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P05632 (ATP5E_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit epsilon, mitochondrial

Short name=ATPase subunit epsilon
Gene names
Name:ATP5E
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length51 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.5

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the eukaryotic ATPase epsilon family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 5150ATP synthase subunit epsilon, mitochondrial
PRO_0000071661

Amino acid modifications

Modified residue211N6-acetyllysine; alternate By similarity
Modified residue211N6-succinyllysine; alternate By similarity
Modified residue321N6-acetyllysine; alternate By similarity
Modified residue321N6-succinyllysine; alternate By similarity
Modified residue371N6-acetyllysine; alternate By similarity
Modified residue371N6-succinyllysine; alternate By similarity
Modified residue441N6-acetyllysine By similarity

Secondary structure

........... 51
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05632 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E0D70FA7C9191CAE

FASTA515,783
        10         20         30         40         50 
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK E 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16978 mRNA. Translation: CAA34849.1. Different initiation.
BC108146 mRNA. Translation: AAI08147.1.
PIRPWBOE. S08239.
RefSeqNP_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.
UniGeneBt.58312.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP05632.
SMRP05632. Positions 2-48.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46312N.
IntActP05632. 1 interaction.
MINTMINT-5007161.
STRING9913.ENSBTAP00000051455.

Chemistry

ChEMBLCHEMBL612444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954.
ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208.
GeneID100335469.
100852024.
617230.
782270.
KEGGbta:100335469.
bta:100852024.
bta:617230.
bta:782270.

Organism-specific databases

CTD514.

Phylogenomic databases

eggNOGNOG318665.
GeneTreeENSGT00390000015470.
HOGENOMHOG000214506.
HOVERGENHBG050611.
InParanoidP05632.
KOK02135.
OMAIRFSAIC.
OrthoDBEOG7GQXZP.
TreeFamTF300278.

Family and domain databases

Gene3D1.10.1620.20. 1 hit.
InterProIPR006721. ATPase_F1-cplx_esu_mt.
[Graphical view]
PfamPF04627. ATP-synt_Eps. 1 hit.
[Graphical view]
SUPFAMSSF48690. SSF48690. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP05632.
NextBio20900552.

Entry information

Entry nameATP5E_BOVIN
AccessionPrimary (citable) accession number: P05632
Secondary accession number(s): Q32PE5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references