| Tissue Specificity | Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord. |
| Post Translational Modifications | The N-terminus is blocked. Acetylated on lysine residues. BLOC1S1 is required for acetylation. |
| 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. 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. |
| Protein Name | Atp Synthase F(1 Complex Subunit Alpha - MitochondrialAtp Synthase F1 Subunit Alpha |
| Database Links | Reactome: R-HSA-1268020Reactome: R-HSA-163210Reactome: R-HSA-8949613Reactome: R-HSA-9837999 |
| Cellular Localisation | MitochondrionMitochondrion Inner MembranePeripheral Membrane ProteinMatrix SideCell MembraneExtracellular SideColocalizes With Hrg On The Cell Surface Of T-Cells |
| Alternative Antibody Names | Anti-Atp Synthase F(1 Complex Subunit Alpha - Mitochondrial antibodyAnti-Atp Synthase F1 Subunit Alpha antibodyAnti-ATP5F1A antibodyAnti-ATP5A antibodyAnti-ATP5A1 antibodyAnti-ATP5AL2 antibodyAnti-ATPM antibody |
Information sourced from Uniprot.org
