ECT1_YEAST
ID ECT1_YEAST Reviewed; 323 AA.
AC P33412; D6VUE4; Q05725;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ethanolamine-phosphate cytidylyltransferase {ECO:0000303|PubMed:8982874};
DE EC=2.7.7.14 {ECO:0000269|PubMed:8982874};
DE AltName: Full=CTP:phosphoethanolamine cytidylyltransferase {ECO:0000303|PubMed:8982874};
DE AltName: Full=Phosphorylethanolamine transferase {ECO:0000303|PubMed:8982874};
GN Name=ECT1 {ECO:0000303|PubMed:8982874}; Synonyms=MUQ1;
GN OrderedLocusNames=YGR007W; ORFNames=G3856;
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=8474454; DOI=10.1128/mcb.13.5.2959-2970.1993;
RA Horowitz D.S., Abelson J.N.;
RT "A U5 small nuclear ribonucleoprotein particle protein involved only in the
RT second step of pre-mRNA splicing in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:2959-2970(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=S288c / GRF88;
RX PubMed=8982874; DOI=10.1093/oxfordjournals.jbchem.a021497;
RA Min-Seok R., Kawamata Y., Nakamura H., Ohta A., Takagi M.;
RT "Isolation and characterization of ECT1 gene encoding CTP:
RT phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae.";
RL J. Biochem. 120:1040-1047(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 INDUCTION.
RX PubMed=11055939; DOI=10.1128/aem.66.11.4883-4889.2000;
RA Miura S., Zou W., Ueda M., Tanaka A.;
RT "Screening of genes involved in isooctane tolerance in Saccharomyces
RT cerevisiae by using mRNA differential display.";
RL Appl. Environ. Microbiol. 66:4883-4889(2000).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=17761681; DOI=10.1074/jbc.m705098200;
RA Choi H.-S., Carman G.M.;
RT "Respiratory deficiency mediates the regulation of CHO1-encoded
RT phosphatidylserine synthase by mRNA stability in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 282:31217-31227(2007).
RN [10]
RP FUNCTION.
RX PubMed=18776695; DOI=10.1271/bbb.80265;
RA Deng L., Nagasawa J., Ono Y., Ishikawa Y., Kakihara T., Fukuda R., Ohta A.;
RT "Manipulation of major membrane lipid synthesis and its effects on
RT sporulation in Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 72:2362-2368(2008).
RN [11]
RP CRYSTALLIZATION.
RX PubMed=17012796; DOI=10.1107/s1744309106035561;
RA Ohtsuka J., Nagata K., Lee W.C., Ono Y., Fukuda R., Ohta A., Tanokura M.;
RT "Crystallization and preliminary X-ray analysis of CTP:phosphoethanolamine
RT cytidylyltransferase (ECT) from Saccharomyces cerevisiae.";
RL Acta Crystallogr. F 62:1003-1005(2006).
CC -!- FUNCTION: Ethanolamine-phosphate cytidylyltransferase which catalyzes
CC the second step of phosphatidylethanolamine biosynthesis. Involved in
CC the maintenance of plasma membrane and required for proper sporulation.
CC {ECO:0000269|PubMed:17761681, ECO:0000269|PubMed:18776695,
CC ECO:0000269|PubMed:8982874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H(+) + phosphoethanolamine = CDP-ethanolamine +
CC diphosphate; Xref=Rhea:RHEA:24592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57876,
CC ChEBI:CHEBI:58190; EC=2.7.7.14;
CC Evidence={ECO:0000269|PubMed:8982874};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By isooctane. {ECO:0000269|PubMed:11055939}.
CC -!- MISCELLANEOUS: Present with 4700 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; L03536; AAA34916.1; -; Genomic_DNA.
DR EMBL; D50644; BAA09310.1; -; Genomic_DNA.
DR EMBL; Z72792; CAA96990.1; -; Genomic_DNA.
DR EMBL; AY557830; AAS56156.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08105.1; -; Genomic_DNA.
DR PIR; B48067; B48067.
DR RefSeq; NP_011521.1; NM_001181136.1.
DR AlphaFoldDB; P33412; -.
DR SMR; P33412; -.
DR BioGRID; 33251; 66.
DR STRING; 4932.YGR007W; -.
DR SwissLipids; SLP:000000067; -.
DR MaxQB; P33412; -.
DR PaxDb; P33412; -.
DR PRIDE; P33412; -.
DR EnsemblFungi; YGR007W_mRNA; YGR007W; YGR007W.
DR GeneID; 852890; -.
DR KEGG; sce:YGR007W; -.
DR SGD; S000003239; ECT1.
DR VEuPathDB; FungiDB:YGR007W; -.
DR eggNOG; KOG2803; Eukaryota.
DR GeneTree; ENSGT00550000075065; -.
DR HOGENOM; CLU_031246_1_0_1; -.
DR InParanoid; P33412; -.
DR OMA; AAHGSDI; -.
DR BioCyc; YEAST:YGR007W-MON; -.
DR Reactome; R-SCE-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00742.
DR ChiTaRS; ECT1; yeast.
DR PRO; PR:P33412; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33412; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IDA:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:SGD.
DR CDD; cd02174; CCT; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR InterPro; IPR041723; CCT.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR044608; Ect1/PCYT2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR45780; PTHR45780; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Nucleotidyltransferase;
KW Nucleus; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..323
FT /note="Ethanolamine-phosphate cytidylyltransferase"
FT /id="PRO_0000208465"
FT CONFLICT 252
FT /note="S -> I (in Ref. 2; BAA09310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36863 MW; 9BC6DF97007EB689 CRC64;
MTVNLDPDKV WIDGCFDFTH HGHAGAILQA RRTVSKENGK LFCGVHTDED IQHNKGTPVM
NSSERYEHTR SNRWCSEVVE AAPYVTDPNW MDKYQCQYVV HGDDITIDAN GEDCYKLVKE
MGRFKVVKRT YGVSTTEIIH RILTKKSLPP THPDYYPTTQ ELSFYSVAQD AVSKHCYVFQ
RDLDNVLVNG GYKFDAEDCV YVDGDFDLFH MGDIDQLRKL KMDLHPDKKL IVGITTSDYS
STIMTMKERV LSVLSCKYVD AVIIDADATS MSQYNCEKYH IGTAVLTAAG KFSEYLTKEL
IVKRVESQRE VYIARNQKKG MSI
