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Q9D593

- VATE2_MOUSE

UniProt

Q9D593 - VATE2_MOUSE

Protein

V-type proton ATPase subunit E 2

Gene

Atp6v1e2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. This isoform is essential for energy coupling involved in acidification of acrosome.1 Publication

    GO - Molecular functioni

    1. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: MGI
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: MGI

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    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 subunit E 2
    Short name:
    V-ATPase subunit E 2
    Alternative name(s):
    Vacuolar proton pump subunit E 2
    Gene namesi
    Name:Atp6v1e2
    Synonyms:Atp6e1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1922165. Atp6v1e2.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: MGI
    2. proton-transporting two-sector ATPase complex, catalytic domain Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 226226V-type proton ATPase subunit E 2PRO_0000282345Add
    BLAST

    Proteomic databases

    PaxDbiQ9D593.
    PRIDEiQ9D593.

    PTM databases

    PhosphoSiteiQ9D593.

    Expressioni

    Tissue specificityi

    Testis specific.1 Publication

    Gene expression databases

    BgeeiQ9D593.
    CleanExiMM_ATP6V1E2.
    GenevestigatoriQ9D593.

    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

    BioGridi217076. 1 interaction.
    IntActiQ9D593. 3 interactions.
    MINTiMINT-4127094.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D593.
    SMRiQ9D593. Positions 2-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase E subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG1390.
    GeneTreeiENSGT00390000002730.
    HOGENOMiHOG000202506.
    HOVERGENiHBG002309.
    InParanoidiQ9D593.
    KOiK02150.
    OMAiDVGKQIQ.
    OrthoDBiEOG70PC01.
    PhylomeDBiQ9D593.
    TreeFamiTF313479.

    Family and domain databases

    HAMAPiMF_00311. ATP_synth_E_arch.
    InterProiIPR002842. ATPase_V1/A1-cplx_esu.
    [Graphical view]
    PfamiPF01991. vATP-synt_E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9D593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALTDIDVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR    50
    LKIMDYFEKK EKQIEQQKKI QLSTMRNQAR ITVLRARDNL ILELLKDAKM 100
    RLSRIVSDEE IYQDLLDKLV LQALLRLLEP VMIVRCRPQD LHLVESAVLR 150
    AIPQYMRLCQ KHLEVQVDQT EHLPSNAAGG VEVYSSDQKI KVSNTLESRL 200
    NLAAMQKMPE IRGILFGDNT SRKFFT 226
    Length:226
    Mass (Da):26,307
    Last modified:June 1, 2001 - v1
    Checksum:iAE5F501F02B8F98F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551D → G in AAH61059. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB074757 mRNA. Translation: BAB92083.1.
    AK015654 mRNA. Translation: BAB29919.1.
    BC049547 mRNA. Translation: AAH49547.2.
    BC061059 mRNA. Translation: AAH61059.1.
    CCDSiCCDS29009.1.
    RefSeqiNP_083397.3. NM_029121.3.
    UniGeneiMm.159369.

    Genome annotation databases

    EnsembliENSMUST00000065758; ENSMUSP00000065285; ENSMUSG00000053375.
    GeneIDi74915.
    KEGGimmu:74915.
    UCSCiuc008dul.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB074757 mRNA. Translation: BAB92083.1 .
    AK015654 mRNA. Translation: BAB29919.1 .
    BC049547 mRNA. Translation: AAH49547.2 .
    BC061059 mRNA. Translation: AAH61059.1 .
    CCDSi CCDS29009.1.
    RefSeqi NP_083397.3. NM_029121.3.
    UniGenei Mm.159369.

    3D structure databases

    ProteinModelPortali Q9D593.
    SMRi Q9D593. Positions 2-217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 217076. 1 interaction.
    IntActi Q9D593. 3 interactions.
    MINTi MINT-4127094.

    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 Q9D593.

    Proteomic databases

    PaxDbi Q9D593.
    PRIDEi Q9D593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065758 ; ENSMUSP00000065285 ; ENSMUSG00000053375 .
    GeneIDi 74915.
    KEGGi mmu:74915.
    UCSCi uc008dul.1. mouse.

    Organism-specific databases

    CTDi 90423.
    MGIi MGI:1922165. Atp6v1e2.

    Phylogenomic databases

    eggNOGi COG1390.
    GeneTreei ENSGT00390000002730.
    HOGENOMi HOG000202506.
    HOVERGENi HBG002309.
    InParanoidi Q9D593.
    KOi K02150.
    OMAi DVGKQIQ.
    OrthoDBi EOG70PC01.
    PhylomeDBi Q9D593.
    TreeFami TF313479.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 341799.
    PROi Q9D593.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D593.
    CleanExi MM_ATP6V1E2.
    Genevestigatori Q9D593.

    Family and domain databases

    HAMAPi MF_00311. ATP_synth_E_arch.
    InterProi IPR002842. ATPase_V1/A1-cplx_esu.
    [Graphical view ]
    Pfami PF01991. vATP-synt_E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification."
      Sun-Wada G.H., Imai-Senga Y., Yamamoto A., Murata Y., Hirata T., Wada Y., Futai M.
      J. Biol. Chem. 277:18098-18105(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    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].
      Strain: C57BL/6J.
      Tissue: Testis.
    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: Testis.

    Entry informationi

    Entry nameiVATE2_MOUSE
    AccessioniPrimary (citable) accession number: Q9D593
    Secondary accession number(s): Q6P8U8, Q810S5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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