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Protein

Cardiolipin synthase (CMP-forming)

Gene

CRD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.1 Publication

Catalytic activityi

A CDP-diacylglycerol + a phosphatidylglycerol = a cardiolipin + CMP.2 Publications

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=1 mM for phosphatidylglycerol1 Publication
  2. KM=36 µM for CDP-diacylglycerol1 Publication

    pH dependencei

    Optimum pH is 9.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.1 Publication

    GO - Molecular functioni

    • cardiolipin synthase activity Source: SGD

    GO - Biological processi

    • cellular ion homeostasis Source: SGD
    • lipid biosynthetic process Source: SGD
    • mitochondrial genome maintenance Source: SGD
    • mitochondrial membrane organization Source: SGD
    • phospholipid biosynthetic process Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    BioCyciYEAST:YDL142C-MONOMER.
    BRENDAi2.7.8.B12. 984.
    ReactomeiR-SCE-1482925. Acyl chain remodelling of PG.
    R-SCE-1483076. Synthesis of CL.

    Chemistry

    SwissLipidsiSLP:000000062.
    SLP:000000221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cardiolipin synthase (CMP-forming) (EC:2.7.8.412 Publications)
    Short name:
    CLS
    Gene namesi
    Name:CRD1
    Synonyms:CLS1
    Ordered Locus Names:YDL142C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDL142C.
    SGDiS000002301. CRD1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei83 – 10321HelicalSequence analysisAdd
    BLAST
    Transmembranei155 – 17521HelicalSequence analysisAdd
    BLAST
    Transmembranei209 – 22921HelicalSequence analysisAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Cardiolipin synthase (CMP-forming)PRO_0000056810Add
    BLAST

    PTM databases

    iPTMnetiQ07560.

    Interactioni

    Protein-protein interaction databases

    BioGridi31919. 130 interactions.
    IntActiQ07560. 20 interactions.
    MINTiMINT-4479570.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07560.
    SMRiQ07560. Positions 69-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00390000001607.
    HOGENOMiHOG000010898.
    InParanoidiQ07560.
    KOiK08744.
    OMAiWNSYWDI.
    OrthoDBiEOG7M6DKZ.

    Family and domain databases

    InterProiIPR000462. CDP-OH_P_trans.
    [Graphical view]
    PfamiPF01066. CDP-OH_P_transf. 1 hit.
    [Graphical view]
    PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07560-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIQMVPIYSC SALLRRTIPK RPFYHVLSGL TVRFKVNPQL NYNLFRDLTR
    60 70 80 90 100
    REYATNPSKT PHIKSKLLNI PNILTLSRIG CTPFIGLFII TNNLTPALGL
    110 120 130 140 150
    FAFSSITDFM DGYIARKYGL KTIAGTILDP LADKLLMITT TLALSVPSGP
    160 170 180 190 200
    QIIPVSIAAI ILGRDVLLAI SALFIRYSTL KLKYPGRVAW NSYWDIVRYP
    210 220 230 240 250
    SAEVRPSQLS KWNTFFQMVY LGSGVLLLLY EKEEGCEKTE EDFEDRKQDF
    260 270 280
    QKAFSYLGYV TATTTIMSGV SYALKRNAFK LLK
    Length:283
    Mass (Da):32,020
    Last modified:November 1, 1996 - v1
    Checksum:iF19F4FE89D9BE049
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74190 Genomic DNA. Translation: CAA98715.1.
    BK006938 Genomic DNA. Translation: DAA11716.1.
    PIRiS67689.
    RefSeqiNP_010139.1. NM_001180202.1.

    Genome annotation databases

    EnsemblFungiiYDL142C; YDL142C; YDL142C.
    GeneIDi851413.
    KEGGisce:YDL142C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74190 Genomic DNA. Translation: CAA98715.1.
    BK006938 Genomic DNA. Translation: DAA11716.1.
    PIRiS67689.
    RefSeqiNP_010139.1. NM_001180202.1.

    3D structure databases

    ProteinModelPortaliQ07560.
    SMRiQ07560. Positions 69-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31919. 130 interactions.
    IntActiQ07560. 20 interactions.
    MINTiMINT-4479570.

    Chemistry

    SwissLipidsiSLP:000000062.
    SLP:000000221.

    PTM databases

    iPTMnetiQ07560.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL142C; YDL142C; YDL142C.
    GeneIDi851413.
    KEGGisce:YDL142C.

    Organism-specific databases

    EuPathDBiFungiDB:YDL142C.
    SGDiS000002301. CRD1.

    Phylogenomic databases

    GeneTreeiENSGT00390000001607.
    HOGENOMiHOG000010898.
    InParanoidiQ07560.
    KOiK08744.
    OMAiWNSYWDI.
    OrthoDBiEOG7M6DKZ.

    Enzyme and pathway databases

    BioCyciYEAST:YDL142C-MONOMER.
    BRENDAi2.7.8.B12. 984.
    ReactomeiR-SCE-1482925. Acyl chain remodelling of PG.
    R-SCE-1483076. Synthesis of CL.

    Miscellaneous databases

    PROiQ07560.

    Family and domain databases

    InterProiIPR000462. CDP-OH_P_trans.
    [Graphical view]
    PfamiPF01066. CDP-OH_P_transf. 1 hit.
    [Graphical view]
    PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Sarma P.V.G.K., Sarma P.U.
      Submitted (DEC-1999) to UniProtKB
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-135.
    4. "Biochemical characterization and regulation of cardiolipin synthase in Saccharomyces cerevisiae."
      Tamai K.T., Greenberg M.L.
      Biochim. Biophys. Acta 1046:214-222(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "YDL142c encodes cardiolipin synthase (Cls1p) and is non-essential for aerobic growth of Saccharomyces cerevisiae."
      Tuller G., Hrastnik C., Achleitner G., Schiefthaler U., Klein F., Daum G.
      FEBS Lett. 421:15-18(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "Isolation and characterization of the gene (CLS1) encoding cardiolipin synthase in Saccharomyces cerevisiae."
      Chang S.C., Heacock P.N., Mileykovskaya E., Voelker D.R., Dowhan W.
      J. Biol. Chem. 273:14933-14941(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    7. Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCRD1_YEAST
    AccessioniPrimary (citable) accession number: Q07560
    Secondary accession number(s): D6VRK6, P82260
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: June 8, 2016
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 876 molecules/cell in log phase SD medium.1 Publication

    Caution

    Ref. 3 sequence was originally thought to originate from Mycobacterium phlei.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.