UniProt:Q9UBM1 PEMT

chain
  • chain:1-199
checksum 98C07AB54B3B4E6A
comment
  • 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).FUNCTION 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).FUNCTION Produces a higher increase in the level of PC species containing long chains with three double bonds than isoform 1.CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)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(+)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(+)CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-homocysteine + H(+)CATALYTIC ACTIVITY 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + S-adenosyl-L-homocysteine + H(+)ACTIVITY REGULATION The first methylation is rate-limiting.PATHWAY Phospholipid metabolism; phosphatidylcholine biosynthesis.INTERACTION 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).SUBCELLULAR LOCATION Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria.SUBCELLULAR LOCATION Primarily expressed in liver (at protein level).PTM Isoform 2 is N-glycosylated with high-mannose oligosaccharides.SIMILARITY Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.
crossReference
databaseName UniProt
dbId 61496
description
  • recommendedName: fullName evidence="15 19"Phosphatidylethanolamine N-methyltransferase shortName evidence="2"PEAMT shortName evidence="15 19"PEMT ecNumber evidence="21 24"2.1.1.17 ecNumber evidence="4 9"2.1.1.71 alternativeName: PEMT2 alternativeName: fullName evidence="2"Phospholipid methyltransferase shortName evidence="2"PLMT
displayName UniProt:Q9UBM1 PEMT
geneName
  • PEMT
  • PEMPT
  • PNMT
identifier Q9UBM1
isSequenceChanged false
keyword
  • Alternative splicing
  • Endoplasmic reticulum
  • Lipid biosynthesis
  • Lipid metabolism
  • Membrane
  • Methyltransferase
  • Mitochondrion
  • Phospholipid biosynthesis
  • Phospholipid metabolism
  • Proteomics identification
  • Reference proteome
  • S-adenosyl-L-methionine
  • Transferase
  • Transmembrane
  • Transmembrane helix
modified [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
moleculeType Protein
name
  • PEMT
otherIdentifier
  • 10400
  • 11731113_a_at
  • 207621_PM_s_at
  • 207621_s_at
  • 3747813
  • 3747814
  • 3747817
  • 3747818
  • 3747819
  • 3747820
  • 3747821
  • 3747822
  • 3747823
  • 3747825
  • 3747826
  • 3747828
  • 3747829
  • 3747831
  • 3747855
  • 3747857
  • 3747859
  • 3747861
  • 3747862
  • 3747863
  • 39787_at
  • 8013120
  • A_23_P163955
  • GE53759
  • GO:0000773
  • GO:0001835
  • GO:0004608
  • GO:0005515
  • GO:0005739
  • GO:0005783
  • GO:0005789
  • GO:0005829
  • GO:0006629
  • GO:0006656
  • GO:0006686
  • GO:0008168
  • GO:0008654
  • GO:0008757
  • GO:0016020
  • GO:0016740
  • GO:0031966
  • GO:0032259
  • GO:0120162
  • HMNXSV003027881
  • ILMN_1689116
  • ILMN_1727855
  • ILMN_1745806
  • ILMN_1803402
  • PH_hs_0001418
  • g6005827_3p_a_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • PEMT_HUMAN
  • A8MZ66
  • B4DY41
  • D3DXC3
  • Q6IAQ5
  • Q86VL3
  • Q9BW86
  • Q9UHY6
  • Q9Y6V9
sequenceLength 199
species [Species:48887] Homo sapiens
stId uniprot:Q9UBM1
url http://purl.uniprot.org/uniprot/Q9UBM1
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