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P17898

- CPT1_YEAST

UniProt

P17898 - CPT1_YEAST

Protein

Cholinephosphotransferase 1

Gene

CPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono-unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition.5 Publications

    Catalytic activityi

    CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine.2 Publications

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Requires a divalent cation activator, and is inhibited by CMP. Activated by phospholipids, especially phosphatidylcholine.1 Publication

    Kineticsi

    1. KM=100 µM for CDP-choline1 Publication
    2. KM=137 µM for CDP-dimethylethanolamine1 Publication

    Vmax=0.2 nmol/min/mg enzyme for CDP-choline1 Publication

    Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine1 Publication

    Pathwayi

    GO - Molecular functioni

    1. diacylglycerol cholinephosphotransferase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. CDP-choline pathway Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13671.
    YEAST:YNL130C-MONOMER.
    UniPathwayiUPA00753; UER00740.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholinephosphotransferase 1 (EC:2.7.8.2)
    Alternative name(s):
    Aminoalcohol phosphotransferase CPT1
    Diacylglycerol cholinephosphotransferase 1
    Sn-1,2-diacylglycerol cholinephosphotransferase
    Short name:
    CHOPT
    Gene namesi
    Name:CPT1
    Ordered Locus Names:YNL130C
    ORF Names:N1218, N1867
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL130c.
    SGDiS000005074. CPT1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi apparatus Source: SGD
    3. integral component of membrane Source: UniProtKB-KW
    4. mitochondrial outer membrane Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Cholinephosphotransferase 1PRO_0000056808Add
    BLAST

    Proteomic databases

    MaxQBiP17898.
    PaxDbiP17898.

    Expressioni

    Inductioni

    Repressed by inositol.1 Publication

    Gene expression databases

    GenevestigatoriP17898.

    Interactioni

    Protein-protein interaction databases

    BioGridi35697. 57 interactions.
    DIPiDIP-7848N.
    IntActiP17898. 7 interactions.
    MINTiMINT-4499922.
    STRINGi4932.YNL130C.

    Structurei

    3D structure databases

    ProteinModelPortaliP17898.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4040LumenalSequence AnalysisAdd
    BLAST
    Topological domaini62 – 172111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini194 – 21017LumenalSequence AnalysisAdd
    BLAST
    Topological domaini232 – 26332CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini285 – 2851LumenalSequence Analysis
    Topological domaini307 – 32014CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini342 – 3487LumenalSequence Analysis
    Topological domaini370 – 39324CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei41 – 6121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei173 – 19321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei211 – 23121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei264 – 28421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei286 – 30621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei321 – 34121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei349 – 36921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5050.
    GeneTreeiENSGT00530000063048.
    HOGENOMiHOG000157893.
    KOiK00994.
    OrthoDBiEOG7W9S4H.

    Family and domain databases

    InterProiIPR000462. CDP-OH_P_trans.
    IPR014472. CHOPT.
    [Graphical view]
    PANTHERiPTHR10414. PTHR10414. 1 hit.
    PfamiPF01066. CDP-OH_P_transf. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015665. CHOPT. 1 hit.
    PROSITEiPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17898-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL    50
    VTLLGFCFII FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG 100
    MHARRTGQQG PLGELFDHCI DSINTTLSMI PVCSMTGMGY TYMTIFSQFA 150
    ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI IVLCISFIAV GIYGPQTIWH 200
    TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV VRYYESQSTK 250
    SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS 300
    VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV 350
    SALVWMGLGL TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI 393
    Length:393
    Mass (Da):44,829
    Last modified:September 5, 2006 - v3
    Checksum:i320845FE9A79C5D6
    GO

    Sequence cautioni

    The sequence AAA63571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA86895.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA96012.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05203 Genomic DNA. Translation: AAA63571.1. Different initiation.
    Z46843 Genomic DNA. Translation: CAA86895.1. Different initiation.
    Z71406 Genomic DNA. Translation: CAA96012.1. Sequence problems.
    BK006947 Genomic DNA. Translation: DAA10418.1.
    PIRiS63075.
    RefSeqiNP_014269.4. NM_001182968.3.

    Genome annotation databases

    EnsemblFungiiYNL130C; YNL130C; YNL130C.
    GeneIDi855593.
    KEGGisce:YNL130C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05203 Genomic DNA. Translation: AAA63571.1 . Different initiation.
    Z46843 Genomic DNA. Translation: CAA86895.1 . Different initiation.
    Z71406 Genomic DNA. Translation: CAA96012.1 . Sequence problems.
    BK006947 Genomic DNA. Translation: DAA10418.1 .
    PIRi S63075.
    RefSeqi NP_014269.4. NM_001182968.3.

    3D structure databases

    ProteinModelPortali P17898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35697. 57 interactions.
    DIPi DIP-7848N.
    IntActi P17898. 7 interactions.
    MINTi MINT-4499922.
    STRINGi 4932.YNL130C.

    Proteomic databases

    MaxQBi P17898.
    PaxDbi P17898.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL130C ; YNL130C ; YNL130C .
    GeneIDi 855593.
    KEGGi sce:YNL130C.

    Organism-specific databases

    CYGDi YNL130c.
    SGDi S000005074. CPT1.

    Phylogenomic databases

    eggNOGi COG5050.
    GeneTreei ENSGT00530000063048.
    HOGENOMi HOG000157893.
    KOi K00994.
    OrthoDBi EOG7W9S4H.

    Enzyme and pathway databases

    UniPathwayi UPA00753 ; UER00740 .
    BioCyci MetaCyc:MONOMER-13671.
    YEAST:YNL130C-MONOMER.

    Miscellaneous databases

    NextBioi 979741.
    PROi P17898.

    Gene expression databases

    Genevestigatori P17898.

    Family and domain databases

    InterProi IPR000462. CDP-OH_P_trans.
    IPR014472. CHOPT.
    [Graphical view ]
    PANTHERi PTHR10414. PTHR10414. 1 hit.
    Pfami PF01066. CDP-OH_P_transf. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015665. CHOPT. 1 hit.
    PROSITEi PS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sn-1,2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPT1 gene."
      Hjelmstad R.H., Bell R.M.
      J. Biol. Chem. 265:1755-1764(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine deaminase gene and 14 new open reading frames."
      Mallet L., Bussereau F., Jacquet M.
      Yeast 11:1195-1209(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Subcellular and submitochondrial localization of phospholipid-synthesizing enzymes in Saccharomyces cerevisiae."
      Kuchler K., Daum G., Paltauf F.
      J. Bacteriol. 165:901-910(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Mutants of Saccharomyces cerevisiae defective in sn-1,2-diacylglycerol cholinephosphotransferase. Isolation, characterization, and cloning of the CPT1 gene."
      Hjelmstad R.H., Bell R.M.
      J. Biol. Chem. 262:3909-3917(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products."
      Hjelmstad R.H., Bell R.M.
      J. Biol. Chem. 266:4357-4365(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes in phospholipid biosynthesis: ethanolamine-dependent effects on steady-state membrane phospholipid composition in Saccharomyces cerevisiae."
      McGee T.P., Skinner H.B., Bankaitis V.A.
      J. Bacteriol. 176:6861-6868(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases."
      McMaster C.R., Bell R.M.
      J. Biol. Chem. 269:28010-28016(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants implicate the CPT1 gene in coordinate regulation of phospholipid biosynthesis."
      Morash S.C., McMaster C.R., Hjelmstad R.H., Bell R.M.
      J. Biol. Chem. 269:28769-28776(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Phospholipid-synthesizing enzymes in Golgi membranes of the yeast, Saccharomyces cerevisiae."
      Leber A., Hrastnik C., Daum G.
      FEBS Lett. 377:271-274(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
      Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
      Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVISION OF GENE MODEL.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "The selective utilization of substrates in vivo by the phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p and Cpt1p in yeast."
      Boumann H.A., de Kruijff B., Heck A.J., de Kroon A.I.
      FEBS Lett. 569:173-177(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiCPT1_YEAST
    AccessioniPrimary (citable) accession number: P17898
    Secondary accession number(s): D6W152
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 981 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3