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The TCP1 eta gene 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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6.
AA408524; AL022769; CCT7; CCTETA; CCT-eta; CCTH; Cctz; chaperonin containing t-complex polypeptide 1, eta subunit; chaperonin containing t-complex subunit eta; chaperonin containing TCP1 subunit 7; chaperonin containing Tcp1, subunit 7 (eta); chaperonin subunit 7 (eta); HIV-1 Nef interacting protein; HIV-1 Nef-interacting protein; MGC110985; NIP7-1; T-complex protein 1 subunit eta; T-complex protein 1 subunit eta, N-terminally processed; TCP1ETA; TCP-1-eta
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