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Q12165

- ATPD_YEAST

UniProt

Q12165 - ATPD_YEAST

Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 turnover 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 of the central stalk which is part of the complex rotary element. 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 - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29435-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 delta, mitochondrial
    Alternative name(s):
    F-ATPase delta subunit
    Gene namesi
    Name:ATP16
    Ordered Locus Names:YDL004W
    ORF Names:D2935, YD8119.03
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL004w.
    SGDiS000002162. ATP16.

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
    BLAST
    Chaini23 – 160138ATP synthase subunit delta, mitochondrialPRO_0000002671Add
    BLAST

    Proteomic databases

    MaxQBiQ12165.
    PaxDbiQ12165.
    PeptideAtlasiQ12165.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12165.

    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

    BioGridi32050. 10 interactions.
    DIPiDIP-3032N.
    IntActiQ12165. 3 interactions.
    MINTiMINT-2781010.

    Structurei

    Secondary structure

    1
    160
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi44 – 463
    Beta strandi51 – 544
    Beta strandi56 – 594
    Beta strandi61 – 633
    Beta strandi70 – 745
    Beta strandi78 – 836
    Beta strandi86 – 927
    Beta strandi95 – 1006
    Turni101 – 1033
    Beta strandi104 – 1107
    Beta strandi112 – 1143
    Helixi115 – 1173
    Helixi120 – 13314
    Beta strandi136 – 1394
    Helixi140 – 15617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HLDX-ray2.80H/Q/Z23-160[»]
    2WPDX-ray3.43H23-160[»]
    2XOKX-ray3.01H1-160[»]
    3FKSX-ray3.59H/Q/Z23-160[»]
    3OE7X-ray3.19H/Q/Z24-160[»]
    3OEEX-ray2.74H/Q/Z23-160[»]
    3OEHX-ray3.00H/Q/Z23-160[»]
    3OFNX-ray3.20H/Q23-160[»]
    3ZIAX-ray2.50H/R23-160[»]
    3ZRYX-ray6.50H23-160[»]
    4B2Qelectron microscopy37.00H/h29-160[»]
    ProteinModelPortaliQ12165.
    SMRiQ12165. Positions 29-160.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12165.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase epsilon chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0355.
    GeneTreeiENSGT00390000017576.
    HOGENOMiHOG000216023.
    KOiK02134.
    OMAiLPHQAIF.
    OrthoDBiEOG7S7SSS.

    Family and domain databases

    Gene3Di2.60.15.10. 1 hit.
    HAMAPiMF_00530. ATP_synth_epsil_bac.
    InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    [Graphical view]
    PANTHERiPTHR13822. PTHR13822. 1 hit.
    PfamiPF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view]
    ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF51344. SSF51344. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q12165-1 [UniParc]FASTAAdd to Basket

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    MLRSIIGKSA SRSLNFVAKR SYAEAAAASS GLKLQFALPH ETLYSGSEVT    50
    QVNLPAKSGR IGVLANHVPT VEQLLPGVVE VMEGSNSKKF FISGGFATVQ 100
    PDSQLCVTAI EAFPLESFSQ ENIKNLLAEA KKNVSSSDAR EAAEAAIQVE 150
    VLENLQSVLK 160
    Length:160
    Mass (Da):17,020
    Last modified:November 1, 1996 - v1
    Checksum:iAE8D0BA364107977
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21857 Genomic DNA. Translation: CAA79912.1.
    Z48008 Genomic DNA. Translation: CAA88057.1.
    Z48432 Genomic DNA. Translation: CAA88355.1.
    Z74052 Genomic DNA. Translation: CAA98560.1.
    AY558155 Genomic DNA. Translation: AAS56481.1.
    BK006938 Genomic DNA. Translation: DAA11844.1.
    PIRiS45632.
    RefSeqiNP_010280.1. NM_001180063.1.

    Genome annotation databases

    EnsemblFungiiYDL004W; YDL004W; YDL004W.
    GeneIDi851560.
    KEGGisce:YDL004W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21857 Genomic DNA. Translation: CAA79912.1 .
    Z48008 Genomic DNA. Translation: CAA88057.1 .
    Z48432 Genomic DNA. Translation: CAA88355.1 .
    Z74052 Genomic DNA. Translation: CAA98560.1 .
    AY558155 Genomic DNA. Translation: AAS56481.1 .
    BK006938 Genomic DNA. Translation: DAA11844.1 .
    PIRi S45632.
    RefSeqi NP_010280.1. NM_001180063.1.

    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 H/Q/Z 23-160 [» ]
    2WPD X-ray 3.43 H 23-160 [» ]
    2XOK X-ray 3.01 H 1-160 [» ]
    3FKS X-ray 3.59 H/Q/Z 23-160 [» ]
    3OE7 X-ray 3.19 H/Q/Z 24-160 [» ]
    3OEE X-ray 2.74 H/Q/Z 23-160 [» ]
    3OEH X-ray 3.00 H/Q/Z 23-160 [» ]
    3OFN X-ray 3.20 H/Q 23-160 [» ]
    3ZIA X-ray 2.50 H/R 23-160 [» ]
    3ZRY X-ray 6.50 H 23-160 [» ]
    4B2Q electron microscopy 37.00 H/h 29-160 [» ]
    ProteinModelPortali Q12165.
    SMRi Q12165. Positions 29-160.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32050. 10 interactions.
    DIPi DIP-3032N.
    IntActi Q12165. 3 interactions.
    MINTi MINT-2781010.

    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 Q12165.
    PaxDbi Q12165.
    PeptideAtlasi Q12165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL004W ; YDL004W ; YDL004W .
    GeneIDi 851560.
    KEGGi sce:YDL004W.

    Organism-specific databases

    CYGDi YDL004w.
    SGDi S000002162. ATP16.

    Phylogenomic databases

    eggNOGi COG0355.
    GeneTreei ENSGT00390000017576.
    HOGENOMi HOG000216023.
    KOi K02134.
    OMAi LPHQAIF.
    OrthoDBi EOG7S7SSS.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29435-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q12165.
    NextBioi 968992.
    PROi Q12165.

    Gene expression databases

    Genevestigatori Q12165.

    Family and domain databases

    Gene3Di 2.60.15.10. 1 hit.
    HAMAPi MF_00530. ATP_synth_epsil_bac.
    InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    [Graphical view ]
    PANTHERi PTHR13822. PTHR13822. 1 hit.
    Pfami PF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view ]
    ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF51344. SSF51344. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "ATP synthase of yeast mitochondria. Isolation of the F1 delta subunit, sequence and disruption of the structural gene."
      Giraud M.-F., Velours J.
      Eur. J. Biochem. 222:851-859(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-72; 112-121 AND 141-160.
      Strain: D273-10B/A.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    6. "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 nameiATPD_YEAST
    AccessioniPrimary (citable) accession number: Q12165
    Secondary accession number(s): D6VRY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    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

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

    External Data

    Dasty 3