CPT1_YEAST
ID CPT1_YEAST Reviewed; 393 AA.
AC P17898; D6W152;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cholinephosphotransferase 1;
DE EC=2.7.8.2;
DE AltName: Full=Aminoalcohol phosphotransferase CPT1;
DE AltName: Full=Diacylglycerol cholinephosphotransferase 1;
DE AltName: Full=Sn-1,2-diacylglycerol cholinephosphotransferase;
DE Short=CHOPT;
GN Name=CPT1; OrderedLocusNames=YNL130C; ORFNames=N1218, N1867;
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].
RX PubMed=2153142; DOI=10.1016/s0021-9258(19)40081-1;
RA Hjelmstad R.H., Bell R.M.;
RT "The sn-1,2-diacylglycerol cholinephosphotransferase of Saccharomyces
RT cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product
RT analysis of the CPT1 gene.";
RL J. Biol. Chem. 265:1755-1764(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=3005242; DOI=10.1128/jb.165.3.901-910.1986;
RA Kuchler K., Daum G., Paltauf F.;
RT "Subcellular and submitochondrial localization of phospholipid-synthesizing
RT enzymes in Saccharomyces cerevisiae.";
RL J. Bacteriol. 165:901-910(1986).
RN [6]
RP FUNCTION.
RX PubMed=3029130; DOI=10.1016/s0021-9258(18)61443-7;
RA Hjelmstad R.H., Bell R.M.;
RT "Mutants of Saccharomyces cerevisiae defective in sn-1,2-diacylglycerol
RT cholinephosphotransferase. Isolation, characterization, and cloning of the
RT CPT1 gene.";
RL J. Biol. Chem. 262:3909-3917(1987).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=8543066; DOI=10.1016/0014-5793(95)01361-x;
RA Leber A., Hrastnik C., Daum G.;
RT "Phospholipid-synthesizing enzymes in Golgi membranes of the yeast,
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 377:271-274(1995).
RN [12]
RP REVISION OF GENE MODEL.
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
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-choline route leading to
CC phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine
CC as aminoalcohol substrate. Shows highest activity toward di- and mono-
CC unsaturated diacylglycerol species as lipid substrates. The CDP-choline
CC pathway only contributes to net PC synthesis if exogenous choline is
CC present. In its absence, this pathway recycles choline from PC turnover
CC and may contribute to maintaining the proper PC species composition.
CC {ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919,
CC ECO:0000269|PubMed:3029130, ECO:0000269|PubMed:7961445,
CC ECO:0000269|PubMed:7961735}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
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 -!- 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=100 uM for CDP-choline {ECO:0000269|PubMed:1847919};
CC KM=137 uM for CDP-dimethylethanolamine {ECO:0000269|PubMed:1847919};
CC Vmax=0.2 nmol/min/mg enzyme for CDP-choline
CC {ECO:0000269|PubMed:1847919};
CC Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine
CC {ECO:0000269|PubMed:1847919};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 2/2.
CC -!- INTERACTION:
CC P17898; P22140: EPT1; NbExp=4; IntAct=EBI-2050738, EBI-6494;
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC Mitochondrion outer membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Repressed by inositol. {ECO:0000269|PubMed:7961831}.
CC -!- MISCELLANEOUS: Present with 981 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63571.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA86895.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA96012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J05203; AAA63571.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z46843; CAA86895.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71406; CAA96012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006947; DAA10418.1; -; Genomic_DNA.
DR PIR; S63075; S63075.
DR RefSeq; NP_014269.4; NM_001182968.3.
DR AlphaFoldDB; P17898; -.
DR BioGRID; 35697; 123.
DR DIP; DIP-7848N; -.
DR IntAct; P17898; 20.
DR MINT; P17898; -.
DR STRING; 4932.YNL130C; -.
DR SwissLipids; SLP:000000070; -.
DR iPTMnet; P17898; -.
DR MaxQB; P17898; -.
DR PaxDb; P17898; -.
DR PRIDE; P17898; -.
DR EnsemblFungi; YNL130C_mRNA; YNL130C; YNL130C.
DR GeneID; 855593; -.
DR KEGG; sce:YNL130C; -.
DR SGD; S000005074; CPT1.
DR VEuPathDB; FungiDB:YNL130C; -.
DR eggNOG; KOG2877; Eukaryota.
DR GeneTree; ENSGT00950000183117; -.
DR HOGENOM; CLU_035066_5_2_1; -.
DR InParanoid; P17898; -.
DR OMA; FPYQNVL; -.
DR BioCyc; MetaCyc:YNL130C-MON; -.
DR BioCyc; YEAST:YNL130C-MON; -.
DR BRENDA; 2.7.8.2; 984.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR SABIO-RK; P17898; -.
DR UniPathway; UPA00753; UER00740.
DR PRO; PR:P17898; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P17898; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006657; P:CDP-choline pathway; 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 Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Membrane; Metal-binding; Microsome; Mitochondrion;
KW Mitochondrion outer membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Cholinephosphotransferase 1"
FT /id="PRO_0000056808"
FT TOPO_DOM 1..40
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..210
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..348
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 44829 MW; 320845FE9A79C5D6 CRC64;
MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL VTLLGFCFII
FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG MHARRTGQQG PLGELFDHCI
DSINTTLSMI PVCSMTGMGY TYMTIFSQFA ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI
IVLCISFIAV GIYGPQTIWH TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV
VRYYESQSTK SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS
VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV SALVWMGLGL
TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI
