ATP synthase is extremely conserved through evolution and can be found in plants, fungi, bacteria, and animals. The ATP synthase enzyme is a transmembrane protein responsible for driving the reversible reaction from ADP+ phosphate to ATP. This reaction is accomplished by a flux of protons across the membrane as a result of electron transfer. The ATP synthase protein has two main sections; the F1 ATP-ase (soluble) and the F0 ATP-ase (membrane embedded). The F1 section consists of the alpha, beta, gamma, delta, and epsilon subunits. While the F0 consists of a, b, and c subunits.
Protein Aliases: apoptosis inhibitor protein 3; baculoviral IAP repeat-containing 4; Baculoviral IAP repeat-containing protein 4; BIR4; E3 ubiquitin-protein ligase XIAP; HILP; IAP homolog A; IAP-3; IAP-like protein; ILP; Inhibitor of apoptosis protein 3; RIAP-3; RING-type E3 ubiquitin transferase XIAP; RP1-315G1.5; X-linked IAP; X-linked inhibitor of apoptosis protein; X-linked inhibitor of apoptosis, E3 ubiquitin protein ligase
Gene Aliases: 1110015C02Rik; Aipa; API3; BIRC4; hIAP-3; hIAP3; IAP-3; IAP3; ILP-1; ILP1; MIHA; riap3; XIAP; XLP2
Molecular Function: protease inhibitor