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P05630

- ATPD_BOVIN

UniProt

P05630 - ATPD_BOVIN

Protein

ATP synthase subunit delta, mitochondrial

Gene

ATP5D

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      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. hydrogen ion transmembrane transporter activity Source: MGI
    2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
    3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP synthesis coupled proton transport Source: InterPro
    2. proton transport Source: MGI

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_212639. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit delta, mitochondrial
    Alternative name(s):
    F-ATPase delta subunit
    Gene namesi
    Name:ATP5D
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 7

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial envelope Source: MGI
    2. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    3. proton-transporting ATP synthase complex Source: MGI
    4. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2222Mitochondrion2 PublicationsAdd
    BLAST
    Chaini23 – 168146ATP synthase subunit delta, mitochondrialPRO_0000002660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
    Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
    Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP05630.
    PRIDEiP05630.

    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 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68.2 Publications

    Protein-protein interaction databases

    DIPiDIP-39022N.
    IntActiP05630. 2 interactions.
    MINTiMINT-5007030.

    Structurei

    Secondary structure

    1
    168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 436
    Beta strandi48 – 503
    Beta strandi56 – 605
    Beta strandi62 – 654
    Beta strandi66 – 705
    Beta strandi76 – 805
    Beta strandi82 – 898
    Beta strandi92 – 998
    Beta strandi101 – 1033
    Beta strandi108 – 1103
    Beta strandi114 – 1196
    Beta strandi122 – 1243
    Helixi129 – 14012
    Beta strandi141 – 1433
    Beta strandi147 – 1504
    Helixi151 – 16414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E79X-ray2.40H23-168[»]
    1H8EX-ray2.00H23-168[»]
    2CK3X-ray1.90H23-168[»]
    2JDIX-ray1.90H23-168[»]
    2V7QX-ray2.10H23-168[»]
    2W6HX-ray5.00H1-168[»]
    2W6IX-ray4.00H1-168[»]
    2W6JX-ray3.84H1-168[»]
    2WSSX-ray3.20H/Q23-168[»]
    2XNDX-ray3.50H37-167[»]
    4ASUX-ray2.60H23-168[»]
    ProteinModelPortaliP05630.
    SMRiP05630. Positions 37-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05630.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase epsilon chain family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0355.
    GeneTreeiENSGT00390000017576.
    HOGENOMiHOG000216023.
    HOVERGENiHBG001856.
    InParanoidiP05630.
    KOiK02134.
    OMAiLPHQAIF.
    OrthoDBiEOG7RNK2T.
    TreeFamiTF313029.

    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.
    IPR020547. ATPase_F1_dsu/esu_C.
    [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]
    SUPFAMiSSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P05630-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPSALLRRP GLGRLVRQVR LYAEAAAAQA PAAGPGQMSF TFASPTQVFF    50
    NSANVRQVDV PTQTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS 100
    SGSVTVNADS SVQLLAEEAV TLDMLDLGAA KANLEKAQSE LLGAADEATR 150
    AEIQIRIEAN EALVKALE 168
    Length:168
    Mass (Da):17,612
    Last modified:August 1, 1990 - v2
    Checksum:i7C47BBAD5A151608
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17019 mRNA. Translation: CAA34885.1.
    BC146208 mRNA. Translation: AAI46209.1.
    PIRiS09202. PWBOD.
    RefSeqiNP_788843.1. NM_176670.2.
    UniGeneiBt.1426.

    Genome annotation databases

    EnsembliENSBTAT00000000721; ENSBTAP00000000721; ENSBTAG00000000550.
    GeneIDi338081.
    KEGGibta:338081.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17019 mRNA. Translation: CAA34885.1 .
    BC146208 mRNA. Translation: AAI46209.1 .
    PIRi S09202. PWBOD.
    RefSeqi NP_788843.1. NM_176670.2.
    UniGenei Bt.1426.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E79 X-ray 2.40 H 23-168 [» ]
    1H8E X-ray 2.00 H 23-168 [» ]
    2CK3 X-ray 1.90 H 23-168 [» ]
    2JDI X-ray 1.90 H 23-168 [» ]
    2V7Q X-ray 2.10 H 23-168 [» ]
    2W6H X-ray 5.00 H 1-168 [» ]
    2W6I X-ray 4.00 H 1-168 [» ]
    2W6J X-ray 3.84 H 1-168 [» ]
    2WSS X-ray 3.20 H/Q 23-168 [» ]
    2XND X-ray 3.50 H 37-167 [» ]
    4ASU X-ray 2.60 H 23-168 [» ]
    ProteinModelPortali P05630.
    SMRi P05630. Positions 37-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-39022N.
    IntActi P05630. 2 interactions.
    MINTi MINT-5007030.

    Chemistry

    ChEMBLi CHEMBL612444.

    Proteomic databases

    PaxDbi P05630.
    PRIDEi P05630.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000000721 ; ENSBTAP00000000721 ; ENSBTAG00000000550 .
    GeneIDi 338081.
    KEGGi bta:338081.

    Organism-specific databases

    CTDi 513.

    Phylogenomic databases

    eggNOGi COG0355.
    GeneTreei ENSGT00390000017576.
    HOGENOMi HOG000216023.
    HOVERGENi HBG001856.
    InParanoidi P05630.
    KOi K02134.
    OMAi LPHQAIF.
    OrthoDBi EOG7RNK2T.
    TreeFami TF313029.

    Enzyme and pathway databases

    Reactomei REACT_212639. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    EvolutionaryTracei P05630.
    NextBioi 20812529.

    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.
    IPR020547. ATPase_F1_dsu/esu_C.
    [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 SSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsi TIGR01216. ATP_synt_epsi. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The delta-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence of its import precursor cloned with the aid of the polymerase chain reaction."
      Runswick M.J., Medd S.M., Walker J.E.
      Biochem. J. 266:421-426(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart muscle.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Uterus.
    3. "Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria."
      Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D., Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.
      J. Mol. Biol. 184:677-701(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-168.
    4. "Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
      Walker J.E., Lutter R., Dupuis A., Runswick M.J.
      Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-31.
      Tissue: Heart.
    5. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
      Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
      FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
    6. "Structure at 2.8-A resolution of F1-ATPase from bovine heart mitochondria."
      Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.
      Nature 370:621-628(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    7. "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria."
      Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.
      Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-168 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5C1 AND ATP5E.

    Entry informationi

    Entry nameiATPD_BOVIN
    AccessioniPrimary (citable) accession number: P05630
    Secondary accession number(s): A6H7D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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

    External Data

    Dasty 3