Complex V, also called F1F0 ATPase or 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, in oxidative phosphorylation, and as a proton pumping ATPase. This reaction is accomplished by a flux of protons across the membrane as a result of electron transfer. The enzyme was thought to be localized exclusively to mitochondria; however, it has recently been identified on the plasma membrane of several cell types including hepatocytes where it functions as the HDL receptor, on endothelial cells where it may act as the angiostatin receptor, and on the surface of cancer cells. 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. The enzyme in mammals is composed of 17 subunits, five of which make up the easily detached F1. The remainder subunits are components of two stalk domains and the proton pumping F0 part of the machinery. Two of the subunits of the F0 part are encoded on mitochondrial DNA while the other subunits are nuclearly encoded. Mutations in the mitochondrial-encoded subunits of ATP synthase (Complex V) cause OXPHOS disease.
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Protein Aliases: ATP synthase F1 subunit epsilon; ATP synthase inhibitor protein; ATPase inhibitor protein; ATPase inhibitor, mitochondrial; IF(1); IF1; Inhibitor of F(1)F(o)-ATPase
Gene Aliases: ATP5IF1; ATPI; ATPIF1; ATPIP; IP
UniProt ID: (Human) Q9UII2
Entrez Gene ID: (Human) 93974
Molecular Function: ligase