PMT1_CAEEL
ID PMT1_CAEEL Reviewed; 475 AA.
AC Q23552; H2KZF5; Q86NB3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phosphoethanolamine N-methyltransferase 1 {ECO:0000303|PubMed:17313371};
DE Short=PEAMT-1;
DE Short=PMT-1 {ECO:0000303|PubMed:17313371};
DE EC=2.1.1.103 {ECO:0000269|PubMed:17313371};
DE AltName: Full=Methyltransf_25 domain-containing protein {ECO:0000312|EMBL:CCD68005.1};
DE AltName: Full=S-adenosyl-L-methionine:phosphoethanolamine N-methyltransferase {ECO:0000303|PubMed:17313371};
GN Name=pmt-1 {ECO:0000312|EMBL:CCD68005.1, ECO:0000312|WormBase:ZK622.3a};
GN ORFNames=ZK622.3 {ECO:0000312|WormBase:ZK622.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
RX PubMed=17313371; DOI=10.1042/bj20061815;
RA Brendza K.M., Haakenson W., Cahoon R.E., Hicks L.M., Palavalli L.H.,
RA Chiapelli B.J., McLaird M., McCarter J.P., Williams D.J., Hresko M.C.,
RA Jez J.M.;
RT "Phosphoethanolamine N-methyltransferase (PMT-1) catalyses the first
RT reaction of a new pathway for phosphocholine biosynthesis in Caenorhabditis
RT elegans.";
RL Biochem. J. 404:439-448(2007).
CC -!- FUNCTION: Catalyzes the first step in the synthesis of phosphocholine
CC by converting phosphoethanolamine into phospho-monomethylethanolamine
CC (N-methylethanolamine phosphate). Phosphocholine is a precursor for
CC phosphatidylcholine, a major component in membranes and a precursor
CC itself in the production of glycoconjugates secreted by parasitic
CC nematodes to avoid host immune responses.
CC {ECO:0000269|PubMed:17313371}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N-
CC methylethanolamine phosphate + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20365, ChEBI:CHEBI:15378, ChEBI:CHEBI:57781,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58190, ChEBI:CHEBI:59789;
CC EC=2.1.1.103; Evidence={ECO:0000269|PubMed:17313371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20366;
CC Evidence={ECO:0000269|PubMed:17313371};
CC -!- ACTIVITY REGULATION: Feedback inhibition by phosphatidylcholine.
CC {ECO:0000269|PubMed:17313371}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=145 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17313371};
CC KM=9.9 uM for phosphoethanolamine {ECO:0000269|PubMed:17313371};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from phosphoethanolamine. {ECO:0000269|PubMed:17313371}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q23552-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q23552-2; Sequence=VSP_061097;
CC Name=3;
CC IsoId=Q23552-3; Sequence=VSP_061096;
CC -!- DISRUPTION PHENOTYPE: Necessary at multiple stages in the worm's life
CC cycle, its disruption alters worm growth and development.
CC {ECO:0000269|PubMed:17313371}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; BX284602; CCD68005.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD68006.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD68008.1; -; Genomic_DNA.
DR PIR; T27936; T27936.
DR RefSeq; NP_494990.2; NM_062589.6. [Q23552-1]
DR RefSeq; NP_494991.1; NM_062590.3. [Q23552-2]
DR RefSeq; NP_871998.1; NM_182198.6.
DR AlphaFoldDB; Q23552; -.
DR SMR; Q23552; -.
DR STRING; 6239.ZK622.3b; -.
DR SwissLipids; SLP:000000513; -.
DR EPD; Q23552; -.
DR PeptideAtlas; Q23552; -.
DR EnsemblMetazoa; ZK622.3a.1; ZK622.3a.1; WBGene00022781. [Q23552-1]
DR EnsemblMetazoa; ZK622.3a.2; ZK622.3a.2; WBGene00022781. [Q23552-1]
DR EnsemblMetazoa; ZK622.3b.1; ZK622.3b.1; WBGene00022781. [Q23552-2]
DR EnsemblMetazoa; ZK622.3d.1; ZK622.3d.1; WBGene00022781. [Q23552-3]
DR EnsemblMetazoa; ZK622.3d.2; ZK622.3d.2; WBGene00022781. [Q23552-3]
DR EnsemblMetazoa; ZK622.3d.3; ZK622.3d.3; WBGene00022781. [Q23552-3]
DR EnsemblMetazoa; ZK622.3d.4; ZK622.3d.4; WBGene00022781. [Q23552-3]
DR GeneID; 173901; -.
DR KEGG; cel:CELE_ZK622.3; -.
DR UCSC; ZK622.3a.1; c. elegans.
DR CTD; 173901; -.
DR WormBase; ZK622.3a; CE33504; WBGene00022781; pmt-1.
DR WormBase; ZK622.3b; CE29162; WBGene00022781; pmt-1.
DR WormBase; ZK622.3d; CE33505; WBGene00022781; pmt-1.
DR eggNOG; KOG1269; Eukaryota.
DR GeneTree; ENSGT00940000172618; -.
DR HOGENOM; CLU_044637_0_0_1; -.
DR OMA; VIRKNWV; -.
DR OrthoDB; 425421at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00022781; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q23552; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:WormBase.
DR GO; GO:0000234; F:phosphoethanolamine N-methyltransferase activity; IDA:WormBase.
DR GO; GO:0052667; F:phosphomethylethanolamine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032504; P:multicellular organism reproduction; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0070832; P:phosphatidylcholine biosynthesis from phosphoryl-ethanolamine via N-dimethylethanolamine phosphate and CDP-choline; IDA:WormBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..475
FT /note="Phosphoethanolamine N-methyltransferase 1"
FT /id="PRO_0000452991"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 3)"
FT /id="VSP_061096"
FT VAR_SEQ 1..14
FT /note="MSTDQQSSVEDQTV -> MDRYSPYDKTVFLIFCTAYILQK (in
FT isoform 2)"
FT /id="VSP_061097"
SQ SEQUENCE 475 AA; 55148 MW; 0B30BC89651526D9 CRC64;
MSTDQQSSVE DQTVAMVNVR RANFKSFWDK YSDKPDTNSM MLNHSAEELE SSDRADILAS
LPLLHNKDVV DIGAGIGRFT TVLAETARWV LSTDFIDSFI KKNQERNAHL GNINYQVGDA
VGLKMESNSV DLVFTNWLMM YLSDEETVEF IFNCMRWLRS HGIVHLRESC SEPSTGRSKA
KSMHDTANAN PTHYRFSSLY INLLRAIRYR DVDNKLWRFN VQWSCSVPTY IKRSNNWRQV
HWLAEKVPAE DGAKGTSFNE LVELIKNTWQ NEQEAWDAKL DDEKYVWTDK VFSSALTSLP
SNSTFFLYTP RTVSPYCHIN AHTLAETFNA NVWNTEIIPE YYRTSLTKSN NLKDQRVRFG
WNQSLTDSVT YWQQKDALFD VFVATEFLST VDDETIRQLP NVMSDGAKFI TLEPVDEVNE
AEMKQRIQEL GYTLKSFTDV TDQCIEAQEQ YFKDHEQLRD EKVIRKNWVL LELTH
