Search Results
Overview
| Uniprot ID | P30049 |
|---|---|
| Protein Name | ATP synthase F(1) complex subunit delta, mitochondrial |
| Gene Name | ATP5F1D |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 136 | AAKANLEKAQAELVG |
| 165 | EANEALVKALE**** |
Function
Subunit delta, 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 (Probable) (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the central stalk subunit gamma, is essential for the biogenesis of F(1) catalytic part of the ATP synthase complex namely in the formation of F1 assembly intermediate (PubMed:29499186)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0045259 | proton-transporting ATP synthase complex |
| Molecular Function | GO:0046933 | proton-transporting ATP synthase activity, rotational mechanism |
| Molecular Function | GO:0005198 | structural molecule activity |
| Biological Process | GO:0009060 | aerobic respiration |
| Biological Process | GO:0033615 | mitochondrial proton-transporting ATP synthase complex assembly |
| Biological Process | GO:0015986 | proton motive force-driven ATP synthesis |
| Biological Process | GO:0042776 | proton motive force-driven mitochondrial ATP synthesis |
| Biological Process | GO:0046688 | response to copper ion |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.