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P05632

- ATP5E_BOVIN

UniProt

P05632 - ATP5E_BOVIN

Protein

ATP synthase subunit epsilon, mitochondrial

Gene

ATP5E

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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 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 synthesis coupled proton transport Source: InterPro

    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 epsilon, mitochondrial
    Short name:
    ATPase subunit epsilon
    Gene namesi
    Name:ATP5E
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 22

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    2. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: InterPro

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 5150ATP synthase subunit epsilon, mitochondrialPRO_0000071661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211N6-acetyllysine; alternateBy similarity
    Modified residuei21 – 211N6-succinyllysine; alternateBy similarity
    Modified residuei32 – 321N6-acetyllysine; alternateBy similarity
    Modified residuei32 – 321N6-succinyllysine; alternateBy similarity
    Modified residuei37 – 371N6-acetyllysine; alternateBy similarity
    Modified residuei37 – 371N6-succinyllysine; alternateBy similarity
    Modified residuei44 – 441N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    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-46312N.
    IntActiP05632. 1 interaction.
    MINTiMINT-5007161.
    STRINGi9913.ENSBTAP00000051455.

    Structurei

    Secondary structure

    1
    51
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi12 – 2413
    Turni29 – 313
    Helixi33 – 364
    Beta strandi44 – 463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E79X-ray2.40I2-51[»]
    1H8EX-ray2.00I2-51[»]
    2CK3X-ray1.95I2-51[»]
    2JDIX-ray1.90I2-51[»]
    2V7QX-ray2.10I2-51[»]
    2W6HX-ray5.00I1-51[»]
    2W6IX-ray4.00I1-51[»]
    2W6JX-ray3.84I1-51[»]
    2WSSX-ray3.20I/R2-51[»]
    2XNDX-ray3.50I2-48[»]
    4ASUX-ray2.60I2-51[»]
    ProteinModelPortaliP05632.
    SMRiP05632. Positions 2-48.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05632.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic ATPase epsilon family.Curated

    Phylogenomic databases

    eggNOGiNOG318665.
    GeneTreeiENSGT00390000015470.
    HOGENOMiHOG000214506.
    HOVERGENiHBG050611.
    InParanoidiP05632.
    KOiK02135.
    OMAiIRFSAIC.
    OrthoDBiEOG7GQXZP.
    TreeFamiTF300278.

    Family and domain databases

    Gene3Di1.10.1620.20. 1 hit.
    InterProiIPR006721. ATPase_F1-cplx_esu_mt.
    [Graphical view]
    PfamiPF04627. ATP-synt_Eps. 1 hit.
    [Graphical view]
    SUPFAMiSSF48690. SSF48690. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P05632-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK   50
    E 51
    Length:51
    Mass (Da):5,783
    Last modified:January 23, 2007 - v4
    Checksum:iE0D70FA7C9191CAE
    GO

    Sequence cautioni

    The sequence CAA34849.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16978 mRNA. Translation: CAA34849.1. Different initiation.
    BC108146 mRNA. Translation: AAI08147.1.
    PIRiS08239. PWBOE.
    RefSeqiNP_001137213.1. NM_001143741.1.
    XP_001250629.4. XM_001250628.5.
    XP_002697025.2. XM_002696979.2.
    XP_005193391.1. XM_005193334.1.
    XP_005196491.1. XM_005196434.1.
    UniGeneiBt.58312.

    Genome annotation databases

    EnsembliENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954.
    ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208.
    GeneIDi100335469.
    100852024.
    617230.
    782270.
    KEGGibta:100335469.
    bta:100852024.
    bta:617230.
    bta:782270.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16978 mRNA. Translation: CAA34849.1 . Different initiation.
    BC108146 mRNA. Translation: AAI08147.1 .
    PIRi S08239. PWBOE.
    RefSeqi NP_001137213.1. NM_001143741.1.
    XP_001250629.4. XM_001250628.5.
    XP_002697025.2. XM_002696979.2.
    XP_005193391.1. XM_005193334.1.
    XP_005196491.1. XM_005196434.1.
    UniGenei Bt.58312.

    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 I 2-51 [» ]
    1H8E X-ray 2.00 I 2-51 [» ]
    2CK3 X-ray 1.95 I 2-51 [» ]
    2JDI X-ray 1.90 I 2-51 [» ]
    2V7Q X-ray 2.10 I 2-51 [» ]
    2W6H X-ray 5.00 I 1-51 [» ]
    2W6I X-ray 4.00 I 1-51 [» ]
    2W6J X-ray 3.84 I 1-51 [» ]
    2WSS X-ray 3.20 I/R 2-51 [» ]
    2XND X-ray 3.50 I 2-48 [» ]
    4ASU X-ray 2.60 I 2-51 [» ]
    ProteinModelPortali P05632.
    SMRi P05632. Positions 2-48.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46312N.
    IntActi P05632. 1 interaction.
    MINTi MINT-5007161.
    STRINGi 9913.ENSBTAP00000051455.

    Chemistry

    ChEMBLi CHEMBL612444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000035337 ; ENSBTAP00000035213 ; ENSBTAG00000032954 .
    ENSBTAT00000056576 ; ENSBTAP00000051455 ; ENSBTAG00000039208 .
    GeneIDi 100335469.
    100852024.
    617230.
    782270.
    KEGGi bta:100335469.
    bta:100852024.
    bta:617230.
    bta:782270.

    Organism-specific databases

    CTDi 514.

    Phylogenomic databases

    eggNOGi NOG318665.
    GeneTreei ENSGT00390000015470.
    HOGENOMi HOG000214506.
    HOVERGENi HBG050611.
    InParanoidi P05632.
    KOi K02135.
    OMAi IRFSAIC.
    OrthoDBi EOG7GQXZP.
    TreeFami TF300278.

    Enzyme and pathway databases

    Reactomei REACT_212639. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    EvolutionaryTracei P05632.
    NextBioi 20900552.

    Family and domain databases

    Gene3Di 1.10.1620.20. 1 hit.
    InterProi IPR006721. ATPase_F1-cplx_esu_mt.
    [Graphical view ]
    Pfami PF04627. ATP-synt_Eps. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48690. SSF48690. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The epsilon-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence, expression in bovine tissues and evidence of homologous sequences in man and rat."
      Vinas O., Powell S.J., Runswick M.J., Iacobazzi V., Walker J.E.
      Biochem. J. 265:321-326(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    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 2-51.
    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 2-7.
      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 2-50 IN COMPLEX WITH ATPIF1; ATP5A1; ATP5B; ATP5C1 AND ATP5D.

    Entry informationi

    Entry nameiATP5E_BOVIN
    AccessioniPrimary (citable) accession number: P05632
    Secondary accession number(s): Q32PE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 4 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