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Protein

ATP synthase subunit epsilon, mitochondrial

Gene

ATP5F1E

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit epsilon, mitochondrialCurated
Short name:
ATPase subunit epsilon
Alternative name(s):
ATP synthase F1 subunit epsilonBy similarity
Gene namesi
Name:ATP5F1EBy similarity
Synonyms:ATP5E
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componentsi: Chromosome 13, Chromosome 22

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL612444

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000716612 – 51ATP synthase subunit epsilon, mitochondrialAdd BLAST50

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21N6-acetyllysine; alternateBy similarity1
Modified residuei21N6-succinyllysine; alternateBy similarity1
Modified residuei32N6-acetyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternateBy similarity1
Modified residuei37N6-acetyllysine; alternateBy similarity1
Modified residuei37N6-succinyllysine; alternateBy similarity1
Modified residuei44N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP05632
PRIDEiP05632

Expressioni

Gene expression databases

BgeeiENSBTAG00000032954

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, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68.2 Publications

Protein-protein interaction databases

CORUMiP05632
DIPiDIP-46312N
IntActiP05632, 8 interactors
MINTiP05632
STRINGi9913.ENSBTAP00000051455

Chemistry databases

BindingDBiP05632

Structurei

Secondary structure

151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 24Combined sources13
Turni29 – 31Combined sources3
Helixi33 – 36Combined sources4
Beta strandi44 – 46Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YXWX-ray3.10I2-51[»]
5ARAelectron microscopy6.70I2-51[»]
5AREelectron microscopy7.40I2-51[»]
5ARHelectron microscopy7.20I2-51[»]
5ARIelectron microscopy7.40I2-51[»]
5FIJelectron microscopy7.40I2-51[»]
5FIKelectron microscopy6.40I2-51[»]
5FILelectron microscopy7.10I2-51[»]
ProteinModelPortaliP05632
SMRiP05632
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05632

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase epsilon family.Curated

Phylogenomic databases

eggNOGiKOG3495 Eukaryota
ENOG410Y5P5 LUCA
GeneTreeiENSGT00390000015470
HOGENOMiHOG000214506
HOVERGENiHBG050611
InParanoidiP05632
KOiK02135
OMAiANAMKTS
OrthoDBiEOG091G16RI
TreeFamiTF300278

Family and domain databases

CDDicd12153 F1-ATPase_epsilon, 1 hit
Gene3Di1.10.1620.20, 1 hit
InterProiView protein in InterPro
IPR006721 ATP_synth_F1_esu_mt
IPR036742 ATP_synth_F1_esu_sf_mt
PANTHERiPTHR12448 PTHR12448, 1 hit
PfamiView protein in Pfam
PF04627 ATP-synt_Eps, 1 hit
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 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_002697025.2, XM_002696979.4
XP_005193391.1, XM_005193334.3
UniGeneiBt.58312

Genome annotation databases

EnsembliENSBTAT00000035337; ENSBTAP00000035213; ENSBTAG00000032954
ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208
GeneIDi617230
782270
KEGGibta:617230
bta:782270

Similar proteinsi

Entry informationi

Entry nameiATP5E_BOVIN
AccessioniPrimary (citable) accession number: P05632
Secondary accession number(s): Q32PE5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 161 of the entry and version 4 of the sequence. See 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

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