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P38606

- VATA_HUMAN

UniProt

P38606 - VATA_HUMAN

Protein

V-type proton ATPase catalytic subunit A

Gene

ATP6V1A

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 2 (02 Aug 2002)
      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
    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. transferrin transport Source: Reactome
    7. transmembrane transport Source: Reactome
    8. transport Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03781-MONOMER.
    ReactomeiREACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    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 catalytic subunit A (EC:3.6.3.14)
    Short name:
    V-ATPase subunit A
    Alternative name(s):
    V-ATPase 69 kDa subunit
    Vacuolar ATPase isoform VA68
    Vacuolar proton pump subunit alpha
    Gene namesi
    Name:ATP6V1A
    Synonyms:ATP6A1, ATP6V1A1, VPP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:851. ATP6V1A.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of plasma membrane Source: ProtInc
    5. lysosomal membrane Source: UniProtKB
    6. microvillus Source: Ensembl
    7. mitochondrion Source: Ensembl
    8. plasma membrane Source: UniProtKB
    9. proton-transporting two-sector ATPase complex Source: ProtInc
    10. proton-transporting V-type ATPase, V1 domain Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25152.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 617617V-type proton ATPase catalytic subunit APRO_0000144560Add
    BLAST

    Proteomic databases

    MaxQBiP38606.
    PaxDbiP38606.
    PeptideAtlasiP38606.
    PRIDEiP38606.

    PTM databases

    PhosphoSiteiP38606.

    Expressioni

    Tissue specificityi

    Present in all tissues analyzed.

    Gene expression databases

    ArrayExpressiP38606.
    BgeeiP38606.
    CleanExiHS_ATP6V1A.
    GenevestigatoriP38606.

    Organism-specific databases

    HPAiCAB006910.
    HPA035083.
    HPA035084.

    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

    BioGridi107007. 47 interactions.
    IntActiP38606. 63 interactions.
    MINTiMINT-224589.
    STRINGi9606.ENSP00000273398.

    Structurei

    3D structure databases

    ProteinModelPortaliP38606.
    SMRiP38606. Positions 40-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Phylogenomic databases

    eggNOGiCOG1155.
    HOGENOMiHOG000161057.
    HOVERGENiHBG053351.
    InParanoidiP38606.
    KOiK02145.
    OMAiENKITWN.
    OrthoDBiEOG7Q8CMM.
    PhylomeDBiP38606.
    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: P38606-1) [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

    MDFSKLPKIL DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL    50
    VGEIIRLEGD MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD 100
    GIQRPLSDIS SQTQSIYIPR GVNVSALSRD IKWDFTPCKN LRVGSHITGG 150
    DIYGIVSENS LIKHKIMLPP RNRGTVTYIA PPGNYDTSDV VLELEFEGVK 200
    EKFTMVQVWP 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 LSNMIAFYDM 550
    ARRAVETTAQ SDNKITWSII REHMGDILYK LSSMKFKDPL KDGEAKIKSD 600
    YAQLLEDMQN AFRSLED 617
    Length:617
    Mass (Da):68,304
    Last modified:August 2, 2002 - v2
    Checksum:iDB409A8731D772CB
    GO
    Isoform 2 (identifier: P38606-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:584
    Mass (Da):64,736
    Checksum:i6F677073A4B4A48B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711S → C in AAA83249. (PubMed:8463241)Curated
    Sequence conflicti89 – 902EL → DV in AAA83249. (PubMed:8463241)Curated
    Sequence conflicti211 – 2111V → A in AAA83249. (PubMed:8463241)Curated
    Sequence conflicti211 – 2111V → A in AAF14870. (PubMed:10931946)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_056408Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09235 mRNA. Translation: AAA83249.1.
    AF113129 mRNA. Translation: AAF14870.1.
    BT006672 mRNA. Translation: AAP35318.1.
    AK293804 mRNA. Translation: BAH11601.1.
    AK314779 mRNA. Translation: BAG37315.1.
    AC079944 Genomic DNA. No translation available.
    AC108693 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79625.1.
    CH471052 Genomic DNA. Translation: EAW79626.1.
    BC013138 mRNA. Translation: AAH13138.1.
    CCDSiCCDS2976.1.
    PIRiB46091.
    RefSeqiNP_001681.2. NM_001690.3.
    UniGeneiHs.477155.

    Genome annotation databases

    EnsembliENST00000273398; ENSP00000273398; ENSG00000114573.
    ENST00000538620; ENSP00000439874; ENSG00000114573.
    GeneIDi523.
    KEGGihsa:523.
    UCSCiuc003eao.3. human.

    Polymorphism databases

    DMDMi22096378.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L09235 mRNA. Translation: AAA83249.1 .
    AF113129 mRNA. Translation: AAF14870.1 .
    BT006672 mRNA. Translation: AAP35318.1 .
    AK293804 mRNA. Translation: BAH11601.1 .
    AK314779 mRNA. Translation: BAG37315.1 .
    AC079944 Genomic DNA. No translation available.
    AC108693 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79625.1 .
    CH471052 Genomic DNA. Translation: EAW79626.1 .
    BC013138 mRNA. Translation: AAH13138.1 .
    CCDSi CCDS2976.1.
    PIRi B46091.
    RefSeqi NP_001681.2. NM_001690.3.
    UniGenei Hs.477155.

    3D structure databases

    ProteinModelPortali P38606.
    SMRi P38606. Positions 40-587.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107007. 47 interactions.
    IntActi P38606. 63 interactions.
    MINTi MINT-224589.
    STRINGi 9606.ENSP00000273398.

    Chemistry

    DrugBanki DB00630. Alendronate.
    DB01077. Etidronic acid.
    DB01133. Tiludronate.

    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 P38606.

    Polymorphism databases

    DMDMi 22096378.

    Proteomic databases

    MaxQBi P38606.
    PaxDbi P38606.
    PeptideAtlasi P38606.
    PRIDEi P38606.

    Protocols and materials databases

    DNASUi 523.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273398 ; ENSP00000273398 ; ENSG00000114573 .
    ENST00000538620 ; ENSP00000439874 ; ENSG00000114573 .
    GeneIDi 523.
    KEGGi hsa:523.
    UCSCi uc003eao.3. human.

    Organism-specific databases

    CTDi 523.
    GeneCardsi GC03P113465.
    HGNCi HGNC:851. ATP6V1A.
    HPAi CAB006910.
    HPA035083.
    HPA035084.
    MIMi 607027. gene.
    neXtProti NX_P38606.
    PharmGKBi PA25152.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1155.
    HOGENOMi HOG000161057.
    HOVERGENi HBG053351.
    InParanoidi P38606.
    KOi K02145.
    OMAi ENKITWN.
    OrthoDBi EOG7Q8CMM.
    PhylomeDBi P38606.
    TreeFami TF300811.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03781-MONOMER.
    Reactomei REACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi ATP6V1A. human.
    GeneWikii ATP6V1A.
    GenomeRNAii 523.
    NextBioi 2175.
    PROi P38606.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38606.
    Bgeei P38606.
    CleanExi HS_ATP6V1A.
    Genevestigatori P38606.

    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. "Identification of two subunit A isoforms of the vacuolar H(+)-ATPase in human osteoclastoma."
      van Hille B., Richener H., Evans D.B., Green J.R., Bilbe G.
      J. Biol. Chem. 268:7075-7080(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal adrenal gland and Leukocyte.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hypothalamus.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Cerebellum.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
      Tissue: Kidney.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVATA_HUMAN
    AccessioniPrimary (citable) accession number: P38606
    Secondary accession number(s): B2RBR8
    , B7Z1R5, D3DN75, Q53YD9, Q96DY6, Q9UHY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: August 2, 2002
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 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 3
      Human chromosome 3: 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