L8YCQ4 · L8YCQ4_TUPCH
- ProteinPhosphatidylethanolamine N-methyltransferase
- GenePEMT
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids225 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure. Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H+
Pathway
Lipid metabolism.
Phospholipid metabolism; phosphatidylcholine biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | mitochondrial membrane | |
Molecular Function | phosphatidyl-N-methylethanolamine N-methyltransferase activity | |
Molecular Function | phosphatidylethanolamine N-methyltransferase activity | |
Biological Process | methylation | |
Biological Process | phosphatidylcholine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylethanolamine N-methyltransferase
- EC number
- Short namesPEAMT ; PEMT
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Scandentia > Tupaiidae > Tupaia
Accessions
- Primary accessionL8YCQ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Mitochondrion membrane ; Multi-pass membrane protein
Note: Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria.
Features
Showing features for topological domain, intramembrane, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-38 | Lumenal | ||||
Sequence: MSSSAAGPDCCGGLGNIDFRKADLCVMTRLLGYVDLWE | ||||||
Intramembrane | 39-59 | Helical | ||||
Sequence: PRFVAAVLATAFNPLFWNVVA | ||||||
Transmembrane | 41-58 | Helical | ||||
Sequence: FVAAVLATAFNPLFWNVV | ||||||
Topological domain | 60-71 | Lumenal | ||||
Sequence: RWEHRTRKLSRA | ||||||
Topological domain | 93-119 | Cytoplasmic | ||||
Sequence: RSHCFTQAMLSQPQMESLDNPTAYRLG | ||||||
Transmembrane | 120-145 | Helical | ||||
Sequence: LAFLGVGVVLVLSSFFALGFTGTFLG | ||||||
Topological domain | 141-183 | Lumenal | ||||
Sequence: GTFLGDYFGILKEARVTSFPFNVLDNPMYWGSTANYLGWALMH | ||||||
Transmembrane | 188-205 | Helical | ||||
Sequence: GLLLAAVVGLIYMVAILY | ||||||
Topological domain | 205-225 | Cytoplasmic | ||||
Sequence: YEEPFTTEIYQRKASESHRRS |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length225
- Mass (Da)24,967
- Last updated2013-04-03 v1
- ChecksumF5D7ADD1E92FC1C0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB359564 EMBL· GenBank· DDBJ | ELV14007.1 EMBL· GenBank· DDBJ | Genomic DNA |