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P22203

- VATE_YEAST

UniProt

P22203 - VATE_YEAST

Protein

V-type proton ATPase subunit E

Gene

VMA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      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.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. proton-transporting ATPase activity, rotational mechanism Source: SGD

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. vacuolar acidification Source: SGD

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33808-MONOMER.
    ReactomeiREACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.3. 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
    Short name:
    V-ATPase subunit E
    Alternative name(s):
    V-ATPase 27 kDa subunit
    Vacuolar proton pump subunit E
    Gene namesi
    Name:VMA4
    Synonyms:VAT5
    Ordered Locus Names:YOR332W
    ORF Names:O6241
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    SGDiS000005859. VMA4.

    Subcellular locationi

    Vacuole membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. fungal-type vacuole membrane Source: SGD
    2. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21S → A: Reduces ATPase activity by 11%. 1 Publication
    Mutagenesisi6 – 61T → A: Reduces ATPase activity by 73%. 1 Publication
    Mutagenesisi9 – 91T → A: Increases ATPase activity 1.4-fold. 1 Publication
    Mutagenesisi78 – 781S → A: Reduces ATPase activity by 88%. Prevents assembly of V1 subunits at the membrane. 1 Publication
    Mutagenesisi145 – 1451D → G in VMA4-1; is rapidly degraded at 37 degrees Celsius. 1 Publication
    Mutagenesisi160 – 1601Y → A: Reduces ATPase activity by 22%. 1 Publication
    Mutagenesisi202 – 2021T → A: Increases ATPase activity 2.1-fold by increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-233. 1 Publication
    Mutagenesisi230 – 2301K → A: Increases ATPase activity 1.3-fold. 1 Publication
    Mutagenesisi233 – 2331D → A: Reduces ATPase activity by 74%. Reduces ATPase activity by 90% and produces structurally aberrant V-ATPase complexes; when associated with A-202. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 233232V-type proton ATPase subunit EPRO_0000117310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP22203.
    PaxDbiP22203.
    PeptideAtlasiP22203.

    2D gel databases

    SWISS-2DPAGEP22203.

    Expressioni

    Gene expression databases

    GenevestigatoriP22203.

    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'', d and e). VMA4 forms a homodimer within this complex and interacts directly with VMA5 and VMA10. Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAV1P471043EBI-20268,EBI-25471

    Protein-protein interaction databases

    BioGridi34716. 60 interactions.
    DIPiDIP-4595N.
    IntActiP22203. 17 interactions.
    MINTiMINT-564623.
    STRINGi4932.YOR332W.

    Structurei

    Secondary structure

    1
    233
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 111102
    Helixi114 – 13219
    Beta strandi135 – 1417
    Turni143 – 1453
    Helixi146 – 1494
    Helixi153 – 16311
    Turni164 – 1663
    Beta strandi171 – 1744
    Turni181 – 1833
    Beta strandi185 – 1917
    Beta strandi198 – 2025
    Helixi203 – 22220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KZ9NMR-A1-69[»]
    4DL0X-ray2.90E/J1-233[»]
    4EFAX-ray2.82E1-233[»]
    ProteinModelPortaliP22203.
    SMRiP22203. Positions 2-226.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 2013Interaction with VMA5Add
    BLAST
    Regioni19 – 3820Interaction with VMA10Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili15 – 4531Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the V-ATPase E subunit family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1390.
    GeneTreeiENSGT00390000002730.
    HOGENOMiHOG000202506.
    KOiK02150.
    OMAiAIPEYMT.
    OrthoDBiEOG7380GZ.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22203-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSAITALTP NQVNDELNKM QAFIRKEAEE KAKEIQLKAD QEYEIEKTNI    50
    VRNETNNIDG NFKSKLKKAM LSQQITKSTI ANKMRLKVLS AREQSLDGIF 100
    EETKEKLSGI ANNRDEYKPI LQSLIVEALL KLLEPKAIVK ALERDVDLIE 150
    SMKDDIMREY GEKAQRAPLE EIVISNDYLN KDLVSGGVVV SNASDKIEIN 200
    NTLEERLKLL SEEALPAIRL ELYGPSKTRK FFD 233
    Length:233
    Mass (Da):26,471
    Last modified:January 23, 2007 - v4
    Checksum:i7AC5169FF7E5A39C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 982DG → ER in AAA35209. (PubMed:2145285)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60663 Genomic DNA. Translation: AAA35209.1.
    Z49821 Genomic DNA. Translation: CAA89978.1.
    Z75239 Genomic DNA. Translation: CAA99654.1.
    BK006948 Genomic DNA. Translation: DAA11094.1.
    PIRiS62063.
    RefSeqiNP_014977.3. NM_001183752.3.

    Genome annotation databases

    EnsemblFungiiYOR332W; YOR332W; YOR332W.
    GeneIDi854509.
    KEGGisce:YOR332W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60663 Genomic DNA. Translation: AAA35209.1 .
    Z49821 Genomic DNA. Translation: CAA89978.1 .
    Z75239 Genomic DNA. Translation: CAA99654.1 .
    BK006948 Genomic DNA. Translation: DAA11094.1 .
    PIRi S62063.
    RefSeqi NP_014977.3. NM_001183752.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KZ9 NMR - A 1-69 [» ]
    4DL0 X-ray 2.90 E/J 1-233 [» ]
    4EFA X-ray 2.82 E 1-233 [» ]
    ProteinModelPortali P22203.
    SMRi P22203. Positions 2-226.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34716. 60 interactions.
    DIPi DIP-4595N.
    IntActi P22203. 17 interactions.
    MINTi MINT-564623.
    STRINGi 4932.YOR332W.

    Protein family/group databases

    TCDBi 3.A.2.2.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    2D gel databases

    SWISS-2DPAGE P22203.

    Proteomic databases

    MaxQBi P22203.
    PaxDbi P22203.
    PeptideAtlasi P22203.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR332W ; YOR332W ; YOR332W .
    GeneIDi 854509.
    KEGGi sce:YOR332W.

    Organism-specific databases

    SGDi S000005859. VMA4.

    Phylogenomic databases

    eggNOGi COG1390.
    GeneTreei ENSGT00390000002730.
    HOGENOMi HOG000202506.
    KOi K02150.
    OMAi AIPEYMT.
    OrthoDBi EOG7380GZ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33808-MONOMER.
    Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Miscellaneous databases

    NextBioi 976864.

    Gene expression databases

    Genevestigatori P22203.

    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. "The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in Saccharomyces cerevisiae."
      Foury F.
      J. Biol. Chem. 265:18554-18560(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    2. "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces cerevisiae chromosome XV: similarity to part of chromosome I."
      Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.
      Yeast 12:999-1004(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Bienvenut W.V., Peters C.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-26; 39-63; 69-77; 86-131; 145-158; 167-181 AND 197-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar H(+)-ATPase."
      Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.
      J. Biol. Chem. 268:221-227(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 209-219, SUBUNIT.
    7. "Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase."
      Tomashek J.J., Sonnenburg J.L., Artimovich J.M., Klionsky D.J.
      J. Biol. Chem. 271:10397-10404(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    8. "Characterization of a temperature-sensitive yeast vacuolar ATPase mutant with defects in actin distribution and bud morphology."
      Zhang J.W., Parra K.J., Liu J., Kane P.M.
      J. Biol. Chem. 273:18470-18480(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-145.
    9. "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly."
      Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.
      Nat. Cell Biol. 3:384-391(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAV1 AND RAV2.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H(+)-ATPase."
      Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.
      Biochemistry 44:3933-3941(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VMA5 AND VMA10.
    13. Cited for: MUTAGENESIS OF SER-2; THR-6; THR-9; SER-78; TYR-160; THR-202; LYS-230 AND ASP-233.
    14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVATE_YEAST
    AccessioniPrimary (citable) accession number: P22203
    Secondary accession number(s): D6W328
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 16134 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3