PEMT_MOUSE
ID PEMT_MOUSE Reviewed; 199 AA.
AC Q61907; Q3UZN8; Q7TNW6; Q8R0I1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000303|PubMed:9371769};
DE Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03216};
DE Short=PEMT {ECO:0000303|PubMed:12482759, ECO:0000303|PubMed:9371769};
DE EC=2.1.1.17 {ECO:0000305|PubMed:9371769};
DE EC=2.1.1.71 {ECO:0000305|PubMed:9371769};
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=Pempt, Pemt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/J; TISSUE=Liver;
RX PubMed=8978486;
RA Walkey C.J., Cui Z., Agellon L.B., Vance D.E.;
RT "Characterization of the murine phosphatidylethanolamine N-
RT methyltransferase-2 gene.";
RL J. Lipid Res. 37:2341-2350(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Zhou G., Yu L., Zhao S.;
RT "Cloning of Mus musculus phosphatidylethanolamine N-methyltransferase
RT (Pemt).";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=9371769; DOI=10.1073/pnas.94.24.12880;
RA Walkey C.J., Donohue L.R., Bronson R., Agellon L.B., Vance D.E.;
RT "Disruption of the murine gene encoding phosphatidylethanolamine N-
RT methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12880-12885(1997).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9765216; DOI=10.1074/jbc.273.42.27043;
RA Walkey C.J., Yu L., Agellon L.B., Vance D.E.;
RT "Biochemical and evolutionary significance of phospholipid methylation.";
RL J. Biol. Chem. 273:27043-27046(1998).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12482759; DOI=10.1074/jbc.m212194200;
RA Noga A.A., Stead L.M., Zhao Y., Brosnan M.E., Brosnan J.T., Vance D.E.;
RT "Plasma homocysteine is regulated by phospholipid methylation.";
RL J. Biol. Chem. 278:5952-5955(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the three sequential steps of the methylation
CC pathway for the biosynthesis of phosphatidylcholine, a critical and
CC essential component for membrane structure (PubMed:9371769) (Probable).
CC Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as
CC the methyl group donor for the methylation of phosphatidylethanolamine
CC (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to
CC phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-
CC methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine
CC (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and
CC PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine,
CC PC), producing S-adenosyl-L-homocysteine in each step (PubMed:9371769).
CC {ECO:0000269|PubMed:9371769, ECO:0000305|PubMed:9765216}.
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:0000305|PubMed:9371769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32736;
CC Evidence={ECO:0000305|PubMed:9371769};
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:0000305|PubMed:9371769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32740;
CC Evidence={ECO:0000305|PubMed:9371769};
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:0000305|PubMed:9371769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11165;
CC Evidence={ECO:0000305|PubMed:9371769};
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-
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-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 -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC {ECO:0000305|PubMed:9371769}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBM1}; 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:0000250|UniProtKB:Q9UBM1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61907-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61907-2; Sequence=VSP_053224;
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000305|PubMed:9371769, ECO:0000305|PubMed:9765216}.
CC -!- DISRUPTION PHENOTYPE: Severe liver pathology rapidly occurs in knockout
CC mice after 3-days withdrawal of dietary choline, which might occur
CC during starvation, pregnancy or lactation, and may die after 4-5 days
CC (PubMed:9765216). Homocysteine plasma content in knockouts is 50
CC percent less of the content in wild type mice (PubMed:12482759).
CC {ECO:0000269|PubMed:12482759, ECO:0000269|PubMed:9765216}.
CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC superfamily. PEMT/PEM2 methyltransferase family. {ECO:0000255|HAMAP-
CC Rule:MF_03216}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ01190.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U25051; AAA67686.1; -; Genomic_DNA.
DR EMBL; U25046; AAA67686.1; JOINED; Genomic_DNA.
DR EMBL; U25047; AAA67686.1; JOINED; Genomic_DNA.
DR EMBL; U25048; AAA67686.1; JOINED; Genomic_DNA.
DR EMBL; U25049; AAA67686.1; JOINED; Genomic_DNA.
DR EMBL; U25050; AAA67686.1; JOINED; Genomic_DNA.
DR EMBL; AY334571; AAQ01190.1; ALT_FRAME; mRNA.
DR EMBL; AK133744; BAE21818.1; -; mRNA.
DR EMBL; AL603710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026796; AAH26796.1; -; mRNA.
DR CCDS; CCDS24782.1; -. [Q61907-1]
DR CCDS; CCDS78957.1; -. [Q61907-2]
DR RefSeq; NP_001276940.1; NM_001290011.1. [Q61907-2]
DR RefSeq; NP_001276941.1; NM_001290012.1. [Q61907-1]
DR RefSeq; NP_001276942.1; NM_001290013.1. [Q61907-1]
DR RefSeq; NP_001276943.1; NM_001290014.1.
DR RefSeq; NP_032845.2; NM_008819.3. [Q61907-1]
DR AlphaFoldDB; Q61907; -.
DR IntAct; Q61907; 2.
DR MINT; Q61907; -.
DR STRING; 10090.ENSMUSP00000099753; -.
DR SwissPalm; Q61907; -.
DR jPOST; Q61907; -.
DR MaxQB; Q61907; -.
DR PaxDb; Q61907; -.
DR PRIDE; Q61907; -.
DR ProteomicsDB; 288124; -. [Q61907-1]
DR ProteomicsDB; 288125; -. [Q61907-2]
DR Antibodypedia; 25461; 183 antibodies from 24 providers.
DR DNASU; 18618; -.
DR Ensembl; ENSMUST00000000310; ENSMUSP00000000310; ENSMUSG00000000301. [Q61907-1]
DR Ensembl; ENSMUST00000102692; ENSMUSP00000099753; ENSMUSG00000000301. [Q61907-1]
DR Ensembl; ENSMUST00000102693; ENSMUSP00000099754; ENSMUSG00000000301. [Q61907-2]
DR GeneID; 18618; -.
DR KEGG; mmu:18618; -.
DR UCSC; uc007jfi.2; mouse. [Q61907-1]
DR UCSC; uc007jfj.2; mouse. [Q61907-2]
DR CTD; 10400; -.
DR MGI; MGI:104535; Pemt.
DR VEuPathDB; HostDB:ENSMUSG00000000301; -.
DR eggNOG; KOG4142; Eukaryota.
DR GeneTree; ENSGT00390000007041; -.
DR HOGENOM; CLU_086119_0_1_1; -.
DR InParanoid; Q61907; -.
DR OMA; VITSTWA; -.
DR OrthoDB; 1395721at2759; -.
DR TreeFam; TF300198; -.
DR BRENDA; 2.1.1.17; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR UniPathway; UPA00753; -.
DR BioGRID-ORCS; 18618; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pemt; mouse.
DR PRO; PR:Q61907; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61907; protein.
DR Bgee; ENSMUSG00000000301; Expressed in morula and 95 other tissues.
DR ExpressionAtlas; Q61907; baseline and differential.
DR Genevisible; Q61907; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; TAS:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
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:0008429; F:phosphatidylethanolamine binding; ISO:MGI.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; ISS:MGI.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IMP:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; ISO:MGI.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISS:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050747; P:positive regulation of lipoprotein metabolic process; ISO:MGI.
DR GO; GO:0033273; P:response to vitamin; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; ISO:MGI.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Methyltransferase; Mitochondrion;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..199
FT /note="Phosphatidylethanolamine N-methyltransferase"
FT /id="PRO_0000193921"
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"
FT VAR_SEQ 1
FT /note="M -> MEENTSPTTALISSSVAGHDCCGGFGNIDFRQADLFVM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053224"
FT CONFLICT 168
FT /note="L -> V (in Ref. 1; AAA67686)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Y -> N (in Ref. 1; AAA67686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22579 MW; 0F96C1CC3B483DC6 CRC64;
MSWLLGYMDP TEPSFVAAVI TIVFNPLFWN VVARWEQRTR KLSRAFGSPH LACYSLGICI
LLLNILRSHC FTQAMMSQPK MEGLDNHTTY FLGLAFLGWG FVFVLSSFYA LGFTGTFLGD
YFGILKESRV TTFPFSVLDN PMYWGSTANY LGWALMHASP TGLLLTVLVA IVYVVALLYE
EPFTAEIYRQ KATRLHKRS
