UniProtKB - P05632 (ATP5E_BOVIN)
ATP synthase subunit epsilon, mitochondrial
ATP5F1E
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
- proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
GO - Biological processi
- mitochondrial ATP synthesis coupled proton transport Source: GO_Central
Keywordsi
Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Enzyme and pathway databases
Reactomei | R-BTA-163210, Formation of ATP by chemiosmotic coupling R-BTA-8949613, Cristae formation |
Names & Taxonomyi
Protein namesi | Recommended name: ATP synthase subunit epsilon, mitochondrialCuratedShort name: ATPase subunit epsilon Alternative name(s): ATP synthase F1 subunit epsilonBy similarity |
Gene namesi | |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | HostDB:ENSBTAG00000039208 HostDB:ENSBTAG00000051801 |
VGNCi | VGNC:103015, ATP5F1E |
Subcellular locationi
Mitochondrion
Mitochondrion
- mitochondrial inner membrane Source: GO_Central
- mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
- mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) Source: InterPro
Keywords - Cellular componenti
CF(1), Membrane, Mitochondrion, Mitochondrion inner membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000071661 | 2 – 51 | ATP synthase subunit epsilon, mitochondrialAdd BLAST | 50 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 21 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 21 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 32 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 32 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 37 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 44 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P05632 |
PRIDEi | P05632 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000032954, Expressed in renal medulla and 96 other tissues |
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 ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ.
3 PublicationsProtein-protein interaction databases
CORUMi | P05632 |
DIPi | DIP-46312N |
IntActi | P05632, 7 interactors |
MINTi | P05632 |
STRINGi | 9913.ENSBTAP00000051455 |
Chemistry databases
BindingDBi | P05632 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P05632 |
SMRi | P05632 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05632 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3495, Eukaryota |
GeneTreei | ENSGT00390000015470 |
HOGENOMi | CLU_187039_4_0_1 |
InParanoidi | P05632 |
OMAi | SQICANA |
OrthoDBi | 1628103at2759 |
TreeFami | TF300278 |
Family and domain databases
CDDi | cd12153, F1-ATPase_epsilon, 1 hit |
Gene3Di | 1.10.1620.20, 1 hit |
InterProi | View protein in InterPro IPR006721, ATP_synth_F1_esu_mt IPR036742, ATP_synth_F1_esu_sf_mt |
PANTHERi | PTHR12448, PTHR12448, 1 hit |
Pfami | View protein in Pfam PF04627, ATP-synt_Eps, 1 hit |
SUPFAMi | SSF48690, SSF48690, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK
E
Sequence cautioni
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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_002697025.2, XM_002696979.4 XP_005193391.1, XM_005193334.3 |
Genome annotation databases
Ensembli | ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208 ENSBTAT00000085877; ENSBTAP00000063027; ENSBTAG00000051801 |
GeneIDi | 617230 |
KEGGi | bta:617230 |
Similar proteinsi
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 |
PIRi | S08239, PWBOE |
RefSeqi | NP_001137213.1, NM_001143741.1 XP_002697025.2, XM_002696979.4 XP_005193391.1, XM_005193334.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
4YXW | X-ray | 3.10 | I | 2-51 | [»] | |
5ARA | electron microscopy | 6.70 | I | 2-51 | [»] | |
5ARE | electron microscopy | 7.40 | I | 2-51 | [»] | |
5ARH | electron microscopy | 7.20 | I | 2-51 | [»] | |
5ARI | electron microscopy | 7.40 | I | 2-51 | [»] | |
5FIJ | electron microscopy | 7.40 | I | 2-51 | [»] | |
5FIK | electron microscopy | 6.40 | I | 2-51 | [»] | |
5FIL | electron microscopy | 7.10 | I | 2-51 | [»] | |
6YY0 | electron microscopy | 3.23 | I | 2-51 | [»] | |
6Z1R | electron microscopy | 3.29 | I | 2-51 | [»] | |
6Z1U | electron microscopy | 3.47 | I | 2-51 | [»] | |
6ZG7 | electron microscopy | 3.49 | I | 2-51 | [»] | |
6ZG8 | electron microscopy | 3.49 | I | 2-51 | [»] | |
6ZIK | electron microscopy | 3.66 | I | 2-51 | [»] | |
6ZPO | electron microscopy | 4.00 | I | 2-51 | [»] | |
6ZQM | electron microscopy | 3.29 | I | 2-51 | [»] | |
6ZQN | electron microscopy | 4.00 | I | 2-51 | [»] | |
7AJB | electron microscopy | 9.20 | AI/I | 2-51 | [»] | |
7AJC | electron microscopy | 11.90 | AI/I | 2-51 | [»] | |
7AJD | electron microscopy | 9.00 | AI/I | 2-51 | [»] | |
7AJE | electron microscopy | 9.40 | AI/I | 2-51 | [»] | |
7AJF | electron microscopy | 8.45 | AI/I | 2-51 | [»] | |
7AJG | electron microscopy | 10.70 | AI/I | 2-51 | [»] | |
7AJH | electron microscopy | 9.70 | AI/I | 2-51 | [»] | |
7AJI | electron microscopy | 11.40 | AI/I | 2-51 | [»] | |
7AJJ | electron microscopy | 13.10 | AI/I | 2-51 | [»] | |
AlphaFoldDBi | P05632 | |||||
SMRi | P05632 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P05632 |
DIPi | DIP-46312N |
IntActi | P05632, 7 interactors |
MINTi | P05632 |
STRINGi | 9913.ENSBTAP00000051455 |
Chemistry databases
BindingDBi | P05632 |
ChEMBLi | CHEMBL612444 |
Proteomic databases
PaxDbi | P05632 |
PRIDEi | P05632 |
Genome annotation databases
Ensembli | ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208 ENSBTAT00000085877; ENSBTAP00000063027; ENSBTAG00000051801 |
GeneIDi | 617230 |
KEGGi | bta:617230 |
Organism-specific databases
CTDi | 514 |
VEuPathDBi | HostDB:ENSBTAG00000039208 HostDB:ENSBTAG00000051801 |
VGNCi | VGNC:103015, ATP5F1E |
Phylogenomic databases
eggNOGi | KOG3495, Eukaryota |
GeneTreei | ENSGT00390000015470 |
HOGENOMi | CLU_187039_4_0_1 |
InParanoidi | P05632 |
OMAi | SQICANA |
OrthoDBi | 1628103at2759 |
TreeFami | TF300278 |
Enzyme and pathway databases
Reactomei | R-BTA-163210, Formation of ATP by chemiosmotic coupling R-BTA-8949613, Cristae formation |
Miscellaneous databases
EvolutionaryTracei | P05632 |
PROi | PR:P05632 |
Gene expression databases
Bgeei | ENSBTAG00000032954, Expressed in renal medulla and 96 other tissues |
Family and domain databases
CDDi | cd12153, F1-ATPase_epsilon, 1 hit |
Gene3Di | 1.10.1620.20, 1 hit |
InterProi | View protein in InterPro IPR006721, ATP_synth_F1_esu_mt IPR036742, ATP_synth_F1_esu_sf_mt |
PANTHERi | PTHR12448, PTHR12448, 1 hit |
Pfami | View protein in Pfam PF04627, ATP-synt_Eps, 1 hit |
SUPFAMi | SSF48690, SSF48690, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATP5E_BOVIN | |
Accessioni | P05632Primary (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: | May 25, 2022 | |
This is version 181 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families