Based on limited published evidence, CCT8L2 is a chaperonin-containing TCP1 subunit-like protein with predicted molecular chaperone function. UniProt annotations indicate it assists protein folding through ATP hydrolysis and binds unfolded proteins. GO terms suggest involvement in the chaperonin-containing T-complex and protein folding pathways. CCT8L2 originated from duplication of the CCT8 lineage at the onset of mammalian evolution and duplicated further in primates 1. Unlike canonical CCT complexes, CCT8L2 likely retains a chaperonin-like core structure but is unlikely to form typical oligomeric complexes 1. Additional functions in calcium-activated potassium channel activity remain uncharacterized.