ATP5F1A — ATP synthase F1 subunit alpha
ATP5F1A belongs to a gene co-expression module in 8 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
ATP5F1A's module in each cell type
About the gene
| Synonyms | ATP5A, ATP5A1, ATP5AL2, ATPM, hATP1, OMR, ORM |
|---|---|
| Chromosome | 18: 46080248-46104334 |
| Predicted location | Intracellular |
| Essential gene | Yes |
| Protein class | Disease related genes, Essential proteins, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Transporters |
| Molecular function | Translocase |
| Biological process | ATP synthesis, Hydrogen ion transport, Ion transport, Transport |
Function
Subunit alpha, 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). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain. Subunit alpha does not bear the catalytic high- affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.