Based on the available literature, FMC1 (formation of mitochondrial complex V assembly factor 1) appears to function as an assembly factor for mitochondrial ATP synthase (complex V). Computational coevolution analysis and deep learning-based structure modeling identified FMC1 as having a predicted protein-protein interaction with ATPAF2, another ATP synthase assembly factor, suggesting these proteins work together in complex V biogenesis 1. This functional connection between FMC1 and the mitochondrial ATP synthase complex has been experimentally validated through co-expression analysis across large transcriptomic datasets 2. The protein localizes to mitochondria and is involved in mitochondrial proton-transporting ATP synthase complex assembly, consistent with its predicted role in energy metabolism. However, detailed mechanistic studies of FMC1's specific role in complex V assembly, its precise binding partners, and its clinical significance in mitochondrial diseases remain to be characterized. The current evidence strongly supports FMC1's function in mitochondrial bioenergetics, but more research is needed to fully elucidate its molecular mechanisms and potential therapeutic relevance.