ACBD6 is a protein coding gene that encodes a protein with a molecular mass of approximately 32.2 kDa . The protein contains an acyl-CoA-binding domain near its N-terminus and two ankyrin repeat motifs near its C-terminus . These structural features are essential for its function in binding long-chain acyl-coenzyme A (acyl-CoA) molecules.
The primary function of ACBD6 is to bind long-chain acyl-CoA molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA . Notably, ACBD6 does not bind free fatty acids . This binding activity is crucial for the sequestration, transport, and distribution of long-chain acyl-CoAs within the cell .
ACBD6 is expressed in various human tissues, with notable expression in the placenta and spleen . It is also detected in CD34-positive progenitor cells, cord blood, bone marrow, and undifferentiated placenta-derived stromal embryo-like cells . Immunohistochemical analysis has revealed its presence in hematopoietic CD34-positive progenitors and hemangioblasts .
The binding of long-chain acyl-CoAs by ACBD6 is significant for several cellular processes, including lipid metabolism and gene regulation . Long-chain acyl-CoAs are intermediates in lipid metabolism and can function as signaling molecules. By binding these molecules, ACBD6 plays a role in their cellular sequestration and transport, which is essential for maintaining cellular lipid homeostasis .
Recombinant ACBD6 protein is used in research to study its binding properties and role in lipid metabolism. Studies using recombinant protein expressed in E. coli have shown that ACBD6 binds acyl-CoA substrates with varying affinities, suggesting its potential as a target for therapeutic interventions in disorders related to lipid metabolism .