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P07251

- ATPA_YEAST

UniProt

P07251 - ATPA_YEAST

Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP1

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 155 (01 Oct 2014)
      Sequence version 5 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei407 – 4071Required for activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi206 – 2138ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    3. proton-transporting ATP synthase activity, rotational mechanism Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP hydrolysis coupled proton transport Source: InterPro
    3. ATP synthesis coupled proton transport Source: SGD

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28984-MONOMER.
    ReactomeiREACT_189012. Mitochondrial protein import.

    Protein family/group databases

    TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit alpha, mitochondrial
    Gene namesi
    Name:ATP1
    Ordered Locus Names:YBL099W
    ORF Names:YBL0827
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    SGDiS000000195. ATP1.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication
    Note: Peripheral membrane protein.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial intermembrane space Source: Reactome
    3. mitochondrial nucleoid Source: SGD
    4. mitochondrial proton-transporting ATP synthase, catalytic core Source: SGD
    5. mitochondrion Source: SGD
    6. proton-transporting ATP synthase complex, catalytic core F(1) Source: SGD

    Keywords - Cellular componenti

    CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi291 – 2911G → D in ATP1-2; growth-defect. 1 Publication
    Mutagenesisi383 – 3831T → I in ATP1-1; growth-defect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535MitochondrionAdd
    BLAST
    Chaini36 – 545510ATP synthase subunit alpha, mitochondrialPRO_0000002433Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphoserine1 Publication
    Modified residuei178 – 1781Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP07251.
    PaxDbiP07251.
    PeptideAtlasiP07251.
    PRIDEiP07251.

    Expressioni

    Gene expression databases

    GenevestigatoriP07251.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

    Protein-protein interaction databases

    BioGridi32606. 93 interactions.
    DIPiDIP-3025N.
    IntActiP07251. 18 interactions.
    MINTiMINT-2786223.

    Structurei

    Secondary structure

    1
    545
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni62 – 643
    Beta strandi65 – 728
    Beta strandi75 – 806
    Beta strandi88 – 925
    Beta strandi97 – 1037
    Beta strandi108 – 1147
    Helixi116 – 1183
    Beta strandi124 – 13714
    Helixi138 – 1403
    Beta strandi144 – 1463
    Beta strandi153 – 1553
    Beta strandi161 – 1677
    Beta strandi173 – 1764
    Beta strandi181 – 1833
    Helixi188 – 1936
    Beta strandi203 – 2075
    Beta strandi208 – 2114
    Helixi212 – 22110
    Helixi224 – 2274
    Beta strandi228 – 2303
    Turni232 – 2343
    Beta strandi237 – 2448
    Helixi247 – 25812
    Turni259 – 2613
    Helixi263 – 2653
    Beta strandi266 – 2716
    Helixi277 – 29620
    Beta strandi300 – 3067
    Helixi308 – 32114
    Helixi328 – 3303
    Helixi335 – 3439
    Beta strandi347 – 3493
    Turni351 – 3544
    Beta strandi357 – 3659
    Beta strandi367 – 3693
    Helixi374 – 3829
    Beta strandi383 – 3897
    Helixi391 – 3966
    Turni404 – 4063
    Beta strandi408 – 4114
    Helixi412 – 4154
    Helixi418 – 43720
    Helixi438 – 4469
    Helixi449 – 46517
    Helixi475 – 48713
    Turni488 – 4925
    Helixi495 – 4973
    Helixi498 – 51215
    Helixi514 – 52310
    Helixi528 – 54215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLDX-ray2.80A/B/C/J/K/L/S/T/U36-545[»]
    2WPDX-ray3.43A/B/C36-545[»]
    2XOKX-ray3.01A/B/C1-545[»]
    3FKSX-ray3.59A/B/C/J/K/L/S/T/U36-545[»]
    3OE7X-ray3.19A/B/C/J/K/L/S/T/U36-545[»]
    3OEEX-ray2.74A/B/C/J/K/L/S/T/U36-545[»]
    3OEHX-ray3.00A/B/C/J/K/L/S/T/U36-545[»]
    3OFNX-ray3.20A/B/C/J/K/L/S/T/U36-545[»]
    3ZIAX-ray2.50A/B/C/K/L/M36-545[»]
    3ZRYX-ray6.50A/B/C36-545[»]
    4B2Qelectron microscopy37.00A/C/a/c61-545[»]
    B/b60-545[»]
    ProteinModelPortaliP07251.
    SMRiP07251. Positions 61-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07251.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0056.
    GeneTreeiENSGT00550000074846.
    HOGENOMiHOG000130111.
    KOiK02132.
    OMAiLHASNTC.
    OrthoDBiEOG7FNCHF.

    Family and domain databases

    Gene3Di2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01346. ATP_synth_alpha_bact.
    InterProiIPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    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.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00962. atpA. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07251-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLARTAAIRS LSRTLINSTK AARPAAAALA STRRLASTKA QPTEVSSILE    50
    ERIKGVSDEA NLNETGRVLA VGDGIARVFG LNNIQAEELV EFSSGVKGMA 100
    LNLEPGQVGI VLFGSDRLVK EGELVKRTGN IVDVPVGPGL LGRVVDALGN 150
    PIDGKGPIDA AGRSRAQVKA PGILPRRSVH EPVQTGLKAV DALVPIGRGQ 200
    RELIIGDRQT GKTAVALDTI LNQKRWNNGS DESKKLYCVY VAVGQKRSTV 250
    AQLVQTLEQH DAMKYSIIVA ATASEAAPLQ YLAPFTAASI GEWFRDNGKH 300
    ALIVYDDLSK QAVAYRQLSL LLRRPPGREA YPGDVFYLHS RLLERAAKLS 350
    EKEGSGSLTA LPVIETQGGD VSAYIPTNVI SITDGQIFLE AELFYKGIRP 400
    AINVGLSVSR VGSAAQVKAL KQVAGSLKLF LAQYREVAAF AQFGSDLDAS 450
    TKQTLVRGER LTQLLKQNQY SPLATEEQVP LIYAGVNGHL DGIELSRIGE 500
    FESSFLSYLK SNHNELLTEI REKGELSKEL LASLKSATES FVATF 545
    Length:545
    Mass (Da):58,608
    Last modified:July 27, 2011 - v5
    Checksum:iE8041D289B924696
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti311 – 3133QAV → ASL in AAA66888. (PubMed:2876995)Curated
    Sequence conflicti321 – 3211L → M in AAA66888. (PubMed:2876995)Curated
    Sequence conflicti340 – 3401S → P in CAA56001. (PubMed:7502586)Curated
    Sequence conflicti340 – 3401S → P in CAA84924. (PubMed:7813418)Curated
    Sequence conflicti385 – 3851G → A in AAA66888. (PubMed:2876995)Curated
    Sequence conflicti459 – 4591E → Q in AAA66888. (PubMed:2876995)Curated
    Sequence conflicti479 – 4835VPLIY → SMII in AAA66888. (PubMed:2876995)Curated
    Sequence conflicti490 – 4934LDGI → SGWY in AAA66888. (PubMed:2876995)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02603 Genomic DNA. Translation: AAA66888.1.
    D88458 Genomic DNA. Translation: BAA13613.1.
    D37948 Genomic DNA. Translation: BAA22508.1.
    X79489 Genomic DNA. Translation: CAA56001.1.
    Z35861 Genomic DNA. Translation: CAA84924.1.
    AY692969 Genomic DNA. Translation: AAT92988.1.
    BK006936 Genomic DNA. Translation: DAA07026.2.
    PIRiS45401. PWBYA.
    RefSeqiNP_009453.2. NM_001178339.2.

    Genome annotation databases

    EnsemblFungiiYBL099W; YBL099W; YBL099W.
    GeneIDi852177.
    KEGGisce:YBL099W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02603 Genomic DNA. Translation: AAA66888.1 .
    D88458 Genomic DNA. Translation: BAA13613.1 .
    D37948 Genomic DNA. Translation: BAA22508.1 .
    X79489 Genomic DNA. Translation: CAA56001.1 .
    Z35861 Genomic DNA. Translation: CAA84924.1 .
    AY692969 Genomic DNA. Translation: AAT92988.1 .
    BK006936 Genomic DNA. Translation: DAA07026.2 .
    PIRi S45401. PWBYA.
    RefSeqi NP_009453.2. NM_001178339.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HLD X-ray 2.80 A/B/C/J/K/L/S/T/U 36-545 [» ]
    2WPD X-ray 3.43 A/B/C 36-545 [» ]
    2XOK X-ray 3.01 A/B/C 1-545 [» ]
    3FKS X-ray 3.59 A/B/C/J/K/L/S/T/U 36-545 [» ]
    3OE7 X-ray 3.19 A/B/C/J/K/L/S/T/U 36-545 [» ]
    3OEE X-ray 2.74 A/B/C/J/K/L/S/T/U 36-545 [» ]
    3OEH X-ray 3.00 A/B/C/J/K/L/S/T/U 36-545 [» ]
    3OFN X-ray 3.20 A/B/C/J/K/L/S/T/U 36-545 [» ]
    3ZIA X-ray 2.50 A/B/C/K/L/M 36-545 [» ]
    3ZRY X-ray 6.50 A/B/C 36-545 [» ]
    4B2Q electron microscopy 37.00 A/C/a/c 61-545 [» ]
    B/b 60-545 [» ]
    ProteinModelPortali P07251.
    SMRi P07251. Positions 61-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32606. 93 interactions.
    DIPi DIP-3025N.
    IntActi P07251. 18 interactions.
    MINTi MINT-2786223.

    Protein family/group databases

    TCDBi 3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Proteomic databases

    MaxQBi P07251.
    PaxDbi P07251.
    PeptideAtlasi P07251.
    PRIDEi P07251.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL099W ; YBL099W ; YBL099W .
    GeneIDi 852177.
    KEGGi sce:YBL099W.

    Organism-specific databases

    SGDi S000000195. ATP1.

    Phylogenomic databases

    eggNOGi COG0056.
    GeneTreei ENSGT00550000074846.
    HOGENOMi HOG000130111.
    KOi K02132.
    OMAi LHASNTC.
    OrthoDBi EOG7FNCHF.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28984-MONOMER.
    Reactomei REACT_189012. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P07251.
    NextBioi 970637.
    PROi P07251.

    Gene expression databases

    Genevestigatori P07251.

    Family and domain databases

    Gene3Di 2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01346. ATP_synth_alpha_bact.
    InterProi IPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    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.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00962. atpA. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nuclear genes encoding the yeast mitochondrial ATPase complex. Analysis of ATP1 coding the F1-ATPase alpha-subunit and its assembly."
      Takeda M., Chen W.-J., Saltzgaber J., Douglas M.G.
      J. Biol. Chem. 261:15126-15133(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "ASC1/RAS2 suppresses the growth-defect on glycerol caused by the atp1-2 mutation in the yeast Saccharomyces cerevisiae."
      Mabuchi T., Ichimura Y., Takeda M., Douglas M.G.
      J. Biol. Chem. 275:10492-10497(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-291 AND THR-383.
      Strain: ATCC 64665 / S288c / DC5.
    3. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
      Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
      Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 340.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
      Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
      Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    10. "Molecular architecture of the rotary motor in ATP synthase."
      Stock D., Leslie A.G., Walker J.E.
      Science 286:1700-1705(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiATPA_YEAST
    AccessioniPrimary (citable) accession number: P07251
    Secondary accession number(s): D6VPQ6, Q92449
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 155 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 41500 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3