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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

Pemt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidyl-N-dimethylethanolamine = S-adenosyl-L-homocysteine + phosphatidylcholine.PROSITE-ProRule annotation
S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.PROSITE-ProRule annotation

Pathwayi: phosphatidylcholine biosynthesis

This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

  • glycerophospholipid metabolic process Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • phosphatidylcholine biosynthetic process Source: RGD
  • positive regulation of lipoprotein metabolic process Source: RGD
  • positive regulation of protein targeting to mitochondrion Source: Ensembl
  • response to amino acid Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to nutrient Source: RGD
  • response to vitamin Source: RGD
  • S-adenosylhomocysteine metabolic process Source: RGD
  • S-adenosylmethionine metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16675.
BRENDAi2.1.1.17. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.
UniPathwayiUPA00753.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine N-methyltransferase (EC:2.1.1.17, EC:2.1.1.71)
Short name:
PEAMT
Short name:
PEMT
Gene namesi
Name:Pemt
Synonyms:Pempt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi3297. Pemt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211LumenalSequence analysisAdd
BLAST
Intramembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 4512LumenalSequence analysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence analysisAdd
BLAST
Topological domaini67 – 9024CytoplasmicSequence analysisAdd
BLAST
Transmembranei91 – 11121HelicalSequence analysisAdd
BLAST
Topological domaini112 – 15847LumenalSequence analysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence analysisAdd
BLAST
Topological domaini180 – 19920CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • brush border membrane Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • mitochondrial membrane Source: UniProtKB-SubCell
  • sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 199198Phosphatidylethanolamine N-methyltransferasePRO_0000193922Add
BLAST

Proteomic databases

PaxDbiQ08388.
PRIDEiQ08388.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

GenevisibleiQ08388. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4568090.
STRINGi10116.ENSRNOP00000004488.

Family & Domainsi

Sequence similaritiesi

Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4142. Eukaryota.
ENOG4111HY0. LUCA.
GeneTreeiENSGT00390000007041.
HOVERGENiHBG000990.
InParanoidiQ08388.
KOiK00551.
PhylomeDBiQ08388.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08388-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWLLGYVDP TEPSFVAAVL TIVFNPLFWN VVARWEQRTR KLSRAFGSPY
60 70 80 90 100
LACYSLGSII LLLNILRSHC FTQAMMSQPK MEGLDSHTIY FLGLALLGWG
110 120 130 140 150
LVFVLSSFYA LGFTGTFLGD YFGILKESRV TTFPFSVLDN PMYWGSTANY
160 170 180 190
LGWALMHASP TGLLLTVLVA LVYVVALLFE EPFTAEIYRR KATRLHKRS
Length:199
Mass (Da):22,486
Last modified:January 23, 2007 - v2
Checksum:i8F1A938ED883B0FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14441 mRNA. Translation: AAA03154.1.
BC091162 mRNA. Translation: AAH91162.1.
PIRiA47353.
RefSeqiNP_037135.1. NM_013003.1.
UniGeneiRn.9875.

Genome annotation databases

EnsembliENSRNOT00000083698; ENSRNOP00000074801; ENSRNOG00000054423.
GeneIDi25511.
KEGGirno:25511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14441 mRNA. Translation: AAA03154.1.
BC091162 mRNA. Translation: AAH91162.1.
PIRiA47353.
RefSeqiNP_037135.1. NM_013003.1.
UniGeneiRn.9875.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4568090.
STRINGi10116.ENSRNOP00000004488.

Proteomic databases

PaxDbiQ08388.
PRIDEiQ08388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083698; ENSRNOP00000074801; ENSRNOG00000054423.
GeneIDi25511.
KEGGirno:25511.

Organism-specific databases

CTDi10400.
RGDi3297. Pemt.

Phylogenomic databases

eggNOGiKOG4142. Eukaryota.
ENOG4111HY0. LUCA.
GeneTreeiENSGT00390000007041.
HOVERGENiHBG000990.
InParanoidiQ08388.
KOiK00551.
PhylomeDBiQ08388.

Enzyme and pathway databases

UniPathwayiUPA00753.
BioCyciMetaCyc:MONOMER-16675.
BRENDAi2.1.1.17. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.

Miscellaneous databases

NextBioi606945.
PROiQ08388.

Gene expression databases

GenevisibleiQ08388. RN.

Family and domain databases

InterProiIPR024960. PEMT/MFAP.
IPR007318. Phopholipid_MeTrfase.
[Graphical view]
PANTHERiPTHR15458. PTHR15458. 1 hit.
PfamiPF04191. PEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF005444. PEMT. 1 hit.
PROSITEiPS51599. SAM_PEMT_PEM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiPEMT_RAT
AccessioniPrimary (citable) accession number: Q08388
Secondary accession number(s): Q5BK89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.