PLMT_ARATH
ID PLMT_ARATH Reviewed; 164 AA.
AC Q9SAH5; Q8GWP8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphatidyl-N-methylethanolamine N-methyltransferase {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=PLMT; OrderedLocusNames=At1g80860; ORFNames=F23A5.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-164.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19366698; DOI=10.1074/jbc.m109.005991;
RA Keogh M.R., Courtney P.D., Kinney A.J., Dewey R.E.;
RT "Functional characterization of phospholipid N-methyltransferases from
RT Arabidopsis and soybean.";
RL J. Biol. Chem. 284:15439-15447(2009).
CC -!- FUNCTION: Catalyzes the second two steps of the methylation pathway of
CC phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC phosphatidylmonomethylethanolamine (PMME) to
CC phosphatidyldimethylethanolamine (PDME) and of PDME to
CC phosphatidylcholine (PC). {ECO:0000255|HAMAP-Rule:MF_03216,
CC ECO:0000269|PubMed:19366698}.
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 -!- 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}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19366698}.
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=BAC43303.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011713; AAF14673.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36459.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36460.1; -; Genomic_DNA.
DR EMBL; BT043493; ACF88498.1; -; mRNA.
DR EMBL; AK118709; BAC43303.1; ALT_INIT; mRNA.
DR PIR; C96841; C96841.
DR RefSeq; NP_565246.1; NM_106734.2.
DR RefSeq; NP_849916.2; NM_179585.4.
DR AlphaFoldDB; Q9SAH5; -.
DR STRING; 3702.AT1G80860.1; -.
DR PaxDb; Q9SAH5; -.
DR PRIDE; Q9SAH5; -.
DR ProteomicsDB; 235068; -.
DR EnsemblPlants; AT1G80860.1; AT1G80860.1; AT1G80860.
DR EnsemblPlants; AT1G80860.2; AT1G80860.2; AT1G80860.
DR GeneID; 844425; -.
DR Gramene; AT1G80860.1; AT1G80860.1; AT1G80860.
DR Gramene; AT1G80860.2; AT1G80860.2; AT1G80860.
DR KEGG; ath:AT1G80860; -.
DR Araport; AT1G80860; -.
DR TAIR; locus:2025707; AT1G80860.
DR eggNOG; ENOG502S2X5; Eukaryota.
DR HOGENOM; CLU_111785_0_0_1; -.
DR InParanoid; Q9SAH5; -.
DR OMA; FYYWLWT; -.
DR OrthoDB; 1395721at2759; -.
DR PhylomeDB; Q9SAH5; -.
DR BioCyc; ARA:AT1G80860-MON; -.
DR BRENDA; 2.1.1.71; 399.
DR UniPathway; UPA00753; -.
DR PRO; PR:Q9SAH5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAH5; baseline and differential.
DR Genevisible; Q9SAH5; AT.
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:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:TAIR.
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.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..164
FT /note="Phosphatidyl-N-methylethanolamine N-
FT methyltransferase"
FT /id="PRO_0000425530"
FT INTRAMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 22..30
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 53..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 91..131
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT TOPO_DOM 152..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 74..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
FT BINDING 154..155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03216"
SQ SEQUENCE 164 AA; 18819 MW; 348A1D237A8E1709 CRC64;
MGLLAAIGVL LPFPFYWWLW TNAQSWVNLC GRERDPSTVM ARVSHVLKAA QLLSLFSVAS
LSWPPPLYFW PLMAFGQFLN FRVYQLLGEA GTYYGVRFGK NIPWVTEFPF GVIRDPQYVG
SIMSLLACLS WVPFQYILLW SLGYVFMMFL ESKEDPNARA KSIS
