Search Results
Overview
| Uniprot ID | P56382 |
|---|---|
| Protein Name | ATP synthase F(1) complex subunit epsilon, mitochondrial |
| Gene Name | Atp5f1e |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 21 | RFSQICAKAVRDALK |
| 32 | DALKTEFKANAEKTS |
| 37 | EFKANAEKTSGSSIK |
| 44 | KTSGSSIKIVKVSKK |
Function
Subunit epsilon, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). May be essential for the assembly of F(1) and may play an important role in the incorporation of the hydrophobic subunit c into the F(1)-c oligomer rotor of the mitochondrial ATP synthase complex (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0045259 | proton-transporting ATP synthase complex |
| Molecular Function | GO:0008553 | P-type proton-exporting transporter activity |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0046933 | proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process | GO:0015986 | proton motive force-driven ATP synthesis |
| Biological Process | GO:0042776 | proton motive force-driven mitochondrial ATP synthesis |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.