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Protein

V-type proton ATPase subunit d 1

Gene

Atp6v0d1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: MGI

    GO - Biological processi

    Complete GO annotation...

    Keywords - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_290403. Transferrin endocytosis and recycling.
    REACT_299823. Ion channel transport.
    REACT_324664. Insulin receptor 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 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:1201778. Atp6v0d1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.
    GenevisibleiP51863. MM.

    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. 5 interactions.
    IntActiP51863. 8 interactions.
    MINTiMINT-1858223.
    STRINGi10090.ENSMUSP00000013304.

    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.
    OMAiFMDFITY.
    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

            10         20         30         40         50
    MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ
    60 70 80 90 100
    STDYGNFLAN EASPLTVSVI DDKLKEKMVV EFRHMRNHAY EPLASFLDFI
    110 120 130 140 150
    TYSYMIDNVI LLITGTLHQR SIAELVPKCH PLGSFEQMEA VNIAQTPAEL
    160 170 180 190 200
    YNAILVDTPL AAFFQDCISE QDLDEMNIEI IRNTLYKAYL ESFYKFCTLL
    210 220 230 240 250
    GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL FPHCGRLYPE
    260 270 280 290 300
    GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
    310 320 330 340 350
    LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI

    F
    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 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi198264. 5 interactions.
    IntActiP51863. 8 interactions.
    MINTiMINT-1858223.
    STRINGi10090.ENSMUSP00000013304.

    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.

    PTM databases

    PhosphoSiteiP51863.

    Proteomic databases

    MaxQBiP51863.
    PaxDbiP51863.
    PRIDEiP51863.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi9114.
    MGIiMGI:1201778. Atp6v0d1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    ReactomeiREACT_290403. Transferrin endocytosis and recycling.
    REACT_299823. Ion channel transport.
    REACT_324664. Insulin receptor recycling.

    Miscellaneous databases

    ChiTaRSiAtp6v0d1. mouse.
    NextBioi280095.
    PROiP51863.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP51863.
    CleanExiMM_ATP6V0D1.
    GenevisibleiP51863. MM.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 130 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

    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 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.