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P17255

- VATA_YEAST

UniProt

P17255 - VATA_YEAST

Protein

V-type proton ATPase catalytic subunit A

Gene

VMA1

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 184 (01 Oct 2014)
      Sequence version 3 (23 Jan 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. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca2+ homeostasis. This is a catalytic subunit.1 Publication
    PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.1 Publication

    Catalytic activityi

    ATP + H2O + H+(In) = ADP + phosphate + H+(Out).PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi257 – 2648ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. endodeoxyribonuclease activity Source: SGD
    4. protein binding Source: IntAct
    5. proton-transporting ATPase activity, rotational mechanism Source: SGD

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. cellular protein metabolic process Source: SGD
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. intein-mediated protein splicing Source: InterPro
    5. intron homing Source: SGD
    6. vacuolar acidification Source: SGD

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Hydrogen ion transport, Intron homing, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29571-MONOMER.
    ReactomeiREACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Protein family/group databases

    MEROPSiN09.001.
    REBASEi2615. PI-SceI.
    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 catalytic subunit A (EC:3.6.3.14)
    Short name:
    V-ATPase subunit A
    Alternative name(s):
    Vacuolar proton pump subunit A
    Cleaved into the following chain:
    Alternative name(s):
    Sce VMA intein
    VMA1-derived endonuclease
    Short name:
    VDE
    Gene namesi
    Name:VMA1
    Synonyms:CLS8, TFP1
    Ordered Locus Names:YDL185W
    ORF Names:D1286
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002344. VMA1.

    Subcellular locationi

    Endomembrane system 1 Publication. Vacuole membrane 1 Publication
    Note: Membranes of various intracellular acidic compartments.

    GO - Cellular componenti

    1. endomembrane system Source: UniProtKB-SubCell
    2. fungal-type vacuole membrane Source: UniProtKB
    3. vacuolar proton-transporting V-type ATPase, V1 domain Source: SGD

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi284 – 2841C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE. 3 Publications
    Mutagenesisi362 – 3621H → N: Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE. 1 Publication
    Mutagenesisi737 – 7371N → S: Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE. 2 Publications
    Mutagenesisi738 – 7381C → S: Reduces splicing reaction speed. Inhibits splicing; when associated with S-284; N-362 and S-737 in X10SSS VDE. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 283282V-type proton ATPase catalytic subunit A, 1st partPRO_0000002458Add
    BLAST
    Chaini284 – 737454Endonuclease PI-SceIPRO_0000002459Add
    BLAST
    Chaini738 – 1071334V-type proton ATPase catalytic subunit A, 2nd partPRO_0000002460Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei131 – 1311Phosphothreonine1 Publication
    Modified residuei858 – 8581Phosphoserine1 Publication
    Modified residuei928 – 9281Phosphoserine1 Publication

    Post-translational modificationi

    This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.

    Keywords - PTMi

    Acetylation, Autocatalytic cleavage, Phosphoprotein, Protein splicing

    Proteomic databases

    MaxQBiP17255.
    PaxDbiP17255.
    PeptideAtlasiP17255.
    PRIDEiP17255.

    2D gel databases

    UCD-2DPAGEP17255.

    Miscellaneous databases

    PMAP-CutDBP17255.

    Expressioni

    Gene expression databases

    GenevestigatoriP17255.

    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 with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAV1P471042EBI-20245,EBI-25471
    VMA6P323662EBI-20245,EBI-20201

    Protein-protein interaction databases

    BioGridi31859. 371 interactions.
    DIPiDIP-2293N.
    IntActiP17255. 71 interactions.
    MINTiMINT-641889.

    Structurei

    Secondary structure

    1
    1071
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi290 – 2934
    Beta strandi298 – 3003
    Helixi301 – 3033
    Beta strandi309 – 3124
    Beta strandi315 – 3228
    Beta strandi325 – 33511
    Beta strandi343 – 3453
    Beta strandi347 – 3493
    Beta strandi355 – 3595
    Beta strandi363 – 3697
    Beta strandi372 – 3798
    Beta strandi382 – 39615
    Beta strandi398 – 4003
    Beta strandi402 – 41413
    Helixi415 – 4173
    Helixi420 – 43112
    Beta strandi434 – 44310
    Helixi444 – 4496
    Helixi452 – 4576
    Beta strandi459 – 4624
    Turni471 – 4744
    Beta strandi479 – 4813
    Beta strandi485 – 4873
    Helixi488 – 50114
    Beta strandi506 – 5149
    Helixi516 – 52813
    Beta strandi531 – 5333
    Beta strandi534 – 5374
    Beta strandi538 – 5403
    Turni541 – 5433
    Beta strandi544 – 5485
    Turni556 – 5594
    Helixi570 – 5756
    Beta strandi579 – 5846
    Helixi588 – 5914
    Helixi595 – 60915
    Beta strandi610 – 6134
    Beta strandi619 – 6257
    Helixi627 – 63913
    Beta strandi643 – 6508
    Helixi654 – 6563
    Beta strandi657 – 6593
    Beta strandi661 – 6699
    Helixi672 – 6787
    Turni684 – 6863
    Helixi693 – 6953
    Beta strandi700 – 7023
    Beta strandi704 – 71916
    Beta strandi721 – 7233
    Beta strandi727 – 7293
    Beta strandi733 – 7353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DFAX-ray2.00A284-737[»]
    1EF0X-ray2.10A/B283-741[»]
    1GPPX-ray1.35A284-736[»]
    1JVAX-ray2.10A/B274-747[»]
    1LWSX-ray3.50A284-737[»]
    1LWTX-ray3.20A284-737[»]
    1UM2X-ray2.90A/B284-737[»]
    C/D274-747[»]
    1VDEX-ray2.40A/B284-737[»]
    ProteinModelPortaliP17255.
    SMRiP17255. Positions 46-1063.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17255.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 642149DOD-type homing endonucleasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated
    Contains 1 DOD-type homing endonuclease domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1372.
    GeneTreeiENSGT00550000074787.
    HOGENOMiHOG000141780.
    KOiK02145.
    OMAiVHNCGER.
    OrthoDBiEOG7M98QZ.

    Family and domain databases

    Gene3Di1.10.1140.10. 1 hit.
    2.170.16.10. 1 hit.
    3.10.28.10. 1 hit.
    3.40.50.300. 2 hits.
    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.
    IPR028992. Hedgehog/Intein_dom.
    IPR003586. Hint_dom_C.
    IPR003587. Hint_dom_N.
    IPR007868. Hom_end_hint.
    IPR007869. Homing_endonuc_PI-Sce.
    IPR027434. Homing_endonucl.
    IPR006142. INTEIN.
    IPR004042. Intein_endonuc.
    IPR006141. Intein_splice_site.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    PF05204. Hom_end. 2 hits.
    PF05203. Hom_end_hint. 1 hit.
    [Graphical view]
    PRINTSiPR00379. INTEIN.
    SMARTiSM00305. HintC. 1 hit.
    SM00306. HintN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF51294. SSF51294. 2 hits.
    SSF52540. SSF52540. 2 hits.
    SSF55608. SSF55608. 2 hits.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    PS50818. INTEIN_C_TER. 1 hit.
    PS50819. INTEIN_ENDONUCLEASE. 1 hit.
    PS50817. INTEIN_N_TER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17255-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAIENARK EIKRISLEDH AESEYGAIYS VSGPVVIAEN MIGCAMYELV     50
    KVGHDNLVGE VIRIDGDKAT IQVYEETAGL TVGDPVLRTG KPLSVELGPG 100
    LMETIYDGIQ RPLKAIKEES QSIYIPRGID TPALDRTIKW QFTPGKFQVG 150
    DHISGGDIYG SVFENSLISS HKILLPPRSR GTITWIAPAG EYTLDEKILE 200
    VEFDGKKSDF TLYHTWPVRV PRPVTEKLSA DYPLLTGQRV LDALFPCVQG 250
    GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCFAKGTN VLMADGSIEC 300
    IENIEVGNKV MGKDGRPREV IKLPRGRETM YSVVQKSQHR AHKSDSSREV 350
    PELLKFTCNA THELVVRTPR SVRRLSRTIK GVEYFEVITF EMGQKKAPDG 400
    RIVELVKEVS KSYPISEGPE RANELVESYR KASNKAYFEW TIEARDLSLL 450
    GSHVRKATYQ TYAPILYEND HFFDYMQKSK FHLTIEGPKV LAYLLGLWIG 500
    DGLSDRATFS VDSRDTSLME RVTEYAEKLN LCAEYKDRKE PQVAKTVNLY 550
    SKVVRGNGIR NNLNTENPLW DAIVGLGFLK DGVKNIPSFL STDNIGTRET 600
    FLAGLIDSDG YVTDEHGIKA TIKTIHTSVR DGLVSLARSL GLVVSVNAEP 650
    AKVDMNGTKH KISYAIYMSG GDVLLNVLSK CAGSKKFRPA PAAAFARECR 700
    GFYFELQELK EDDYYGITLS DDSDHQFLLA NQVVVHNCGE RGNEMAEVLM 750
    EFPELYTEMS GTKEPIMKRT TLVANTSNMP VAAREASIYT GITLAEYFRD 800
    QGKNVSMIAD SSSRWAEALR EISGRLGEMP ADQGFPAYLG AKLASFYERA 850
    GKAVALGSPD RTGSVSIVAA VSPAGGDFSD PVTTATLGIT QVFWGLDKKL 900
    AQRKHFPSIN TSVSYSKYTN VLNKFYDSNY PEFPVLRDRM KEILSNAEEL 950
    EQVVQLVGKS ALSDSDKITL DVATLIKEDF LQQNGYSTYD AFCPIWKTFD 1000
    MMRAFISYHD EAQKAVANGA NWSKLADSTG DVKHAVSSSK FFEPSRGEKE 1050
    VHGEFEKLLS TMQERFAEST D 1071
    Length:1,071
    Mass (Da):118,637
    Last modified:January 23, 2007 - v3
    Checksum:i2A4C65D2F59426FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti875 – 8751G → D in AAB63978. (PubMed:2905423)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05409 Genomic DNA. Translation: AAA34664.1.
    X83276 Genomic DNA. Translation: CAA58261.1.
    Z74233 Genomic DNA. Translation: CAA98760.1.
    Z74233 Genomic DNA. Translation: CAA98761.1. Sequence problems.
    Z74233 Genomic DNA. Translation: CAA98762.1.
    X58857 Genomic DNA. Translation: CAA41657.1.
    M21609 Genomic DNA. Translation: AAB63978.1.
    BK006938 Genomic DNA. Translation: DAA11677.1.
    PIRiA35746. PXBYVA.
    RefSeqiNP_010096.1. NM_001180245.1.

    Genome annotation databases

    EnsemblFungiiYDL185W; YDL185W; YDL185W.
    GeneIDi851342.
    KEGGisce:YDL185W.

    Cross-referencesi

    Web resourcesi

    Description of Sce VMA in Inbase

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05409 Genomic DNA. Translation: AAA34664.1 .
    X83276 Genomic DNA. Translation: CAA58261.1 .
    Z74233 Genomic DNA. Translation: CAA98760.1 .
    Z74233 Genomic DNA. Translation: CAA98761.1 . Sequence problems.
    Z74233 Genomic DNA. Translation: CAA98762.1 .
    X58857 Genomic DNA. Translation: CAA41657.1 .
    M21609 Genomic DNA. Translation: AAB63978.1 .
    BK006938 Genomic DNA. Translation: DAA11677.1 .
    PIRi A35746. PXBYVA.
    RefSeqi NP_010096.1. NM_001180245.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DFA X-ray 2.00 A 284-737 [» ]
    1EF0 X-ray 2.10 A/B 283-741 [» ]
    1GPP X-ray 1.35 A 284-736 [» ]
    1JVA X-ray 2.10 A/B 274-747 [» ]
    1LWS X-ray 3.50 A 284-737 [» ]
    1LWT X-ray 3.20 A 284-737 [» ]
    1UM2 X-ray 2.90 A/B 284-737 [» ]
    C/D 274-747 [» ]
    1VDE X-ray 2.40 A/B 284-737 [» ]
    ProteinModelPortali P17255.
    SMRi P17255. Positions 46-1063.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31859. 371 interactions.
    DIPi DIP-2293N.
    IntActi P17255. 71 interactions.
    MINTi MINT-641889.

    Protein family/group databases

    MEROPSi N09.001.
    REBASEi 2615. PI-SceI.
    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

    UCD-2DPAGE P17255.

    Proteomic databases

    MaxQBi P17255.
    PaxDbi P17255.
    PeptideAtlasi P17255.
    PRIDEi P17255.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL185W ; YDL185W ; YDL185W .
    GeneIDi 851342.
    KEGGi sce:YDL185W.

    Organism-specific databases

    SGDi S000002344. VMA1.

    Phylogenomic databases

    eggNOGi COG1372.
    GeneTreei ENSGT00550000074787.
    HOGENOMi HOG000141780.
    KOi K02145.
    OMAi VHNCGER.
    OrthoDBi EOG7M98QZ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29571-MONOMER.
    Reactomei REACT_189031. Phagosomal maturation (early endosomal stage).
    REACT_189190. Transferrin endocytosis and recycling.

    Miscellaneous databases

    EvolutionaryTracei P17255.
    NextBioi 968420.
    PMAP-CutDB P17255.
    PROi P17255.

    Gene expression databases

    Genevestigatori P17255.

    Family and domain databases

    Gene3Di 1.10.1140.10. 1 hit.
    2.170.16.10. 1 hit.
    3.10.28.10. 1 hit.
    3.40.50.300. 2 hits.
    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.
    IPR028992. Hedgehog/Intein_dom.
    IPR003586. Hint_dom_C.
    IPR003587. Hint_dom_N.
    IPR007868. Hom_end_hint.
    IPR007869. Homing_endonuc_PI-Sce.
    IPR027434. Homing_endonucl.
    IPR006142. INTEIN.
    IPR004042. Intein_endonuc.
    IPR006141. Intein_splice_site.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    PF05204. Hom_end. 2 hits.
    PF05203. Hom_end_hint. 1 hit.
    [Graphical view ]
    PRINTSi PR00379. INTEIN.
    SMARTi SM00305. HintC. 1 hit.
    SM00306. HintN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF51294. SSF51294. 2 hits.
    SSF52540. SSF52540. 2 hits.
    SSF55608. SSF55608. 2 hits.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    PS50818. INTEIN_C_TER. 1 hit.
    PS50819. INTEIN_ENDONUCLEASE. 1 hit.
    PS50817. INTEIN_N_TER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae."
      Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y.
      J. Biol. Chem. 265:6726-6733(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 181-196; 815-820; 826-836; 862-879; 925-936 AND 1004-1013, SUBUNIT.
      Strain: ATCC 26786 / X2180-1A.
    2. "New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae."
      Verhasselt P., Voet M., Volckaert G.
      Yeast 11:961-966(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(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. "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis."
      Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.
      Mol. Cell. Biol. 11:4876-4884(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
      Strain: ATCC 208353 / W303-1A.
    6. Bienvenut W.V., Peters C.
      Submitted (OCT-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 52-63; 115-136; 173-178; 181-207; 220-239; 264-272; 770-784; 804-814; 826-842; 853-861; 918-937; 940-959; 1004-1014 AND 1058-1065, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides."
      Mizutani R., Nogami S., Kawasaki M., Ohya Y., Anraku Y., Satow Y.
      J. Mol. Biol. 316:919-929(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6, CLEAVAGE OF INITIATOR METHIONINE, MUTAGENESIS OF CYS-284; HIS-362; ASN-737 AND CYS-738, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 274-747.
    8. "A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth."
      Shih C.K., Wagner R., Feinstein S., Kanik-Ennulat C., Neff N.
      Mol. Cell. Biol. 8:3094-3103(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-1071.
    9. "Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase."
      Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H.
      Science 250:651-657(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SPLICING.
    10. "Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing."
      Hirata R., Anraku Y.
      Biochem. Biophys. Res. Commun. 188:40-47(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-284 AND CYS-738.
    11. "Protein splicing of the yeast TFP1 intervening protein sequence: a model for self-excision."
      Cooper A.A., Chen Y.-J., Lindorfer M.A., Stevens T.H.
      EMBO J. 12:2575-2583(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-SPLICING MECHANISM.
    12. "Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae."
      Gimble F.S., Thorner J.
      Nature 357:301-306(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF VDE.
    13. "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.
    14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    16. "Homing in on an endosymbiotic endonuclease."
      Grivell L.A.
      Curr. Biol. 2:450-452(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131; SER-858 AND SER-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity."
      Duan X., Gimble F.S., Quiocho F.A.
      Cell 89:555-564(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PI-SCE I.
    21. "Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking."
      Hu D., Crist M., Duan X., Quiocho F.A., Gimble F.S.
      J. Biol. Chem. 275:2705-2712(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PI-SCE I.
    22. "Structural insights into the protein splicing mechanism of PI-SceI."
      Poland B.W., Xu M.-Q., Quiocho F.A.
      J. Biol. Chem. 275:16408-16413(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 283-741, MUTAGENESIS OF CYS-284 AND ASN-737.
    23. "High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI."
      Werner E., Wende W., Pingoud A., Heinemann U.
      Nucleic Acids Res. 30:3962-3971(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 284-465.

    Entry informationi

    Entry nameiVATA_YEAST
    AccessioniPrimary (citable) accession number: P17255
    Secondary accession number(s): D6VRG7, O74301, Q9Y7W5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 184 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 199895 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3