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P61421

- VA0D1_HUMAN

UniProt

P61421 - VA0D1_HUMAN

Protein

V-type proton ATPase subunit d 1

Gene

ATP6V0D1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (24 May 2004)
      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 By similarity. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium By similarity.By similarity

    GO - Molecular functioni

    1. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: Ensembl
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. ATP hydrolysis coupled proton transport Source: InterPro
    3. brain development Source: Ensembl
    4. cellular iron ion homeostasis Source: Reactome
    5. cellular protein metabolic process Source: Reactome
    6. cilium assembly Source: UniProtKB
    7. endoplasmic reticulum unfolded protein response Source: Reactome
    8. insulin receptor signaling pathway Source: Reactome
    9. interaction with host Source: Reactome
    10. phagosome maturation Source: Reactome
    11. proton transport Source: UniProtKB
    12. transferrin transport Source: Reactome
    13. transmembrane transport Source: Reactome

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08417-MONOMER.
    ReactomeiREACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.4. 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):
    32 kDa accessory protein
    V-ATPase 40 kDa accessory protein
    V-ATPase AC39 subunit
    Short name:
    p39
    Vacuolar proton pump subunit d 1
    Gene namesi
    Name:ATP6V0D1
    Synonyms:ATP6D, VPATPD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:13724. ATP6V0D1.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    Note: Localizes to centrosome and the base of the cilium.

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. axon terminus Source: Ensembl
    3. early endosome Source: Ensembl
    4. endosome membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. lysosomal membrane Source: UniProtKB
    7. membrane Source: UniProtKB
    8. phagocytic vesicle membrane Source: Reactome
    9. proton-transporting V-type ATPase, V0 domain Source: InterPro
    10. synaptic vesicle Source: Ensembl
    11. vacuolar proton-transporting V-type ATPase complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25150.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351V-type proton ATPase subunit d 1PRO_0000119350Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP61421.
    PaxDbiP61421.
    PeptideAtlasiP61421.
    PRIDEiP61421.

    PTM databases

    PhosphoSiteiP61421.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Gene expression databases

    ArrayExpressiP61421.
    BgeeiP61421.
    CleanExiHS_ATP6V0D1.
    GenevestigatoriP61421.

    Organism-specific databases

    HPAiHPA016938.

    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

    BioGridi114564. 10 interactions.
    IntActiP61421. 2 interactions.
    MINTiMINT-5006032.
    STRINGi9606.ENSP00000290949.

    Structurei

    3D structure databases

    ProteinModelPortaliP61421.
    SMRiP61421. Positions 28-55.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1527.
    HOGENOMiHOG000199065.
    HOVERGENiHBG018065.
    InParanoidiP61421.
    KOiK02146.
    OrthoDBiEOG7KH9JT.
    PhylomeDBiP61421.
    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.

    P61421-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ    50
    STDYGNFLAN EASPLTVSVI DDRLKEKMVV 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):40,329
    Last modified:May 24, 2004 - v1
    Checksum:iA720F8A87511203C
    GO

    Sequence cautioni

    The sequence CAA50591.1 differs from that shown. Reason: Frameshift at positions 22, 25, 64 and 66.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271V → E in CAA50591. (PubMed:8250920)Curated
    Sequence conflicti266 – 2672NV → KL in CAA50591. (PubMed:8250920)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71490 mRNA. Translation: CAA50591.1. Frameshift.
    BC008861 mRNA. Translation: AAH08861.1.
    L05087 mRNA. Translation: AAC15852.1.
    CCDSiCCDS10838.1.
    RefSeqiNP_004682.2. NM_004691.4.
    UniGeneiHs.106876.

    Genome annotation databases

    EnsembliENST00000290949; ENSP00000290949; ENSG00000159720.
    GeneIDi9114.
    KEGGihsa:9114.
    UCSCiuc002ete.1. human.

    Polymorphism databases

    DMDMi47606646.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71490 mRNA. Translation: CAA50591.1 . Frameshift.
    BC008861 mRNA. Translation: AAH08861.1 .
    L05087 mRNA. Translation: AAC15852.1 .
    CCDSi CCDS10838.1.
    RefSeqi NP_004682.2. NM_004691.4.
    UniGenei Hs.106876.

    3D structure databases

    ProteinModelPortali P61421.
    SMRi P61421. Positions 28-55.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114564. 10 interactions.
    IntActi P61421. 2 interactions.
    MINTi MINT-5006032.
    STRINGi 9606.ENSP00000290949.

    Protein family/group databases

    TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    PTM databases

    PhosphoSitei P61421.

    Polymorphism databases

    DMDMi 47606646.

    Proteomic databases

    MaxQBi P61421.
    PaxDbi P61421.
    PeptideAtlasi P61421.
    PRIDEi P61421.

    Protocols and materials databases

    DNASUi 9114.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290949 ; ENSP00000290949 ; ENSG00000159720 .
    GeneIDi 9114.
    KEGGi hsa:9114.
    UCSCi uc002ete.1. human.

    Organism-specific databases

    CTDi 9114.
    GeneCardsi GC16M067471.
    HGNCi HGNC:13724. ATP6V0D1.
    HPAi HPA016938.
    MIMi 607028. gene.
    neXtProti NX_P61421.
    PharmGKBi PA25150.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1527.
    HOGENOMi HOG000199065.
    HOVERGENi HBG018065.
    InParanoidi P61421.
    KOi K02146.
    OrthoDBi EOG7KH9JT.
    PhylomeDBi P61421.
    TreeFami TF300857.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08417-MONOMER.
    Reactomei REACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_18273. XBP1(S) activates chaperone genes.
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi ATP6V0D1. human.
    GeneWikii ATP6V0D1.
    GenomeRNAii 9114.
    NextBioi 34161.
    PROi P61421.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61421.
    Bgeei P61421.
    CleanExi HS_ATP6V0D1.
    Genevestigatori P61421.

    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. "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase."
      van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.
      Biochem. Biophys. Res. Commun. 197:15-21(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Osteoclastoma.
    2. "Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase."
      Agarwal A.K., White P.C.
      Biochem. Biophys. Res. Commun. 279:543-547(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Expressed sequence tags from a human cell line."
      Bhat K.S.
      Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 264-351.
    5. "Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis."
      Smith A.N., Borthwick K.J., Karet F.E.
      Gene 297:169-177(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."
      Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., Shu X., Pei D.
      Cell Res. 22:333-345(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiVA0D1_HUMAN
    AccessioniPrimary (citable) accession number: P61421
    Secondary accession number(s): P12953, Q02547
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3