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P27449

- VATL_HUMAN

UniProt

P27449 - VATL_HUMAN

Protein

V-type proton ATPase 16 kDa proteolipid subunit

Gene

ATP6V0C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei139 – 1391Essential for proton translocationBy similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. proton-transporting ATPase activity, rotational mechanism Source: ProtInc
    3. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. cellular iron ion homeostasis Source: Reactome
    3. insulin receptor signaling pathway Source: Reactome
    4. interaction with host Source: Reactome
    5. phagosome maturation Source: Reactome
    6. positive regulation of Wnt signaling pathway Source: UniProt
    7. proton transport Source: ProtInc
    8. transferrin transport Source: Reactome
    9. transmembrane transport Source: Reactome
    10. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER66-34368.
    ReactomeiREACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase 16 kDa proteolipid subunit
    Short name:
    V-ATPase 16 kDa proteolipid subunit
    Alternative name(s):
    Vacuolar proton pump 16 kDa proteolipid subunit
    Gene namesi
    Name:ATP6V0C
    Synonyms:ATP6C, ATP6L, ATPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:855. ATP6V0C.

    Subcellular locationi

    GO - Cellular componenti

    1. endosome membrane Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: ProtInc
    4. lysosomal membrane Source: UniProtKB
    5. phagocytic vesicle membrane Source: Reactome
    6. proton-transporting V-type ATPase, V0 domain Source: InterPro

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25149.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 155155V-type proton ATPase 16 kDa proteolipid subunitPRO_0000071743Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by RNF182, leading to its degradation via the ubiquitin-proteasome pathway.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP27449.
    PaxDbiP27449.
    PRIDEiP27449.

    PTM databases

    PhosphoSiteiP27449.

    Expressioni

    Gene expression databases

    BgeeiP27449.
    CleanExiHS_ATP6V0C.
    GenevestigatoriP27449.

    Interactioni

    Subunit structurei

    V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein; which is present as a hexamer that forms the proton-conducting pore). Interacts with LASS2. Interacts with HTLV-1 accessory protein p12I. Interacts with RNF182; this interaction leads to ubiquitination and degradation via the proteasome pathway.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CERS2Q96G233EBI-721179,EBI-1057080
    E5P0CK452EBI-721179,EBI-7015490From a different organism.

    Protein-protein interaction databases

    BioGridi107010. 4 interactions.
    IntActiP27449. 6 interactions.
    MINTiMINT-1414327.
    STRINGi9606.ENSP00000329757.

    Structurei

    3D structure databases

    ProteinModelPortaliP27449.
    SMRiP27449. Positions 14-153.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010LumenalSequence Analysis
    Topological domaini34 – 5522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini77 – 9216LumenalSequence AnalysisAdd
    BLAST
    Topological domaini115 – 13117CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini153 – 1553LumenalSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3323HelicalSequence AnalysisAdd
    BLAST
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei93 – 11422HelicalSequence AnalysisAdd
    BLAST
    Transmembranei132 – 15221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0636.
    HOGENOMiHOG000056520.
    HOVERGENiHBG002712.
    InParanoidiP27449.
    KOiK02155.
    OMAiMATELCP.
    OrthoDBiEOG7FV3RW.
    PhylomeDBiP27449.
    TreeFamiTF300025.

    Family and domain databases

    HAMAPiMF_01396. ATP_synth_c_bact.
    InterProiIPR002379. ATPase_proteolipid_c_like_dom.
    IPR000245. ATPase_proteolipid_csu.
    IPR011555. ATPase_proteolipid_su_C_euk.
    [Graphical view]
    PfamiPF00137. ATP-synt_C. 2 hits.
    [Graphical view]
    PRINTSiPR00122. VACATPASE.
    SUPFAMiSSF81333. SSF81333. 2 hits.
    TIGRFAMsiTIGR01100. V_ATP_synt_C. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27449-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE    50
    QIMKSIIPVV MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG 100
    LSGLAAGFAI GIVGDAGVRG TAQQPRLFVG MILILIFAEV LGLYGLIVAL 150
    ILSTK 155
    Length:155
    Mass (Da):15,736
    Last modified:August 1, 1992 - v1
    Checksum:i91141854A0492A5B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62762 mRNA. Translation: AAA60039.1.
    CR541930 mRNA. Translation: CAG46728.1.
    CR541951 mRNA. Translation: CAG46749.1.
    BT007155 mRNA. Translation: AAP35819.1.
    BC004537 mRNA. Translation: AAH04537.1.
    BC007389 mRNA. Translation: AAH07389.1.
    BC007759 mRNA. Translation: AAH07759.1.
    BC009290 mRNA. Translation: AAH09290.1.
    CCDSiCCDS10470.1.
    PIRiA39367.
    RefSeqiNP_001185498.1. NM_001198569.1.
    NP_001685.1. NM_001694.3.
    UniGeneiHs.389107.

    Genome annotation databases

    EnsembliENST00000330398; ENSP00000329757; ENSG00000185883.
    GeneIDi527.
    KEGGihsa:527.
    UCSCiuc002cqn.3. human.

    Polymorphism databases

    DMDMi137479.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62762 mRNA. Translation: AAA60039.1 .
    CR541930 mRNA. Translation: CAG46728.1 .
    CR541951 mRNA. Translation: CAG46749.1 .
    BT007155 mRNA. Translation: AAP35819.1 .
    BC004537 mRNA. Translation: AAH04537.1 .
    BC007389 mRNA. Translation: AAH07389.1 .
    BC007759 mRNA. Translation: AAH07759.1 .
    BC009290 mRNA. Translation: AAH09290.1 .
    CCDSi CCDS10470.1.
    PIRi A39367.
    RefSeqi NP_001185498.1. NM_001198569.1.
    NP_001685.1. NM_001694.3.
    UniGenei Hs.389107.

    3D structure databases

    ProteinModelPortali P27449.
    SMRi P27449. Positions 14-153.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107010. 4 interactions.
    IntActi P27449. 6 interactions.
    MINTi MINT-1414327.
    STRINGi 9606.ENSP00000329757.

    PTM databases

    PhosphoSitei P27449.

    Polymorphism databases

    DMDMi 137479.

    Proteomic databases

    MaxQBi P27449.
    PaxDbi P27449.
    PRIDEi P27449.

    Protocols and materials databases

    DNASUi 527.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330398 ; ENSP00000329757 ; ENSG00000185883 .
    GeneIDi 527.
    KEGGi hsa:527.
    UCSCi uc002cqn.3. human.

    Organism-specific databases

    CTDi 527.
    GeneCardsi GC16P002563.
    HGNCi HGNC:855. ATP6V0C.
    MIMi 108745. gene.
    neXtProti NX_P27449.
    PharmGKBi PA25149.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0636.
    HOGENOMi HOG000056520.
    HOVERGENi HBG002712.
    InParanoidi P27449.
    KOi K02155.
    OMAi MATELCP.
    OrthoDBi EOG7FV3RW.
    PhylomeDBi P27449.
    TreeFami TF300025.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER66-34368.
    Reactomei REACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    GeneWikii ATP6V0C.
    GenomeRNAii 527.
    NextBioi 2187.
    PROi P27449.
    SOURCEi Search...

    Gene expression databases

    Bgeei P27449.
    CleanExi HS_ATP6V0C.
    Genevestigatori P27449.

    Family and domain databases

    HAMAPi MF_01396. ATP_synth_c_bact.
    InterProi IPR002379. ATPase_proteolipid_c_like_dom.
    IPR000245. ATPase_proteolipid_csu.
    IPR011555. ATPase_proteolipid_su_C_euk.
    [Graphical view ]
    Pfami PF00137. ATP-synt_C. 2 hits.
    [Graphical view ]
    PRINTSi PR00122. VACATPASE.
    SUPFAMi SSF81333. SSF81333. 2 hits.
    TIGRFAMsi TIGR01100. V_ATP_synt_C. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "CpG island in the region of an autosomal dominant polycystic kidney disease locus defines the 5' end of a gene encoding a putative proton channel."
      Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D., Reeders S.T.
      Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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, Muscle and Skin.
    5. "Vacuolar type H(+)-ATPase genes: presence of four genes including pseudogenes for the 16-kDa proteolipid subunit in the human genome."
      Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.
      Biochem. Biophys. Res. Commun. 183:856-863(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-155.
    6. "Mapping of the intermolecular association of human T cell leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa subunit protein."
      Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.
      J. Gen. Virol. 76:1909-1916(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
    7. "Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1."
      Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D., Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y., Gu J.-R.
      Genomics 77:58-64(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LASS2.
    8. "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradation."
      Liu Q.Y., Lei J.X., Sikorska M., Liu R.
      Mol. Neurodegener. 3:4-4(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF182, UBIQUITINATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVATL_HUMAN
    AccessioniPrimary (citable) accession number: P27449
    Secondary accession number(s): Q6FH26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 149 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