CRD1_YEAST
ID CRD1_YEAST Reviewed; 283 AA.
AC Q07560; D6VRK6; P82260;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cardiolipin synthase (CMP-forming);
DE Short=CLS;
DE EC=2.7.8.41 {ECO:0000269|PubMed:2171667, ECO:0000269|PubMed:9370334};
GN Name=CRD1; Synonyms=CLS1; OrderedLocusNames=YDL142C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-135.
RA Sarma P.V.G.K., Sarma P.U.;
RL Submitted (DEC-1999) to UniProtKB.
RN [4]
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2171667; DOI=10.1016/0005-2760(90)90192-z;
RA Tamai K.T., Greenberg M.L.;
RT "Biochemical characterization and regulation of cardiolipin synthase in
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1046:214-222(1990).
RN [5]
RP IDENTIFICATION.
RX PubMed=9462830; DOI=10.1016/s0014-5793(97)01525-1;
RA Tuller G., Hrastnik C., Achleitner G., Schiefthaler U., Klein F., Daum G.;
RT "YDL142c encodes cardiolipin synthase (Cls1p) and is non-essential for
RT aerobic growth of Saccharomyces cerevisiae.";
RL FEBS Lett. 421:15-18(1998).
RN [6]
RP IDENTIFICATION.
RX PubMed=9614098; DOI=10.1074/jbc.273.24.14933;
RA Chang S.C., Heacock P.N., Mileykovskaya E., Voelker D.R., Dowhan W.;
RT "Isolation and characterization of the gene (CLS1) encoding cardiolipin
RT synthase in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:14933-14941(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX PubMed=9370334; DOI=10.1016/s0005-2760(97)00117-3;
RA Schlame M., Greenberg M.L.;
RT "Cardiolipin synthase from yeast.";
RL Biochim. Biophys. Acta 1348:201-206(1997).
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).
CC -!- FUNCTION: Catalyzes the synthesis of cardiolipin (CL)
CC (diphosphatidylglycerol) by specifically transferring a phosphatidyl
CC group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key
CC phospholipid in mitochondrial membranes and plays important roles in
CC maintaining the functional integrity and dynamics of mitochondria under
CC both optimal and stress conditions. {ECO:0000269|PubMed:9370334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-
CC diacyl-sn-glycerol = a cardiolipin + CMP + H(+);
CC Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41;
CC Evidence={ECO:0000269|PubMed:2171667, ECO:0000269|PubMed:9370334};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:2171667};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 mM for phosphatidylglycerol {ECO:0000269|PubMed:2171667};
CC KM=36 uM for CDP-diacylglycerol {ECO:0000269|PubMed:2171667};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:2171667};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:2171667};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 876 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 -!- CAUTION: Ref.3 sequence was originally thought to originate from
CC Mycobacterium phlei. {ECO:0000305}.
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DR EMBL; Z74190; CAA98715.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11716.1; -; Genomic_DNA.
DR PIR; S67689; S67689.
DR RefSeq; NP_010139.1; NM_001180202.1.
DR AlphaFoldDB; Q07560; -.
DR SMR; Q07560; -.
DR BioGRID; 31919; 550.
DR IntAct; Q07560; 20.
DR STRING; 4932.YDL142C; -.
DR SwissLipids; SLP:000000062; -.
DR SwissLipids; SLP:000000221; -.
DR iPTMnet; Q07560; -.
DR PaxDb; Q07560; -.
DR PRIDE; Q07560; -.
DR EnsemblFungi; YDL142C_mRNA; YDL142C; YDL142C.
DR GeneID; 851413; -.
DR KEGG; sce:YDL142C; -.
DR SGD; S000002301; CRD1.
DR VEuPathDB; FungiDB:YDL142C; -.
DR eggNOG; KOG1617; Eukaryota.
DR GeneTree; ENSGT00390000001607; -.
DR HOGENOM; CLU_051314_0_2_1; -.
DR InParanoid; Q07560; -.
DR OMA; WNTFLQM; -.
DR BioCyc; YEAST:YDL142C-MON; -.
DR BRENDA; 2.7.8.41; 984.
DR Reactome; R-SCE-1482925; Acyl chain remodelling of PG.
DR Reactome; R-SCE-1483076; Synthesis of CL.
DR SABIO-RK; Q07560; -.
DR PRO; PR:Q07560; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07560; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008808; F:cardiolipin synthase activity; IDA:SGD.
DR GO; GO:0043337; F:CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase activity; IEA:RHEA.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:SGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Cardiolipin synthase (CMP-forming)"
FT /id="PRO_0000056810"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 283 AA; 32020 MW; F19F4FE89D9BE049 CRC64;
MIQMVPIYSC SALLRRTIPK RPFYHVLSGL TVRFKVNPQL NYNLFRDLTR REYATNPSKT
PHIKSKLLNI PNILTLSRIG CTPFIGLFII TNNLTPALGL FAFSSITDFM DGYIARKYGL
KTIAGTILDP LADKLLMITT TLALSVPSGP QIIPVSIAAI ILGRDVLLAI SALFIRYSTL
KLKYPGRVAW NSYWDIVRYP SAEVRPSQLS KWNTFFQMVY LGSGVLLLLY EKEEGCEKTE
EDFEDRKQDF QKAFSYLGYV TATTTIMSGV SYALKRNAFK LLK
