Chaperonin Containing TCP1, Subunit 6B (CCT6B)

CCT6B encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.The deduced 540-amino acid protein has a calculated molecular mass of 59.5 kD. CCT6B shares 83% amino acid identity with TCP20 (CCT6A), suggesting it may be a component of a chaperonin complex.The deduced protein contains 531 amino acids.