Bcs1l

The protein encoded by this gene is a chaperone protein that is involved in the assembly of complex III (CIII), one of the five protein complexes of the mitochondrial respiratory chain, and is necessary for the insertion of the Rieske iron-sulfur (RISP) and Qcr10p proteins into the precomplex. Studies from the yeast ortholog of this protein indicate that it is targeted to the inner membrane of the mitochondria, despite the absence of an N-terminal targeting sequence. Positively charged amino acids located C-terminal to the transmembrane domain are thought to act as an internal targeting signal (PMID:8599931). Mutations in the human ortholog of this gene have been associated with GRACILE syndrome, characterized by Growth retardation, Amino aciduria, Cholestasis, Iron overload, Lactic acidosis, and Early death. Mouse models with the corresponding mutation mimic the phenotype of GRACILE syndrome and display decreased complex III activity and decreased electron transport capacity (PMID:21274865). Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2015]

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in mouse Bcs1l often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.

Describes the biological processes, cellular components, and molecular functions associated with the mouse Bcs1l gene, providing context for its role in the cell.