ATP synthase membrane subunit c locus 1 (ATP5MC1)

ATP synthase membrane subunit c locus 1 (ATP5MC1) encodes a membrane-bound proteolipid subunit (subunit c, also known as subunit 9) that forms part of the Fo domain of mitochondrial ATP synthase, the enzyme complex that produces ATP from ADP using the proton gradient generated by the mitochondrial respiratory chain[1][6][7]. Subunit c oligomerizes to form the c-ring, which acts as a rotary motor and proton channel, coupling the flow of protons across the mitochondrial inner membrane to the mechanical rotation that drives the synthesis of ATP in the F1 catalytic domain[2][4][6]. Inhibitors such as oligomycin and DCCD directly target subunit c, blocking proton translocation and halting ATP production, which underlines its critical role in energy metabolism[2][6]. Dysregulation or mutation of ATP5MC1 can lead to a variety of mitochondrial disorders, and its function is fundamental in all eukaryotic cells[3][6]. **Note:** While ATP5MC1 is a fundamental enzyme subunit and a target for research reagents (e.g., oligomycin), it is *not a drug target* for systemic therapeutic inhibition because of its essential cellular function and the risk of global energy failure. It is, however, a well-established biochemical and pharmacological target in research.

Other names

ATP synthase F(0) complex subunit C1, mitochondrialATP5G1ATP5GATPase protein 9ATPase subunit 9ATPase subunit cATP synthase proteolipid P1ATP synthase proton-transporting mitochondrial F(0) complex subunit C1ATP synthase subunit 9dicyclohexylcarbodiimide (DCCD)-reactive proteolipid subunitProton-conducting channelATP synthase lipid-binding proteinATP synthase, H+ transporting, mitochondrial Fo complex, subunit C1 (subunit 9)

**Oligomycin**: Binds to subunit c and inhibits proton translocation, blocking ATP synthesis[2][6]. **DCCD**: Covalently modifies subunit c, blocking its proton-carrying activity[2][6].