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P31412

- VATC_YEAST

UniProt

P31412 - VATC_YEAST

Protein

V-type proton ATPase subunit C

Gene

VMA5

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 131 (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. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31875-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 C
    Short name:
    V-ATPase subunit C
    Alternative name(s):
    V-ATPase 42 kDa subunit
    Vacuolar proton pump subunit C
    Gene namesi
    Name:VMA5
    Synonyms:VAT3, VATC
    Ordered Locus Names:YKL080W
    ORF Names:YKL410
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001563. VMA5.

    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
    Mutagenesisi255 – 2551F → A: Is rapidly degraded and disrupts stable ATPase assembly. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 392391V-type proton ATPase subunit CPRO_0000209358Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP31412.
    PaxDbiP31412.
    PeptideAtlasiP31412.

    Expressioni

    Gene expression databases

    GenevestigatoriP31412.

    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). Interacts directly with VMA4.2 Publications

    Protein-protein interaction databases

    BioGridi34052. 77 interactions.
    DIPiDIP-4701N.
    IntActiP31412. 16 interactions.
    MINTiMINT-496270.
    STRINGi4932.YKL080W.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 179
    Helixi30 – 367
    Helixi38 – 414
    Beta strandi43 – 475
    Helixi58 – 603
    Helixi61 – 8828
    Beta strandi94 – 963
    Helixi107 – 1126
    Turni118 – 1203
    Helixi127 – 16539
    Turni170 – 1723
    Turni176 – 1783
    Helixi181 – 1833
    Beta strandi189 – 19911
    Helixi200 – 2023
    Helixi203 – 2097
    Helixi210 – 2123
    Beta strandi213 – 2175
    Beta strandi223 – 2275
    Beta strandi229 – 23911
    Helixi240 – 2423
    Helixi243 – 25210
    Beta strandi256 – 2583
    Helixi264 – 31956
    Beta strandi325 – 3328
    Helixi337 – 34812
    Helixi349 – 3524
    Beta strandi384 – 3929

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U7LX-ray1.75A1-392[»]
    4DL0X-ray2.90C/I158-277[»]
    4EFAX-ray2.82C158-277[»]
    ProteinModelPortaliP31412.
    SMRiP31412. Positions 5-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31412.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase C subunit family.Curated

    Phylogenomic databases

    eggNOGiCOG5127.
    GeneTreeiENSGT00390000004263.
    HOGENOMiHOG000207528.
    KOiK02148.
    OMAiQRQYAPL.
    OrthoDBiEOG7RRFJ7.

    Family and domain databases

    InterProiIPR004907. ATPase_V1-cplx_csu.
    [Graphical view]
    PANTHERiPTHR10137. PTHR10137. 1 hit.
    PfamiPF03223. V-ATPase_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P31412-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATALYTAND FILISLPQNA QPVTAPGSKT DSWFNETLIG GRAFVSDFKI    50
    PEFKIGSLDT LIVESEELSK VDNQIGASIG KIIEILQGLN ETSTNAYRTL 100
    PINNMPVPEY LENFQWQTRK FKLDKSIKDL ITLISNESSQ LDADVRATYA 150
    NYNSAKTNLA AAERKKTGDL SVRSLHDIVK PEDFVLNSEH LTTVLVAVPK 200
    SLKSDFEKSY ETLSKNVVPA SASVIAEDAE YVLFNVHLFK KNVQEFTTAA 250
    REKKFIPREF NYSEELIDQL KKEHDSAASL EQSLRVQLVR LAKTAYVDVF 300
    INWFHIKALR VYVESVLRYG LPPHFNIKII AVPPKNLSKC KSELIDAFGF 350
    LGGNAFMKDK KGKINKQDTS LHQYASLVDT EYEPFVMYII NL 392
    Length:392
    Mass (Da):44,189
    Last modified:January 23, 2007 - v4
    Checksum:i0CD1B814046C377E
    GO

    Sequence cautioni

    The sequence AAA34440.1 differs from that shown. Reason: Frameshift at position 25.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77143 Genomic DNA. Translation: AAA34440.1. Frameshift.
    X75560 Genomic DNA. Translation: CAA53237.1.
    Z28080 Genomic DNA. Translation: CAA81917.1.
    BK006944 Genomic DNA. Translation: DAA09077.1.
    PIRiS37905.
    RefSeqiNP_012843.1. NM_001179646.1.

    Genome annotation databases

    EnsemblFungiiYKL080W; YKL080W; YKL080W.
    GeneIDi853782.
    KEGGisce:YKL080W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77143 Genomic DNA. Translation: AAA34440.1 . Frameshift.
    X75560 Genomic DNA. Translation: CAA53237.1 .
    Z28080 Genomic DNA. Translation: CAA81917.1 .
    BK006944 Genomic DNA. Translation: DAA09077.1 .
    PIRi S37905.
    RefSeqi NP_012843.1. NM_001179646.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U7L X-ray 1.75 A 1-392 [» ]
    4DL0 X-ray 2.90 C/I 158-277 [» ]
    4EFA X-ray 2.82 C 158-277 [» ]
    ProteinModelPortali P31412.
    SMRi P31412. Positions 5-392.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34052. 77 interactions.
    DIPi DIP-4701N.
    IntActi P31412. 16 interactions.
    MINTi MINT-496270.
    STRINGi 4932.YKL080W.

    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.

    Proteomic databases

    MaxQBi P31412.
    PaxDbi P31412.
    PeptideAtlasi P31412.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL080W ; YKL080W ; YKL080W .
    GeneIDi 853782.
    KEGGi sce:YKL080W.

    Organism-specific databases

    SGDi S000001563. VMA5.

    Phylogenomic databases

    eggNOGi COG5127.
    GeneTreei ENSGT00390000004263.
    HOGENOMi HOG000207528.
    KOi K02148.
    OMAi QRQYAPL.
    OrthoDBi EOG7RRFJ7.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31875-MONOMER.
    Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Miscellaneous databases

    EvolutionaryTracei P31412.
    NextBioi 974900.

    Gene expression databases

    Genevestigatori P31412.

    Family and domain databases

    InterProi IPR004907. ATPase_V1-cplx_csu.
    [Graphical view ]
    PANTHERi PTHR10137. PTHR10137. 1 hit.
    Pfami PF03223. V-ATPase_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and mutational analysis of the gene encoding subunit C of yeast vacuolar H(+)-ATPase."
      Beltran C., Kopecky J., Pan Y.-C.E., Nelson H., Nelson N.
      J. Biol. Chem. 267:774-779(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 99-117, SUBUNIT.
    2. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 99-111; 147-156; 242-251 AND 311-318.
    3. "Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor and vacuolar ATPase subunit C plus a number of unidentified open reading frames."
      James C.M., Gent M.E., Indge K.J., Oliver S.G.
      Yeast 10:247-255(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Bienvenut W.V., Peters C.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-70; 82-98; 126-146; 157-164; 209-215; 242-251; 259-285; 319-328 AND 342-358, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Evidence for major structural changes in subunit C of the vacuolar ATPase due to nucleotide binding."
      Armbruester A., Hohn C., Hermesdorf A., Schumacher K., Boersch M., Grueber G.
      FEBS Lett. 579:1961-1967(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 106-115 AND 358-365, NUCLEOTIDE-BINDING.
    8. "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes."
      Parra K.J., Keenan K.L., Kane P.M.
      J. Biol. Chem. 275:21761-21767(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Mutational analysis of the subunit C (Vma5p) of the yeast vacuolar H+-ATPase."
      Curtis K.K., Francis S.A., Oluwatosin Y., Kane P.M.
      J. Biol. Chem. 277:8979-8988(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-255.
    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 VMA4.
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of yeast V-ATPase subunit C reveals its stator function."
      Drory O., Frolow F., Nelson N.
      EMBO Rep. 5:1148-1152(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

    Entry informationi

    Entry nameiVATC_YEAST
    AccessioniPrimary (citable) accession number: P31412
    Secondary accession number(s): D6VXK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 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 21114 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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3