PEMT
entrez
10400
canonical
uniprot
Q9UBM1
canonical
ensembl
ENSG00000133027
resolver
ensp
ENSP00000255389
resolver
ensp
ENSP00000379127
resolver
ensp
ENSP00000379128
resolver
ensp
ENSP00000379129
resolver
ensp
ENSP00000665719
resolver
genesymbol
PEMT
resolver
genesymbol_syn
PEMPT
resolver
genesymbol_syn
PNMT
resolver
hgnc
HGNC:8830
resolver
uniprot
A8MZ66
resolver
uniprot
B4DY41
resolver
uniprot
D3DXC3
resolver
uniprot
Q6IAQ5
resolver
uniprot
Q86VL3
resolver
uniprot
Q9BW86
resolver
uniprot
Q9UHY6
resolver
uniprot
Q9Y6V9
resolver
uniprot_entry
PEMT_HUMAN
resolver
uniprot_sec
A8MZ66
resolver
uniprot_sec
B4DY41
resolver
uniprot_sec
D3DXC3
resolver
uniprot_sec
Q6IAQ5
resolver
uniprot_sec
Q86VL3
resolver
uniprot_sec
Q9BW86
resolver
uniprot_sec
Q9UHY6
resolver
uniprot_sec
Q9Y6V9
resolver
activity_regulation
ACTIVITY REGULATION: The first methylation is rate-limiting.
uniprot
proteins
amino_acid_sequence
MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTILLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYEEPFTAEIYRQKASGSHKRS
uniprot
proteins
ec_number
2.1.1.17
uniprot
proteins
ec_number
2.1.1.71
uniprot
proteins
function
FUNCTION: Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure (PubMed:12431977, PubMed:15927961). 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 (PubMed:12431977, PubMed:15927961). Responsible for approximately 30% of hepatic PC with the CDP-choline pathway accounting for the other 70% (Probable). {ECO:0000269|PubMed:12431977, ECO:0000269|PubMed:15927961, ECO:0000305|PubMed:12431977}.; FUNCTION: [Isoform 1]: Catalyzes the three sequential steps of the methylation of 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine (PMME) to 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine (PDME) more efficiently than isoform 2 (PubMed:20860552). Induces increase in PC species with longer polyunsaturated chains than isoform 2 (PubMed:20860552). {ECO:0000269|PubMed:20860552}.; FUNCTION: [Isoform 2]: Produces a higher increase in the level of PC species containing long chains with three double bonds than isoform 1. {ECO:0000269|PubMed:20860552}.
uniprot
proteins
mass_dalton
22134
uniprot
proteins
mutagenesis
MUTAGEN 98; /note="G->E: Impairs binding to S-adenosyl-L-methionine."; /evidence="ECO:0000269|PubMed:12842883"; MUTAGEN 100; /note="G->D: Abolishes binding to S-adenosyl-L-methionine."; /evidence="ECO:0000269|PubMed:12842883"; MUTAGEN 180; /note="E->D: Abolishes binding to S-adenosyl-L-methionine."; /evidence="ECO:0000269|PubMed:12842883"; MUTAGEN 181; /note="E->D: Impairs binding to S-adenosyl-L-methionine."; /evidence="ECO:0000269|PubMed:12842883
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000305|PubMed:12431977}.
uniprot
proteins
post_translational_modification
PTM: Isoform 2 is N-glycosylated with high-mannose oligosaccharides. {ECO:0000269|PubMed:20860552}.
uniprot
proteins
protein_family
Class VI-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
PEMT/PEM2 methyltransferase family
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
11420179
uniprot
proteins
pubmed
12431977
uniprot
proteins
pubmed
12842883
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15927961
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17456783
uniprot
proteins
pubmed
20860552
uniprot
proteins
pubmed
9989271
uniprot
proteins
sequence_length
199
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:15927961}. Note=localized in the endoplasmic reticulum (ER) of the liver and in a lipid metabolism-rich region of the ER known as mitochondria-associated membranes (PubMed:15927961). Adopts a topography within the ER membrane that positions both termini in the cytosol (PubMed:12431977). {ECO:0000269|PubMed:12431977, ECO:0000303|PubMed:15927961}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000269|PubMed:12431977}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
uniprot
proteins
transmembrane_region
TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03216"; TRANSMEM 94..114; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03216"; TRANSMEM 158..178; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03216
uniprot
proteins