16663(1993) [PubMed: 8344945] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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: Liver.
[3]Ridgway N.D.
Thesis (1988), University of British Columbia, Canada
Cited for: PROTEIN SEQUENCE OF 2-31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14441 mRNA. Translation: AAA03154.1.
BC091162 mRNA. Translation: AAH91162.1.
IPIIPI00231668.
PIRA47353.
RefSeqNP_037135.1. NM_013003.1.
UniGeneRn.9875.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ08388.

Proteomic databases

PRIDEQ08388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25511.
KEGGrno:25511.

Organism-specific databases

CTD10400.
RGD3297. Pemt.

Phylogenomic databases

GeneTreeENSGT00390000007041.
HOVERGENHBG000990.
OrthoDBEOG4V9TRP.
PhylomeDBQ08388.

Gene expression databases

GenevestigatorQ08388.

Family and domain databases

InterProIPR007318. PEMT.
[Graphical view]
KOK00551.
PANTHERPTHR15458. PEMT. 1 hit.
PfamPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFPIRSF005444. PEMT. 1 hit.
ProtoNetSearch...

Other

NextBio606945.

Entry information

Entry namePEMT_RAT
AccessionPrimary (citable) accession number: Q08388
Secondary accession number(s): Q5BK89
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 72 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