ATP synthase membrane subunit j, mitochondrial (ATP5MJ)

ATP synthase membrane subunit j, mitochondrial (ATP5MJ) is a small, integral membrane protein that is a component of the F0 complex of mitochondrial ATP synthase (Complex V)[1]. It plays a role in ATP production by participating in the rotary mechanism that couples proton translocation across the mitochondrial membrane to ATP synthesis in the F1 catalytic domain[1][2]. ATP5MJ is necessary for maintaining the overall ATP synthase population within mitochondria and, through this, is essential for normal cellular bioenergetics. Mutations or deficiencies in ATP5MJ may be associated with mitochondrial dysfunction and linked to diseases such as streptococcal meningitis and cone-rod dystrophy[1]. As a subunit of a fundamental energy-generating enzyme complex, it is not commonly a direct therapeutic target, but can be affected by inhibitors of the whole ATP synthase, such as oligomycin[3]. Because of its essential role in mitochondrial energy metabolism, it is highly conserved and critical for cell viability[1].

Other names

ATP5MPLC14orf2MP68PRO1574MLQ6.8PL6.8 kDa mitochondrial proteolipid proteinATP synthase membrane subunit 6.8PL6.8 kDa mitochondrial proteolipid6.8-kDa proteolipid with N-terminal sequence Met-Leu-GlnPLPM

Inhibition of ATP synthase by blocking proton translocation (for drugs like oligomycin that target the F0 domain, which includes membrane subunits)