EPT1_YEAST
ID EPT1_YEAST Reviewed; 391 AA.
AC P22140; D3DL73;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Choline/ethanolaminephosphotransferase 1;
DE Short=ETHPT;
DE Short=Ethanolaminephosphotransferase 1;
DE EC=2.7.8.1 {ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919};
DE EC=2.7.8.2 {ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919};
DE AltName: Full=Aminoalcohol phosphotransferase EPT1;
GN Name=EPT1; OrderedLocusNames=YHR123W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204660 / DBY746;
RX PubMed=1848238; DOI=10.1016/s0021-9258(19)67760-4;
RA Hjelmstad R.H., Bell R.M.;
RT "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in
RT Saccharomyces cerevisiae. Nucleotide sequence of the EPT1 gene and
RT comparison of the CPT1 and EPT1 gene products.";
RL J. Biol. Chem. 266:5094-5103(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=2848840; DOI=10.1016/s0021-9258(19)77698-4;
RA Hjelmstad R.H., Bell R.M.;
RT "The sn-1,2-diacylglycerol ethanolaminephosphotransferase activity of
RT Saccharomyces cerevisiae. Isolation of mutants and cloning of the EPT1
RT gene.";
RL J. Biol. Chem. 263:19748-19757(1988).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1847919; DOI=10.1016/s0021-9258(20)64330-7;
RA Hjelmstad R.H., Bell R.M.;
RT "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in
RT Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene
RT products.";
RL J. Biol. Chem. 266:4357-4365(1991).
RN [6]
RP FUNCTION.
RX PubMed=7961445; DOI=10.1128/jb.176.22.6861-6868.1994;
RA McGee T.P., Skinner H.B., Bankaitis V.A.;
RT "Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes
RT in phospholipid biosynthesis: ethanolamine-dependent effects on steady-
RT state membrane phospholipid composition in Saccharomyces cerevisiae.";
RL J. Bacteriol. 176:6861-6868(1994).
RN [7]
RP FUNCTION.
RX PubMed=7961735; DOI=10.1016/s0021-9258(18)46888-3;
RA McMaster C.R., Bell R.M.;
RT "Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory
RT insights from studies employing null and chimeric sn-1,2-diacylglycerol
RT choline- and ethanolaminephosphotransferases.";
RL J. Biol. Chem. 269:28010-28016(1994).
RN [8]
RP INDUCTION.
RX PubMed=7961831; DOI=10.1016/s0021-9258(19)61972-1;
RA Morash S.C., McMaster C.R., Hjelmstad R.H., Bell R.M.;
RT "Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants
RT implicate the CPT1 gene in coordinate regulation of phospholipid
RT biosynthesis.";
RL J. Biol. Chem. 269:28769-28776(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15225629; DOI=10.1016/j.febslet.2004.05.043;
RA Boumann H.A., de Kruijff B., Heck A.J., de Kroon A.I.;
RT "The selective utilization of substrates in vivo by the
RT phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p
RT and Cpt1p in yeast.";
RL FEBS Lett. 569:173-177(2004).
CC -!- FUNCTION: Catalyzes the final step in the CDP-ethanolamine route
CC leading to phosphatidylethanolamine (PE). Can also catalyze the
CC formation of phosphatidylcholine (PC) from CDP-choline, but does not
CC substantially contribute to PC biosynthesis. Preferentially uses CDP-
CC dimethylethanolamine and CDP-propanolamine as aminoalcohol substrates.
CC Shows highest activity toward di-unsaturated diacylglycerol species as
CC lipid substrates. The CDP-ethanolamine pathway may play a role in
CC maintaining the proper PE species distribution.
CC {ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919,
CC ECO:0000269|PubMed:2848840, ECO:0000269|PubMed:7961445,
CC ECO:0000269|PubMed:7961735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine + CMP + H(+); Xref=Rhea:RHEA:32943,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:64612; EC=2.7.8.1;
CC Evidence={ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-
CC glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC Evidence={ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-N-methylethanolamine = 1,2-
CC diacyl-sn-glycero-3-phospho-N-methylethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:33771, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57547, ChEBI:CHEBI:60377, ChEBI:CHEBI:64573;
CC Evidence={ECO:0000269|PubMed:1847919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33772;
CC Evidence={ECO:0000305|PubMed:1847919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CDP-N,N-dimethylethanolamine = 1,2-
CC diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:33775, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:64572, ChEBI:CHEBI:65117;
CC Evidence={ECO:0000269|PubMed:1847919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33776;
CC Evidence={ECO:0000305|PubMed:1847919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + CDP-choline = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H(+);
CC Xref=Rhea:RHEA:44288, ChEBI:CHEBI:15378, ChEBI:CHEBI:52323,
CC ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:1847919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44289;
CC Evidence={ECO:0000305|PubMed:1847919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + CDP-ethanolamine = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + CMP + H(+);
CC Xref=Rhea:RHEA:44292, ChEBI:CHEBI:15378, ChEBI:CHEBI:52323,
CC ChEBI:CHEBI:57876, ChEBI:CHEBI:60377, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000269|PubMed:1847919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44293;
CC Evidence={ECO:0000305|PubMed:1847919};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1847919};
CC -!- ACTIVITY REGULATION: Requires a divalent cation activator, and is
CC inhibited by CMP. Activated by phospholipids, especially
CC phosphatidylcholine. {ECO:0000269|PubMed:1847919}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for CDP-choline {ECO:0000269|PubMed:1847919};
CC KM=29 uM for CDP-dimethylethanolamine {ECO:0000269|PubMed:1847919};
CC KM=29 uM for CDP-monomethylethanolamine {ECO:0000269|PubMed:1847919};
CC KM=22 uM for CDP-ethanolamine {ECO:0000269|PubMed:1847919};
CC Vmax=0.62 nmol/min/mg enzyme for CDP-choline
CC {ECO:0000269|PubMed:1847919};
CC Vmax=0.42 nmol/min/mg enzyme for CDP-dimethylethanolamine
CC {ECO:0000269|PubMed:1847919};
CC Vmax=0.27 nmol/min/mg enzyme for CDP-monomethylethanolamine
CC {ECO:0000269|PubMed:1847919};
CC Vmax=1.35 nmol/min/mg enzyme for CDP-ethanolamine
CC {ECO:0000269|PubMed:1847919};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC -!- INTERACTION:
CC P22140; P17898: CPT1; NbExp=4; IntAct=EBI-6494, EBI-2050738;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- INDUCTION: Repressed by inositol. Repression is dependent on the
CC presence of CPT1. {ECO:0000269|PubMed:7961831}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; M59311; AAA63572.1; -; Genomic_DNA.
DR EMBL; U10398; AAB68409.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06817.1; -; Genomic_DNA.
DR PIR; S48967; S48967.
DR RefSeq; NP_011991.1; NM_001179253.1.
DR AlphaFoldDB; P22140; -.
DR BioGRID; 36556; 107.
DR DIP; DIP-5619N; -.
DR IntAct; P22140; 20.
DR MINT; P22140; -.
DR STRING; 4932.YHR123W; -.
DR SwissLipids; SLP:000000068; -.
DR MaxQB; P22140; -.
DR PaxDb; P22140; -.
DR PRIDE; P22140; -.
DR EnsemblFungi; YHR123W_mRNA; YHR123W; YHR123W.
DR GeneID; 856523; -.
DR KEGG; sce:YHR123W; -.
DR SGD; S000001165; EPT1.
DR VEuPathDB; FungiDB:YHR123W; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_5_2_1; -.
DR InParanoid; P22140; -.
DR OMA; PWGYDAS; -.
DR BioCyc; YEAST:YHR123W-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR SABIO-RK; P22140; -.
DR UniPathway; UPA00558; UER00743.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:P22140; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P22140; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:SGD.
DR GO; GO:0004307; F:ethanolaminephosphotransferase activity; IDA:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IDA:SGD.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; PTHR10414; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Multifunctional enzyme; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Choline/ethanolaminephosphotransferase 1"
FT /id="PRO_0000056809"
FT TOPO_DOM 1..49
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..211
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..285
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..346
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 96
FT /note="D -> V (in Ref. 1; AAA63572)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="C -> S (in Ref. 1; AAA63572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44560 MW; 038942A7FB9EB580 CRC64;
MGYFVPDSHI ENLKSYKYQS EDRSLVSKYF LKPFWQRFCH IFPTWMAPNI ITLSGFAFIV
INVLTVFYYD PNLNTDTPRW TYFSYALGVF LYQTFDGCDG VHARRINQSG PLGELFDHSI
DAINSTLSIF IFASETGMGF SYNLMLSQFA MLTNFYLSTW EEYHTHTLYL SEFSGPVEGI
LIVCVSLILT GIYGKQVIWH TYLFTITVGD KVIDVDTLDI VFSLAVFGLV MNALSAKRNV
DKYYRNSTSS ANNITQIEQD SAIKGLLPFF AYYASIALLV WMQPSFITLS FILSVGFTGA
FTVGRIIVCH LTKQSFPMFN APMLIPLCQI VLYKICLSLW GIESNKIVFA LSWLGFGLSL
GVHIMFMNDI IHEFTEYLDV YALSIKRSKL T
