Chaperonin Containing TCP1, Subunit 5 (CCT5)

CCT5 encodes a molecular chaperone that is 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 546-amino acid protein shares 95.8% amino acid identity with mouse Cct5. Northern blot analysis detected highest expression in colon, with intermediate or low expression in all other tissues and cell lines examined.