PEMT_BOVIN
ID PEMT_BOVIN Reviewed; 199 AA.
AC Q7YRH6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03216};
DE EC=2.1.1.71 {ECO:0000255|HAMAP-Rule:MF_03216};
DE AltName: Full=Phospholipid methyltransferase {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PLMT {ECO:0000255|HAMAP-Rule:MF_03216};
GN Name=PEMT {ECO:0000255|HAMAP-Rule:MF_03216}; Synonyms=PEMT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou G., Yu L., Zhao S.;
RT "Cloning of Bos taurus pemt2.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC pathway of phosphatidylcholine biosynthesis, the SAM-dependent
CC methylation of phosphatidylethanolamine (PE) to
CC phosphatidylmonomethylethanolamine (PMME), PMME to
CC phosphatidyldimethylethanolamine (PDME), and PDME to
CC phosphatidylcholine (PC). {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S-
CC adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S-
CC adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; EC=2.1.1.71;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03216};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46112, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85679,
CC ChEBI:CHEBI:85680; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46113;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + S-
CC adenosyl-L-methionine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70619, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74986, ChEBI:CHEBI:85679;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70620;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70623, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:85680; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70624;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N-methylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70739, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:172403,
CC ChEBI:CHEBI:189848; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70740;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:189848,
CC ChEBI:CHEBI:189849; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70744;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70747, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:42027, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189849; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70748;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphoethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N-methylethanolamine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70751, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:189858,
CC ChEBI:CHEBI:189859; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70752;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N-
CC methylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phospho-N,N-dimethylethanolamine +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:70755,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:189859, ChEBI:CHEBI:189860;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70756;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phospho-N,N-
CC dimethylethanolamine + S-adenosyl-L-methionine = 1,2-di-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phosphocholine + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:70759, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:86161,
CC ChEBI:CHEBI:189860; Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70760;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:78261, ChEBI:CHEBI:189861;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70764;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N-methylethanolamine + S-adenosyl-L-methionine = 1-
CC hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phospho-N,N-dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:189861, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70768;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phospho-N,N-dimethylethanolamine + S-adenosyl-L-methionine
CC = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:70771, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:74963, ChEBI:CHEBI:189862;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70772;
CC Evidence={ECO:0000250|UniProtKB:Q08388};
CC -!- ACTIVITY REGULATION: The first methylation is rate-limiting.
CC {ECO:0000250}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane
CC {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum
CC where most PEMT activity is generated and in mitochondria.
CC {ECO:0000255|HAMAP-Rule:MF_03216}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|HAMAP-
CC Rule:MF_03216}.
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DR EMBL; AY334572; AAQ01191.1; -; mRNA.
DR EMBL; BC105466; AAI05467.1; -; mRNA.
DR RefSeq; NP_892034.1; NM_182989.3.
DR AlphaFoldDB; Q7YRH6; -.
DR STRING; 9913.ENSBTAP00000041140; -.
DR PaxDb; Q7YRH6; -.
DR Ensembl; ENSBTAT00000043580; ENSBTAP00000041140; ENSBTAG00000016432.
DR GeneID; 360197; -.
DR KEGG; bta:360197; -.
DR CTD; 10400; -.
DR VEuPathDB; HostDB:ENSBTAG00000016432; -.
DR VGNC; VGNC:32745; PEMT.
DR eggNOG; KOG4142; Eukaryota.
DR GeneTree; ENSGT00390000007041; -.
DR InParanoid; Q7YRH6; -.
DR OMA; VITSTWA; -.
DR OrthoDB; 1395721at2759; -.
DR UniPathway; UPA00753; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000016432; Expressed in corpus epididymis and 107 other tissues.
DR ExpressionAtlas; Q7YRH6; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_03216; PLMT; 1.
DR InterPro; IPR024960; PEMT/MFAP.
DR InterPro; IPR007318; Phopholipid_MeTrfase.
DR PANTHER; PTHR15458; PTHR15458; 1.
DR Pfam; PF04191; PEMT; 1.
DR PIRSF; PIRSF005444; PEMT; 1.
DR PROSITE; PS51599; SAM_PEMT_PEM2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Mitochondrion; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..199
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000281924"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT INTRAMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 34..45
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 67..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 115..157
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 179..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 98..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 180..181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 199 AA; 22018 MW; E6F91D9AF795B2CC CRC64;
MTRLLGYVDL SEPHFVAAVL AIVFNPLFWN VVARWEHKTR KLSKAFGSPR LACYTLGGAI
LLLNVLRSHC FTQAMLSQPR MQSLDNPAVY HVGLALLGVG GVFVLSSFLA LGFTGTFLGD
YFGILKEARV TMFPFSVLDN PMYWGSTAIY LGWAIVHASP TGLLLTALVA LIYMVAIVYE
EPFTAEIYQQ KASQAYKRS
