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Protein

ATP synthase subunit epsilon, mitochondrial

Gene

Atp5e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit epsilon, mitochondrial
Short name:
ATPase subunit epsilon
Gene namesi
Name:Atp5e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1855697. Atp5e.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000716631 – 52ATP synthase subunit epsilon, mitochondrialAdd BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21N6-acetyllysine; alternateCombined sources1
Modified residuei21N6-succinyllysine; alternateCombined sources1
Modified residuei32N6-acetyllysine; alternateCombined sources1
Modified residuei32N6-succinyllysine; alternateCombined sources1
Modified residuei37N6-acetyllysine; alternateCombined sources1
Modified residuei37N6-succinyllysine; alternateCombined sources1
Modified residuei44N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP56382.
PaxDbiP56382.
PeptideAtlasiP56382.
PRIDEiP56382.
TopDownProteomicsiP56382.

PTM databases

iPTMnetiP56382.
PhosphoSitePlusiP56382.

Expressioni

Gene expression databases

BgeeiENSMUSG00000016252.
ExpressionAtlasiP56382. baseline and differential.
GenevisibleiP56382. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-1840627.
STRINGi10090.ENSMUSP00000016396.

Structurei

3D structure databases

ProteinModelPortaliP56382.
SMRiP56382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase epsilon family.Curated

Phylogenomic databases

eggNOGiKOG3495. Eukaryota.
ENOG410Y5P5. LUCA.
GeneTreeiENSGT00390000015470.
HOGENOMiHOG000214506.
HOVERGENiHBG050611.
InParanoidiP56382.
KOiK02135.
OMAiANAMKTS.
OrthoDBiEOG091G16RI.
PhylomeDBiP56382.
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.

P56382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAYWRQAGL SYIRFSQICA KAVRDALKTE FKANAEKTSG SSIKIVKVSK

KE
Length:52
Mass (Da):5,838
Last modified:January 23, 2007 - v2
Checksum:i406371C227DAA127
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC024339 mRNA. Translation: AAH24339.1.
CCDSiCCDS38360.1.
RefSeqiNP_080259.1. NM_025983.3.
UniGeneiMm.20841.

Genome annotation databases

EnsembliENSMUST00000016396; ENSMUSP00000016396; ENSMUSG00000016252.
GeneIDi67126.
KEGGimmu:67126.
UCSCiuc008off.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiATP5E_MOUSE
AccessioniPrimary (citable) accession number: P56382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families