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P05632

- ATP5E_BOVIN

UniProt

P05632 - ATP5E_BOVIN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK

E
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

« Hide 'large scale' publications
  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