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P38077

- ATPG_YEAST

UniProt

P38077 - ATPG_YEAST

Protein

ATP synthase subunit gamma, mitochondrial

Gene

ATP3

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 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      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. Part of the complex F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    GO - Molecular functioni

    1. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    GO - Biological processi

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

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29013-MONOMER.

    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 gamma, mitochondrial
    Alternative name(s):
    F-ATPase gamma subunit
    Gene namesi
    Name:ATP3
    Synonyms:ATP3a, ATP3b
    Ordered Locus Names:YBR039W
    ORF Names:YBR0408
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR039w.
    SGDiS000000243. ATP3.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial proton-transporting ATP synthase, central stalk Source: SGD
    2. 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
    Mutagenesisi273 – 2731A → V: Lower activity. 1 Publication
    Mutagenesisi297 – 2971T → A in ATP3-5; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. 1 Publication
    Mutagenesisi303 – 3031I → T in ATP3-1; dominant suppressor of the slow-growth phenotype of yme1 strains lacking mitochondrial DNA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
    BLAST
    Chaini34 – 311278ATP synthase subunit gamma, mitochondrialPRO_0000002691Add
    BLAST

    Proteomic databases

    MaxQBiP38077.
    PaxDbiP38077.
    PeptideAtlasiP38077.

    Expressioni

    Gene expression databases

    GenevestigatoriP38077.

    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

    BioGridi32740. 48 interactions.
    DIPiDIP-3035N.
    IntActiP38077. 23 interactions.
    MINTiMINT-693544.

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 7944
    Helixi83 – 875
    Beta strandi105 – 1106
    Helixi120 – 13415
    Beta strandi139 – 1446
    Helixi145 – 15410
    Helixi156 – 1583
    Beta strandi159 – 1657
    Beta strandi167 – 1693
    Helixi173 – 18614
    Helixi189 – 1913
    Beta strandi193 – 2019
    Beta strandi203 – 2064
    Beta strandi209 – 2157
    Helixi218 – 2225
    Helixi227 – 2293
    Beta strandi234 – 2363
    Helixi239 – 30870

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLDX-ray2.80G/P/Y34-311[»]
    2WPDX-ray3.43G34-311[»]
    2XOKX-ray3.01G1-311[»]
    3FKSX-ray3.59G/P/Y34-311[»]
    3OE7X-ray3.19G/P/Y34-311[»]
    3OEEX-ray2.74G/P/Y34-311[»]
    3OEHX-ray3.00G/P/Y34-311[»]
    3OFNX-ray3.20G/P/Y34-311[»]
    3ZIAX-ray2.50G/Q34-311[»]
    3ZRYX-ray6.50G34-311[»]
    4B2Qelectron microscopy37.00G/g34-311[»]
    ProteinModelPortaliP38077.
    SMRiP38077. Positions 34-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38077.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase gamma chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0224.
    GeneTreeiENSGT00390000006837.
    HOGENOMiHOG000215911.
    KOiK02136.
    OMAiMATLKDX.
    OrthoDBiEOG76QFTN.

    Family and domain databases

    InterProiIPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view]
    PANTHERiPTHR11693. PTHR11693. 1 hit.
    PfamiPF00231. ATP-synt. 1 hit.
    [Graphical view]
    PRINTSiPR00126. ATPASEGAMMA.
    SUPFAMiSSF52943. SSF52943. 1 hit.
    TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P38077-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRIVSNNA TRSVMCHQAQ VGILYKTNPV RTYATLKEVE MRLKSIKNIE    50
    KITKTMKIVA STRLSKAEKA KISAKKMDEA EQLFYKNAET KNLDVEATET 100
    GAPKELIVAI TSDKGLCGSI HSQLAKAVRR HLNDQPNADI VTIGDKIKMQ 150
    LLRTHPNNIK LSINGIGKDA PTFQESALIA DKLLSVMKAG TYPKISIFYN 200
    DPVSSLSFEP SEKPIFNAKT IEQSPSFGKF EIDTDANVPR DLFEYTLANQ 250
    MLTAMAQGYA AEISARRNAM DNASKNAGDM INRYSILYNR TRQAVITNEL 300
    VDIITGASSL G 311
    Length:311
    Mass (Da):34,351
    Last modified:October 1, 1994 - v1
    Checksum:iADC71F3C1E0CDF91
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti207 – 2071S → I in strain: D273-10B/A1.
    Natural varianti308 – 3081S → F in allele ATP3a.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09305 Genomic DNA. Translation: AAA62605.1.
    U08318 Unassigned DNA. Translation: AAA88816.1.
    AB036928 Genomic DNA. Translation: BAC97839.1.
    AB036929 Genomic DNA. Translation: BAC97840.1.
    Z35908 Genomic DNA. Translation: CAA84981.1.
    AY557865 Genomic DNA. Translation: AAS56191.1.
    BK006936 Genomic DNA. Translation: DAA07159.1.
    PIRiS55891.
    RefSeqiNP_009595.1. NM_001178387.1.

    Genome annotation databases

    EnsemblFungiiYBR039W; YBR039W; YBR039W.
    GeneIDi852327.
    KEGGisce:YBR039W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09305 Genomic DNA. Translation: AAA62605.1 .
    U08318 Unassigned DNA. Translation: AAA88816.1 .
    AB036928 Genomic DNA. Translation: BAC97839.1 .
    AB036929 Genomic DNA. Translation: BAC97840.1 .
    Z35908 Genomic DNA. Translation: CAA84981.1 .
    AY557865 Genomic DNA. Translation: AAS56191.1 .
    BK006936 Genomic DNA. Translation: DAA07159.1 .
    PIRi S55891.
    RefSeqi NP_009595.1. NM_001178387.1.

    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 G/P/Y 34-311 [» ]
    2WPD X-ray 3.43 G 34-311 [» ]
    2XOK X-ray 3.01 G 1-311 [» ]
    3FKS X-ray 3.59 G/P/Y 34-311 [» ]
    3OE7 X-ray 3.19 G/P/Y 34-311 [» ]
    3OEE X-ray 2.74 G/P/Y 34-311 [» ]
    3OEH X-ray 3.00 G/P/Y 34-311 [» ]
    3OFN X-ray 3.20 G/P/Y 34-311 [» ]
    3ZIA X-ray 2.50 G/Q 34-311 [» ]
    3ZRY X-ray 6.50 G 34-311 [» ]
    4B2Q electron microscopy 37.00 G/g 34-311 [» ]
    ProteinModelPortali P38077.
    SMRi P38077. Positions 34-311.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32740. 48 interactions.
    DIPi DIP-3035N.
    IntActi P38077. 23 interactions.
    MINTi MINT-693544.

    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 P38077.
    PaxDbi P38077.
    PeptideAtlasi P38077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR039W ; YBR039W ; YBR039W .
    GeneIDi 852327.
    KEGGi sce:YBR039W.

    Organism-specific databases

    CYGDi YBR039w.
    SGDi S000000243. ATP3.

    Phylogenomic databases

    eggNOGi COG0224.
    GeneTreei ENSGT00390000006837.
    HOGENOMi HOG000215911.
    KOi K02136.
    OMAi MATLKDX.
    OrthoDBi EOG76QFTN.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29013-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38077.
    NextBioi 971035.
    PROi P38077.

    Gene expression databases

    Genevestigatori P38077.

    Family and domain databases

    InterProi IPR000131. ATPase_F1-cplx_gsu.
    IPR023632. ATPase_F1_gsu_CS.
    IPR023633. ATPase_F1_gsu_dom.
    [Graphical view ]
    PANTHERi PTHR11693. PTHR11693. 1 hit.
    Pfami PF00231. ATP-synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00126. ATPASEGAMMA.
    SUPFAMi SSF52943. SSF52943. 1 hit.
    TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
    PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the yeast ATP3 gene coding for the gamma-subunit of F1 and characterization of atp3 mutants."
      Paul M.-F., Ackermann S., Yue J., Arselin G., Velours J., Tzagoloff A.
      J. Biol. Chem. 269:26158-26164(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-61; 77-86; 195-207; 220-240 AND 284-290, MUTAGENESIS OF ALA-273.
      Strain: ATCC 201238 / W303-1B and D273-10B/A1.
    2. "Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow-growth phenotype of yme1 yeast lacking mitochondrial DNA."
      Weber E.R., Rooks R.S., Shafer K.S., Chase J.W., Thorsness P.E.
      Genetics 140:435-442(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF THR-297 AND ILE-303.
    3. "Studies on the ATP3 gene of Saccharomyces cerevisiae: presence of two closely linked copies, ATP3a and ATP3b, on the right arm of chromosome II."
      Ohnishi K., Ishibashi S., Kunihiro M., Satoh T., Matsubara K., Oku S., Ono B., Mabuchi T., Takeda M.
      Yeast 20:943-954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ATP3A AND ATP3B).
      Strain: ATCC 64665 / S288c / DC5.
    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.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "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.
    9. "Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase."
      Kabaleeswaran V., Puri N., Walker J.E., Leslie A.G.W., Mueller D.M.
      EMBO J. 25:5433-5442(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-311.
    10. "Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides."
      Kabaleeswaran V., Shen H., Symersky J., Walker J.E., Leslie A.G.W., Mueller D.M.
      J. Biol. Chem. 284:10546-10551(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 34-311.

    Entry informationi

    Entry nameiATPG_YEAST
    AccessioniPrimary (citable) accession number: P38077
    Secondary accession number(s): D6VQ39, Q54AF5, Q76MT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 28100 molecules/cell in log phase SD medium.1 Publication
    PubMed:12898710 reports two tandemly repeated copies of ATP3 (ATP3a and ATP3b) on the right arm of chromosome II in several laboratory strains, including S288c. This has not been confirmed by the yeast genome sequencing project.

    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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3