Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Diacylglycerol pyrophosphate phosphatase 1

Gene

DPP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

Present with 3038 molecules/cell in log phase SD medium.1 Publication

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

    • phospholipid metabolic process Source: SGD

    Keywordsi

    Molecular functionHydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:YDR284C-MONOMER
    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 databases

    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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 21VacuolarSequence analysisAdd BLAST21
    Transmembranei22 – 42Helical; Name=1Sequence analysisAdd BLAST21
    Topological domaini43 – 65CytoplasmicSequence analysisAdd BLAST23
    Transmembranei66 – 86Helical; Name=2Sequence analysisAdd BLAST21
    Topological domaini87 – 92VacuolarSequence analysis6
    Transmembranei93 – 113Helical; Name=3Sequence analysisAdd BLAST21
    Topological domaini114 – 172CytoplasmicSequence analysisAdd BLAST59
    Transmembranei173 – 193Helical; Name=4Sequence analysisAdd BLAST21
    Transmembranei194 – 214Helical; Name=5Sequence analysisAdd BLAST21
    Topological domaini215 – 222CytoplasmicSequence analysis8
    Transmembranei223 – 243Helical; Name=6Sequence analysisAdd BLAST21
    Topological domaini244 – 289VacuolarSequence analysisAdd BLAST46

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi125R → A: Complete loss of DGPP phosphatase activity. 1 Publication1
    Mutagenesisi169H → A: 91% decrease of DGPP phosphatase activity. 1 Publication1
    Mutagenesisi223H → A: Complete loss of DGPP phosphatase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002209181 – 289Diacylglycerol pyrophosphate phosphatase 1Add BLAST289

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei285PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05521
    PaxDbiQ05521
    PRIDEiQ05521
    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, 61 interactors
    DIPiDIP-8807N
    IntActiQ05521, 11 interactors
    MINTiQ05521
    STRINGi4932.YDR284C

    Structurei

    3D structure databases

    ProteinModelPortaliQ05521
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni118 – 126Phosphatase sequence motif I9
    Regioni166 – 169Phosphatase sequence motif II4
    Regioni216 – 227Phosphatase sequence motif IIIAdd BLAST12

    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
    OMAiIQYPFAV
    OrthoDBiEOG092C29DM

    Family and domain databases

    InterProiView protein in InterPro
    IPR036938 P_Acid_Pase_2/haloperoxi_sf
    IPR000326 P_Acid_Pase_2/haloperoxidase
    PfamiView protein in Pfam
    PF01569 PAP2, 1 hit
    SMARTiView protein in SMART
    SM00014 acidPPc, 1 hit
    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

    Similar proteinsi

    Entry informationi

    Entry nameiDPP1_YEAST
    AccessioniPrimary (citable) accession number: Q05521
    Secondary accession number(s): D6VSR4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: November 1, 1996
    Last modified: May 23, 2018
    This is version 147 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health