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P32610

- VATD_YEAST

UniProt

P32610 - VATD_YEAST

Protein

V-type proton ATPase subunit D

Gene

VMA8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. proton-transporting ATPase activity, rotational mechanism Source: SGD

    GO - Biological processi

    1. hydrogen ion transmembrane transport Source: GOC
    2. vacuolar acidification Source: SGD

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30169-MONOMER.
    ReactomeiREACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase subunit D
    Short name:
    V-ATPase subunit D
    Alternative name(s):
    Vacuolar proton pump subunit D
    Gene namesi
    Name:VMA8
    Ordered Locus Names:YEL051W
    ORF Names:SYGP-ORF11
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYEL051w.
    SGDiS000000777. VMA8.

    Subcellular locationi

    GO - Cellular componenti

    1. fungal-type vacuole membrane Source: SGD
    2. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 256256V-type proton ATPase subunit DPRO_0000144244Add
    BLAST

    Proteomic databases

    MaxQBiP32610.
    PaxDbiP32610.
    PeptideAtlasiP32610.

    Expressioni

    Gene expression databases

    GenevestigatoriP32610.

    Interactioni

    Subunit structurei

    V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAV1P471042EBI-20264,EBI-25471
    VMA7P391115EBI-20264,EBI-20272

    Protein-protein interaction databases

    BioGridi36678. 204 interactions.
    DIPiDIP-2959N.
    IntActiP32610. 36 interactions.
    MINTiMINT-640736.
    STRINGi4932.YEL051W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32610.
    SMRiP32610. Positions 10-209.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase D subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG1394.
    GeneTreeiENSGT00390000010770.
    HOGENOMiHOG000230791.
    KOiK02149.
    OMAiQTAFMIL.
    OrthoDBiEOG7PCJTH.

    Family and domain databases

    InterProiIPR002699. V_ATPase_D.
    [Graphical view]
    PANTHERiPTHR11671. PTHR11671. 1 hit.
    PfamiPF01813. ATP-synt_D. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00309. V_ATPase_subD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32610-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGNREQVFP TRMTLGLMKT KLKGANQGYS LLKRKSEALT KRFRDITKRI    50
    DDAKQKMGRV MQTAAFSLAE VSYATGENIG YQVQESVSTA RFKVRARQEN 100
    VSGVYLSQFE SYIDPEINDF RLTGLGRGGQ QVQRAKEIYS RAVETLVELA 150
    SLQTAFIILD EVIKVTNRRV NAIEHVIIPR TENTIAYINS ELDELDREEF 200
    YRLKKVQEKK QNETAKLDAE MKLKRDRAEQ DASEVAADEE PQGETLVADQ 250
    EDDVIF 256
    Length:256
    Mass (Da):29,194
    Last modified:October 1, 1993 - v1
    Checksum:iFDE93E1FAF0AEC5B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18779 Genomic DNA. Translation: AAB64991.1.
    BK006939 Genomic DNA. Translation: DAA07603.1.
    PIRiS30826.
    RefSeqiNP_010863.1. NM_001178866.1.

    Genome annotation databases

    EnsemblFungiiYEL051W; YEL051W; YEL051W.
    GeneIDi856659.
    KEGGisce:YEL051W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18779 Genomic DNA. Translation: AAB64991.1 .
    BK006939 Genomic DNA. Translation: DAA07603.1 .
    PIRi S30826.
    RefSeqi NP_010863.1. NM_001178866.1.

    3D structure databases

    ProteinModelPortali P32610.
    SMRi P32610. Positions 10-209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36678. 204 interactions.
    DIPi DIP-2959N.
    IntActi P32610. 36 interactions.
    MINTi MINT-640736.
    STRINGi 4932.YEL051W.

    Protein family/group databases

    TCDBi 3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Proteomic databases

    MaxQBi P32610.
    PaxDbi P32610.
    PeptideAtlasi P32610.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL051W ; YEL051W ; YEL051W .
    GeneIDi 856659.
    KEGGi sce:YEL051W.

    Organism-specific databases

    CYGDi YEL051w.
    SGDi S000000777. VMA8.

    Phylogenomic databases

    eggNOGi COG1394.
    GeneTreei ENSGT00390000010770.
    HOGENOMi HOG000230791.
    KOi K02149.
    OMAi QTAFMIL.
    OrthoDBi EOG7PCJTH.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30169-MONOMER.
    Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Miscellaneous databases

    NextBioi 982652.
    PROi P32610.

    Gene expression databases

    Genevestigatori P32610.

    Family and domain databases

    InterProi IPR002699. V_ATPase_D.
    [Graphical view ]
    PANTHERi PTHR11671. PTHR11671. 1 hit.
    Pfami PF01813. ATP-synt_D. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00309. V_ATPase_subD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "VMA8 encodes a 32-kDa V1 subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase required for function and assembly of the enzyme complex."
      Graham L.A., Hill K.J., Stevens T.H.
      J. Biol. Chem. 270:15037-15044(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-12; 170-179 AND 182-187.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "A bovine cDNA and a yeast gene (VMA8) encoding the subunit D of the vacuolar H(+)-ATPase."
      Nelson H., Mandiyan S., Nelson N.
      Proc. Natl. Acad. Sci. U.S.A. 92:497-501(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
      Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
      Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAV1 AND RAV2.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVATD_YEAST
    AccessioniPrimary (citable) accession number: P32610
    Secondary accession number(s): D3DLJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    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 8500 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3