The BOLA3 gene provides instructions for making a protein whose function is not well understood. The BOLA3 protein is thought to be involved in the formation of molecules called iron-sulfur (Fe-S) clusters or in the attachment of these clusters to other proteins. Certain proteins require attachment of Fe-S clusters to function properly.

Two versions (isoforms) of the BOLA3 protein are produced from the BOLA3 gene. One version is found in cellular structures called mitochondria. Mitochondria are the energy-producing centers of cells. In these structures, several proteins carry out a series of chemical steps to convert the energy in food into a form that cells can use. Many of the proteins involved in this process require Fe-S clusters to function, including protein complexes called complex I, complex II, and complex III.

Fe-S clusters are also required for another mitochondrial protein to function; this protein is involved in the modification of additional proteins that aid in energy production in mitochondria, including the pyruvate dehydrogenase complex and the alpha-ketoglutarate dehydrogenase complex. This modification is also critical to the function of the glycine cleavage system, a set of proteins that breaks down a protein building block (amino acid) called glycine when levels become too high.

The other version of the BOLA3 protein is found in the fluid-filled space inside the cell (the cytoplasm). While this protein is likely involved in Fe-S cluster formation in the cytoplasm, the role of this isoform is not well understood.