Anti-ATP5G2 Antibody

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. HAMAP-Rule MF_01396<br><br>Dyer M.R., Biochem. J. 293:51-64(1993).<br>Higuti T., Biochim. Biophys. Acta 1173:87-90(1993).<br>Farrell L.B., Biochem. Biophys. Res. Commun. 144:1257-1264(1987).

ATP synthase F (0) complex subunit C2, mitochondrial; ATP synthase lipid-binding protein; ATP synthase proteolipid P2; ATP synthase proton-transporting mitochondrial F (0) complex subunit C2; ATPase protein 9; ATPase subunit c; ATP5G2; PSEC0033

Cancer, Metabolism, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Nucleotide Messenger, Pathways and Processes, Second Messenger, Signal Transduction

Mitochondrial membrane ATP synthase (F (1) F (0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F (1) - containing the extramembraneous catalytic core and F (0) - containing the membrane proton channel, linked together by a central stalk and a 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. Part of the complex F (0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.