PCY1_YEAST
ID PCY1_YEAST Reviewed; 424 AA.
AC P13259; D6VUY4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Choline-phosphate cytidylyltransferase;
DE EC=2.7.7.15 {ECO:0000269|PubMed:2826147};
DE AltName: Full=CTP:phosphocholine cytidylyltransferase;
DE Short=CCT;
DE Short=CT;
DE AltName: Full=Phosphorylcholine transferase;
GN Name=PCT1; Synonyms=CCT, CCT1; OrderedLocusNames=YGR202C; ORFNames=G7729;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2826147; DOI=10.1111/j.1432-1033.1987.tb13635.x;
RA Tsukagoshi Y., Nikawa J., Yamashita S.;
RT "Molecular cloning and characterization of the gene encoding
RT cholinephosphate cytidylyltransferase in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 169:477-486(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-59 AND SER-346, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-346, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline
CC pathway for phosphatidylcholine biosynthesis.
CC {ECO:0000269|PubMed:2826147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate;
CC Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975;
CC EC=2.7.7.15; Evidence={ECO:0000269|PubMed:2826147};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998;
CC Evidence={ECO:0000269|PubMed:2826147};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphatidylcholine from phosphocholine: step 1/2.
CC {ECO:0000305|PubMed:2826147}.
CC -!- SUBCELLULAR LOCATION: Membrane. Note=Most of its activity is membrane-
CC associated.
CC -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family. {ECO:0000305}.
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DR EMBL; M36827; AAA91962.1; -; Genomic_DNA.
DR EMBL; Z49133; CAA88995.1; -; Genomic_DNA.
DR EMBL; Z72987; CAA97229.1; -; Genomic_DNA.
DR EMBL; AY557840; AAS56166.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08295.1; -; Genomic_DNA.
DR PIR; S53925; XNBYCP.
DR RefSeq; NP_011718.1; NM_001181331.1.
DR AlphaFoldDB; P13259; -.
DR SMR; P13259; -.
DR BioGRID; 33455; 123.
DR DIP; DIP-6390N; -.
DR IntAct; P13259; 16.
DR MINT; P13259; -.
DR STRING; 4932.YGR202C; -.
DR SwissLipids; SLP:000000069; -.
DR iPTMnet; P13259; -.
DR MaxQB; P13259; -.
DR PaxDb; P13259; -.
DR PRIDE; P13259; -.
DR EnsemblFungi; YGR202C_mRNA; YGR202C; YGR202C.
DR GeneID; 853116; -.
DR KEGG; sce:YGR202C; -.
DR SGD; S000003434; PCT1.
DR VEuPathDB; FungiDB:YGR202C; -.
DR eggNOG; KOG2804; Eukaryota.
DR GeneTree; ENSGT00940000171345; -.
DR HOGENOM; CLU_034585_0_0_1; -.
DR InParanoid; P13259; -.
DR OMA; CGIPSDE; -.
DR BioCyc; MetaCyc:YGR202C-MON; -.
DR BioCyc; YEAST:YGR202C-MON; -.
DR Reactome; R-SCE-1483191; Synthesis of PC.
DR UniPathway; UPA00753; UER00739.
DR PRO; PR:P13259; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P13259; protein.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IDA:SGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0006657; P:CDP-choline pathway; IDA:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045049; Pcy1-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10739; PTHR10739; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="Choline-phosphate cytidylyltransferase"
FT /id="PRO_0000208460"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..119
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT BINDING 223..227
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 401
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT CONFLICT 90
FT /note="P -> PG (in Ref. 1; AAA91962)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="Missing (in Ref. 1; AAA91962)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Y -> H (in Ref. 1; AAA91962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 49406 MW; 246774FE2F7124A3 CRC64;
MANPTTGKSS IRAKLSNSSL SNLFKKNKNK RQREETEEQD NEDKDESKNQ DENKDTQLTP
RKRRRLTKEF EEKEARYTNE LPKELRKYRP KGFRFNLPPT DRPIRIYADG VFDLFHLGHM
KQLEQCKKAF PNVTLIVGVP SDKITHKLKG LTVLTDKQRC ETLTHCRWVD EVVPNAPWCV
TPEFLLEHKI DYVAHDDIPY VSADSDDIYK PIKEMGKFLT TQRTNGVSTS DIITKIIRDY
DKYLMRNFAR GATRQELNVS WLKKNELEFK KHINEFRSYF KKNQTNLNNA SRDLYFEVRE
ILLKKTLGKK LYSKLIGNEL KKQNQRQRKQ NFLDDPFTRK LIREASPATE FANEFTGENS
TAKSPDDNGN LFSQEDDEDT NSNNTNTNSD SDSNTNSTPP SEDDDDNDRL TLENLTQKKK
QSAN
