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P51863

- VA0D1_MOUSE

UniProt

P51863 - VA0D1_MOUSE

Protein

V-type proton ATPase subunit d 1

Gene

Atp6v0d1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar 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. May play a role in coupling of proton transport and ATP hydrolysis. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium By similarity.By similarity

    Kineticsi

    1. KM=0.31 mM for ATP1 Publication

    GO - Molecular functioni

    1. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: MGI

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. brain development Source: Ensembl
    3. cilium assembly Source: UniProtKB

    Keywords - Biological processi

    Cilium biogenesis/degradation, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
    REACT_198345. Phagosomal maturation (early endosomal stage).
    REACT_198515. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.6. 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 1
    Short name:
    V-ATPase subunit d 1
    Alternative name(s):
    P39
    Physophilin
    V-ATPase 40 kDa accessory protein
    V-ATPase AC39 subunit
    Vacuolar proton pump subunit d 1
    Gene namesi
    Name:Atp6v0d1
    Synonyms:Atp6d
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1201778. Atp6v0d1.

    Subcellular locationi

    Membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Localizes to centrosome and the base of the cilium.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. axon terminus Source: Ensembl
    3. centrosome Source: Ensembl
    4. early endosome Source: MGI
    5. lysosomal membrane Source: Ensembl
    6. proton-transporting V-type ATPase, V0 domain Source: InterPro
    7. synaptic vesicle Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351V-type proton ATPase subunit d 1PRO_0000119351Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP51863.
    PaxDbiP51863.
    PRIDEiP51863.

    PTM databases

    PhosphoSiteiP51863.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Developmental stagei

    Expressed throughout early development.1 Publication

    Gene expression databases

    BgeeiP51863.
    CleanExiMM_ATP6V0D1.
    GenevestigatoriP51863.

    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'' and d).

    Protein-protein interaction databases

    BioGridi198264. 2 interactions.
    IntActiP51863. 8 interactions.
    MINTiMINT-1858223.

    Structurei

    3D structure databases

    ProteinModelPortaliP51863.
    SMRiP51863. Positions 28-54.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase V0D/AC39 subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG1527.
    GeneTreeiENSGT00390000002200.
    HOGENOMiHOG000199065.
    HOVERGENiHBG018065.
    InParanoidiP51863.
    KOiK02146.
    OMAiQMEAIHV.
    OrthoDBiEOG7KH9JT.
    PhylomeDBiP51863.
    TreeFamiTF300857.

    Family and domain databases

    InterProiIPR002843. ATPase_V0-cplx_csu/dsu.
    IPR016727. ATPase_V0-cplx_dsu.
    [Graphical view]
    PANTHERiPTHR11028. PTHR11028. 1 hit.
    PfamiPF01992. vATP-synt_AC39. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018497. V-ATP_synth_D. 1 hit.
    SUPFAMiSSF103486. SSF103486. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P51863-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ    50
    STDYGNFLAN EASPLTVSVI DDKLKEKMVV EFRHMRNHAY EPLASFLDFI 100
    TYSYMIDNVI LLITGTLHQR SIAELVPKCH PLGSFEQMEA VNIAQTPAEL 150
    YNAILVDTPL AAFFQDCISE QDLDEMNIEI IRNTLYKAYL ESFYKFCTLL 200
    GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL FPHCGRLYPE 250
    GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK 300
    LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI 350
    F 351
    Length:351
    Mass (Da):40,301
    Last modified:January 11, 2001 - v2
    Checksum:i62CDF67B982124C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231L → M in AAC83085. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13840 mRNA. Translation: AAC83085.1.
    U21549 mRNA. Translation: AAA92288.1.
    AB088408 mRNA. Translation: BAC57954.1.
    AK083372 mRNA. Translation: BAC38889.1.
    AK171515 mRNA. Translation: BAE42500.1.
    CCDSiCCDS22604.1.
    RefSeqiNP_038505.2. NM_013477.3.
    UniGeneiMm.17708.

    Genome annotation databases

    EnsembliENSMUST00000013304; ENSMUSP00000013304; ENSMUSG00000013160.
    GeneIDi11972.
    KEGGimmu:11972.
    UCSCiuc009ndg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13840 mRNA. Translation: AAC83085.1 .
    U21549 mRNA. Translation: AAA92288.1 .
    AB088408 mRNA. Translation: BAC57954.1 .
    AK083372 mRNA. Translation: BAC38889.1 .
    AK171515 mRNA. Translation: BAE42500.1 .
    CCDSi CCDS22604.1.
    RefSeqi NP_038505.2. NM_013477.3.
    UniGenei Mm.17708.

    3D structure databases

    ProteinModelPortali P51863.
    SMRi P51863. Positions 28-54.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198264. 2 interactions.
    IntActi P51863. 8 interactions.
    MINTi MINT-1858223.

    Protein family/group databases

    TCDBi 3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    PTM databases

    PhosphoSitei P51863.

    Proteomic databases

    MaxQBi P51863.
    PaxDbi P51863.
    PRIDEi P51863.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000013304 ; ENSMUSP00000013304 ; ENSMUSG00000013160 .
    GeneIDi 11972.
    KEGGi mmu:11972.
    UCSCi uc009ndg.1. mouse.

    Organism-specific databases

    CTDi 9114.
    MGIi MGI:1201778. Atp6v0d1.

    Phylogenomic databases

    eggNOGi COG1527.
    GeneTreei ENSGT00390000002200.
    HOGENOMi HOG000199065.
    HOVERGENi HBG018065.
    InParanoidi P51863.
    KOi K02146.
    OMAi QMEAIHV.
    OrthoDBi EOG7KH9JT.
    PhylomeDBi P51863.
    TreeFami TF300857.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.
    REACT_198345. Phagosomal maturation (early endosomal stage).
    REACT_198515. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi ATP6V0D1. mouse.
    NextBioi 280095.
    PROi P51863.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51863.
    CleanExi MM_ATP6V0D1.
    Genevestigatori P51863.

    Family and domain databases

    InterProi IPR002843. ATPase_V0-cplx_csu/dsu.
    IPR016727. ATPase_V0-cplx_dsu.
    [Graphical view ]
    PANTHERi PTHR11028. PTHR11028. 1 hit.
    Pfami PF01992. vATP-synt_AC39. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018497. V-ATP_synth_D. 1 hit.
    SUPFAMi SSF103486. SSF103486. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "cDNA sequences for mouse vacuolar ATPase subunits."
      Howell M.L., Dean G.E.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Brain Ac39/physophilin: cloning, coexpression and colocalization with synaptophysin."
      Carrion-Vazquez M., Fernandez A.M., Chowen J., Nieto-Sampedro M.
      Eur. J. Neurosci. 10:1153-1166(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    3. "Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits."
      Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.
      Gene 302:147-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Thymus.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 25-73; 87-128; 188-237; 240-288; 294-300; 304-320; 328-339 AND 344-351, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Expression and function of the mouse V-ATPase d subunit isoforms."
      Nishi T., Kawasaki-Nishi S., Forgac M.
      J. Biol. Chem. 278:46396-46402(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiVA0D1_MOUSE
    AccessioniPrimary (citable) accession number: P51863
    Secondary accession number(s): Q54A57, Q9QWJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3