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P50516

- VATA_MOUSE

UniProt

P50516 - VATA_MOUSE

Protein

V-type proton ATPase catalytic subunit A

Gene

Atp6v1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

    Catalytic activityi

    ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi250 – 2578ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_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 catalytic subunit A (EC:3.6.3.14)
    Short name:
    V-ATPase subunit A
    Alternative name(s):
    V-ATPase 69 kDa subunit
    Vacuolar proton pump subunit alpha
    Gene namesi
    Name:Atp6v1a
    Synonyms:Atp6a1, Atp6a2, Atp6v1a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1201780. Atp6v1a.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. lysosomal membrane Source: Ensembl
    4. microvillus Source: UniProtKB
    5. mitochondrion Source: MGI
    6. plasma membrane Source: UniProtKB
    7. proton-transporting V-type ATPase, V1 domain Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 617617V-type proton ATPase catalytic subunit APRO_0000144561Add
    BLAST

    Proteomic databases

    MaxQBiP50516.
    PaxDbiP50516.
    PRIDEiP50516.

    PTM databases

    PhosphoSiteiP50516.

    Expressioni

    Gene expression databases

    ArrayExpressiP50516.
    BgeeiP50516.
    CleanExiMM_ATP6V1A.
    GenevestigatoriP50516.

    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).

    Protein-protein interaction databases

    BioGridi198261. 6 interactions.
    IntActiP50516. 108 interactions.
    MINTiMINT-1866559.

    Structurei

    3D structure databases

    ProteinModelPortaliP50516.
    SMRiP50516. Positions 40-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Phylogenomic databases

    eggNOGiCOG1155.
    GeneTreeiENSGT00550000074787.
    HOVERGENiHBG053351.
    InParanoidiP50516.
    KOiK02145.
    OMAiENKITWN.
    OrthoDBiEOG7Q8CMM.
    PhylomeDBiP50516.
    TreeFamiTF300811.

    Family and domain databases

    Gene3Di1.10.1140.10. 1 hit.
    3.40.50.300. 2 hits.
    HAMAPiMF_00309. ATP_synth_A_arch.
    InterProiIPR020003. ATPase_a/bsu_AS.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR005725. ATPase_V1-cplx_asu.
    IPR027417. P-loop_NTPase.
    IPR022878. V-ATPase_asu.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50516-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL    50
    VGEIIRLEGD MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD 100
    GIQRPLSDIS SQTQSIYIPR GVNVSALSRD IKWEFIPSKN LRVGSHITGG 150
    DIYGIVNENS LIKHKIMLPP RNRGSVTYIA PPGNYDASDV VLELEFEGVK 200
    EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC VQGGTTAIPG 250
    AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG 300
    KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS 350
    TSRWAEALRE ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER 400
    EGSVSIVGAV SPPGGDFSDP VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW 450
    LISYSKYMRA LDEYYDKHFT EFVPLRTKAK EILQEEEDLA EIVQLVGKAS 500
    LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM LSNMISFYDM 550
    ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD 600
    YAQLLEDMQN AFRSLED 617
    Length:617
    Mass (Da):68,326
    Last modified:April 17, 2007 - v2
    Checksum:iD46AC76D9C7580A7
    GO
    Isoform 2 (identifier: P50516-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         499-509: ASLAETDKITL → VRGGCTGCHAG
         510-617: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:509
    Mass (Da):55,595
    Checksum:i55D9F7CCEF00CC89
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861L → R in AAC52410. (PubMed:8741845)Curated
    Sequence conflicti189 – 1891D → N in AAC52410. (PubMed:8741845)Curated
    Sequence conflicti302 – 3021V → A in AAC52410. (PubMed:8741845)Curated
    Sequence conflicti330 – 3301G → V in BAE39074. (PubMed:16141072)Curated
    Sequence conflicti487 – 4871E → G in AAC52410. (PubMed:8741845)Curated
    Sequence conflicti616 – 6161E → G in BAE31963. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei499 – 50911ASLAETDKITL → VRGGCTGCHAG in isoform 2. 1 PublicationVSP_024628Add
    BLAST
    Alternative sequencei510 – 617108Missing in isoform 2. 1 PublicationVSP_024629Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13837 Genomic DNA. Translation: AAC52410.1.
    AK140873 mRNA. Translation: BAE24506.1.
    AK149833 mRNA. Translation: BAE29112.1.
    AK152785 mRNA. Translation: BAE31494.1.
    AK153403 mRNA. Translation: BAE31963.1.
    AK154869 mRNA. Translation: BAE32890.1.
    AK160792 mRNA. Translation: BAE36015.1.
    AK166857 mRNA. Translation: BAE39074.1.
    AK170721 mRNA. Translation: BAE41978.1.
    BC038392 mRNA. Translation: AAH38392.1.
    CCDSiCCDS28182.1. [P50516-1]
    RefSeqiNP_031534.2. NM_007508.5. [P50516-1]
    XP_006521783.1. XM_006521720.1. [P50516-1]
    XP_006521784.1. XM_006521721.1. [P50516-1]
    UniGeneiMm.217787.

    Genome annotation databases

    EnsembliENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459. [P50516-1]
    ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459. [P50516-1]
    GeneIDi11964.
    KEGGimmu:11964.
    UCSCiuc007zgu.1. mouse. [P50516-1]
    uc007zgw.1. mouse. [P50516-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13837 Genomic DNA. Translation: AAC52410.1 .
    AK140873 mRNA. Translation: BAE24506.1 .
    AK149833 mRNA. Translation: BAE29112.1 .
    AK152785 mRNA. Translation: BAE31494.1 .
    AK153403 mRNA. Translation: BAE31963.1 .
    AK154869 mRNA. Translation: BAE32890.1 .
    AK160792 mRNA. Translation: BAE36015.1 .
    AK166857 mRNA. Translation: BAE39074.1 .
    AK170721 mRNA. Translation: BAE41978.1 .
    BC038392 mRNA. Translation: AAH38392.1 .
    CCDSi CCDS28182.1. [P50516-1 ]
    RefSeqi NP_031534.2. NM_007508.5. [P50516-1 ]
    XP_006521783.1. XM_006521720.1. [P50516-1 ]
    XP_006521784.1. XM_006521721.1. [P50516-1 ]
    UniGenei Mm.217787.

    3D structure databases

    ProteinModelPortali P50516.
    SMRi P50516. Positions 40-587.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198261. 6 interactions.
    IntActi P50516. 108 interactions.
    MINTi MINT-1866559.

    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 P50516.

    Proteomic databases

    MaxQBi P50516.
    PaxDbi P50516.
    PRIDEi P50516.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063661 ; ENSMUSP00000066886 ; ENSMUSG00000052459 . [P50516-1 ]
    ENSMUST00000114666 ; ENSMUSP00000110314 ; ENSMUSG00000052459 . [P50516-1 ]
    GeneIDi 11964.
    KEGGi mmu:11964.
    UCSCi uc007zgu.1. mouse. [P50516-1 ]
    uc007zgw.1. mouse. [P50516-2 ]

    Organism-specific databases

    CTDi 523.
    MGIi MGI:1201780. Atp6v1a.

    Phylogenomic databases

    eggNOGi COG1155.
    GeneTreei ENSGT00550000074787.
    HOVERGENi HBG053351.
    InParanoidi P50516.
    KOi K02145.
    OMAi ENKITWN.
    OrthoDBi EOG7Q8CMM.
    PhylomeDBi P50516.
    TreeFami TF300811.

    Enzyme and pathway databases

    Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
    REACT_198515. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi ATP6V1A. mouse.
    NextBioi 280087.
    PROi P50516.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50516.
    Bgeei P50516.
    CleanExi MM_ATP6V1A.
    Genevestigatori P50516.

    Family and domain databases

    Gene3Di 1.10.1140.10. 1 hit.
    3.40.50.300. 2 hits.
    HAMAPi MF_00309. ATP_synth_A_arch.
    InterProi IPR020003. ATPase_a/bsu_AS.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR005725. ATPase_V1-cplx_asu.
    IPR027417. P-loop_NTPase.
    IPR022878. V-ATPase_asu.
    [Graphical view ]
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01042. V-ATPase_V1_A. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts."
      Laitala T., Howell M.L., Dean G.E., Vaananen H.K.
      Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow and Head.
    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] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary tumor.
    4. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 45-56; 143-163; 242-251; 253-262; 266-280; 324-338; 514-530 AND 599-613, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiVATA_MOUSE
    AccessioniPrimary (citable) accession number: P50516
    Secondary accession number(s): Q3TKS0
    , Q3U5W3, Q3U777, Q3UDZ9, Q3US31, Q8CHX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 132 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