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Protein

Diacylglycerol pyrophosphate phosphatase 1

Gene

DPP1

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 dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. Substrate preference is DGPP > LPA > PA. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.2 Publications

Catalytic activityi

1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate.1 Publication
A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.1 Publication

Enzyme regulationi

Inhibited by sodium fluoride (NaF) and pyrophosphate. Strongly inhibited by manganese ion and, to a lower extent, by magnesium and calcium ions. Also inhibited by Cu2+ ion. In an indirect manner, it is also inhibited by the zinc ion which is able to form a complex with DGPP and prevent the enzyme from removing the phosphate from the substrate. Not inhibited by N-ethylmaleimide.2 Publications

Kineticsi

    1. Vmax=167 µmol/min/mg enzyme with lysophosphatidic acid as substrate1 Publication

    pH dependencei

    Optimum pH is 6.0-8.5.1 Publication

    GO - Molecular functioni

    • diacylglycerol diphosphate phosphatase activity Source: SGD
    • phosphatidate phosphatase activity Source: SGD

    GO - Biological processi

    • dephosphorylation Source: GOC
    • phospholipid metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15445.
    YEAST:YDR284C-MONOMER.
    BRENDAi3.1.3.81. 984.
    ReactomeiR-SCE-2029485. Role of phospholipids in phagocytosis.

    Protein family/group databases

    TCDBi9.B.105.3.2. the lead resistance fusion protein (pbrbc) family.

    Chemistry

    SwissLipidsiSLP:000000057.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diacylglycerol pyrophosphate phosphatase 1 (EC:3.1.3.81)
    Short name:
    DGPP phosphatase
    Alternative name(s):
    Phosphatidate phosphatase (EC:3.1.3.4)
    Gene namesi
    Name:DPP1
    Synonyms:ZRG1
    Ordered Locus Names:YDR284C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDR284C.
    SGDiS000002692. DPP1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2121VacuolarSequence analysisAdd
    BLAST
    Transmembranei22 – 4221Helical; Name=1Sequence analysisAdd
    BLAST
    Topological domaini43 – 6523CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei66 – 8621Helical; Name=2Sequence analysisAdd
    BLAST
    Topological domaini87 – 926VacuolarSequence analysis
    Transmembranei93 – 11321Helical; Name=3Sequence analysisAdd
    BLAST
    Topological domaini114 – 17259CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei173 – 19321Helical; Name=4Sequence analysisAdd
    BLAST
    Transmembranei194 – 21421Helical; Name=5Sequence analysisAdd
    BLAST
    Topological domaini215 – 2228CytoplasmicSequence analysis
    Transmembranei223 – 24321Helical; Name=6Sequence analysisAdd
    BLAST
    Topological domaini244 – 28946VacuolarSequence analysisAdd
    BLAST

    GO - Cellular componenti

    • fungal-type vacuole membrane Source: SGD
    • integral component of membrane Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251R → A: Complete loss of DGPP phosphatase activity. 1 Publication
    Mutagenesisi169 – 1691H → A: 91% decrease of DGPP phosphatase activity. 1 Publication
    Mutagenesisi223 – 2231H → A: Complete loss of DGPP phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Diacylglycerol pyrophosphate phosphatase 1PRO_0000220918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei285 – 2851PhosphoserineCombined sources

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05521.
    PeptideAtlasiQ05521.
    TopDownProteomicsiQ05521.

    PTM databases

    iPTMnetiQ05521.

    Expressioni

    Inductioni

    Induced by the transcription factor ZAP1 during zinc depletion and negatively regulated by the transcription factor GIS1 predominantly during nutrient limitation. Induced by inositol supplementation.3 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi32337. 46 interactions.
    DIPiDIP-8807N.
    IntActiQ05521. 11 interactions.
    MINTiMINT-1360992.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05521.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni118 – 1269Phosphatase sequence motif I
    Regioni166 – 1694Phosphatase sequence motif II
    Regioni216 – 22712Phosphatase sequence motif IIIAdd
    BLAST

    Domaini

    The phosphatase sequence motif I (including Arg-125) and II (including His-169) are part of the cytoplasmic loop 2 and phosphatase sequence motif III (including His-223) is part of the cytoplasmic loop 3.

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00510000046723.
    HOGENOMiHOG000215098.
    InParanoidiQ05521.
    KOiK18693.
    OMAiDINGWAP.
    OrthoDBiEOG7QNVXN.

    Family and domain databases

    Gene3Di1.20.144.10. 1 hit.
    InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q05521-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL
    60 70 80 90 100
    TISHPYATTE RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL
    110 120 130 140 150
    LGLSLAWFST SFFTNFIKNW IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC
    160 170 180 190 200
    TTKNHERLLD GFRTTPSGHS SESFAGLGYL YFWLCGQLLT ESPLMPLWRK
    210 220 230 240 250
    MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH FFYRRIFPPI
    260 270 280
    DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM
    Length:289
    Mass (Da):33,514
    Last modified:November 1, 1996 - v1
    Checksum:i9CBEA0D7A0F0E13A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U51031 Genomic DNA. Translation: AAB64475.1.
    AY557744 Genomic DNA. Translation: AAS56070.1.
    BK006938 Genomic DNA. Translation: DAA12124.1.
    PIRiS70114.
    RefSeqiNP_010570.1. NM_001180592.1.

    Genome annotation databases

    EnsemblFungiiYDR284C; YDR284C; YDR284C.
    GeneIDi851878.
    KEGGisce:YDR284C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U51031 Genomic DNA. Translation: AAB64475.1.
    AY557744 Genomic DNA. Translation: AAS56070.1.
    BK006938 Genomic DNA. Translation: DAA12124.1.
    PIRiS70114.
    RefSeqiNP_010570.1. NM_001180592.1.

    3D structure databases

    ProteinModelPortaliQ05521.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32337. 46 interactions.
    DIPiDIP-8807N.
    IntActiQ05521. 11 interactions.
    MINTiMINT-1360992.

    Chemistry

    SwissLipidsiSLP:000000057.

    Protein family/group databases

    TCDBi9.B.105.3.2. the lead resistance fusion protein (pbrbc) family.

    PTM databases

    iPTMnetiQ05521.

    Proteomic databases

    MaxQBiQ05521.
    PeptideAtlasiQ05521.
    TopDownProteomicsiQ05521.

    Protocols and materials databases

    DNASUi851878.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR284C; YDR284C; YDR284C.
    GeneIDi851878.
    KEGGisce:YDR284C.

    Organism-specific databases

    EuPathDBiFungiDB:YDR284C.
    SGDiS000002692. DPP1.

    Phylogenomic databases

    GeneTreeiENSGT00510000046723.
    HOGENOMiHOG000215098.
    InParanoidiQ05521.
    KOiK18693.
    OMAiDINGWAP.
    OrthoDBiEOG7QNVXN.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15445.
    YEAST:YDR284C-MONOMER.
    BRENDAi3.1.3.81. 984.
    ReactomeiR-SCE-2029485. Role of phospholipids in phagocytosis.

    Miscellaneous databases

    NextBioi969841.
    PROiQ05521.

    Family and domain databases

    Gene3Di1.20.144.10. 1 hit.
    InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae."
      Wu W.-I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., Carman G.M.
      J. Biol. Chem. 271:1868-1876(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    5. "The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity."
      Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.
      J. Biol. Chem. 271:30548-30553(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc."
      Han G.-S., Johnston C.N., Chen X., Athenstaedt K., Daum G., Carman G.M.
      J. Biol. Chem. 276:10126-10133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
    7. "Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate phosphatase by transcription factor Gis1p."
      Oshiro J., Han G.-S., Iwanyshyn W.M., Conover K., Carman G.M.
      J. Biol. Chem. 278:31495-31503(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae."
      Han G.-S., Johnston C.N., Carman G.M.
      J. Biol. Chem. 279:5338-5345(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, PHOSPHATASE SEQUENCE MOTIF.
    9. "Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae."
      Toke D.A., McClintick M.L., Carman G.M.
      Biochemistry 38:14606-14613(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-125; HIS-169 AND HIS-223.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae."
      Oshiro J., Han G.-S., Carman G.M.
      Biochim. Biophys. Acta 1635:1-9(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, INDUCTION.
    13. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDPP1_YEAST
    AccessioniPrimary (citable) accession number: Q05521
    Secondary accession number(s): D6VSR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 132 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 3038 molecules/cell in log phase SD medium.1 Publication

    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.