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Protein

ATP synthase subunit epsilon, mitochondrial

Gene

ATP5E

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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 catabolic process Source: GO_Central
  2. 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 13, UP000009136: 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 – 96Combined sources
Helixi12 – 2413Combined sources
Turni29 – 313Combined sources
Helixi33 – 364Combined sources
Beta strandi44 – 463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiANAMKTS.
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL612444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi514.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_212639. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP05632.
NextBioi20900552.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.