TCP-1 theta is theta subunit of the CCT (chaperonin containing TCP1 complex) chaperonin molecule which is abundant in the eukaryotic cytosol and may be involved in the transport and assembly of the newly synthesized proteins. Molecular chaperones assist in the protein folding upon ATP hydrolysis and TCP-1 theta may play a role in the assembly of the BBsome, a complex that is involved in ciliogenesis regulating transport vesicles to the cilia. Further, TCP-1 theta is also involved in the folding of actin and tubulin. The intact CCT complex is composed of eight polypeptides in a double ring structure. CCT is important within cells in the folding of the VHL tumor suppressor protein.
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Protein Aliases: bdav; bette davis; CCT-theta; Chaperonin containing T-complex polypeptide 1 subunit 8; chaperonin containing TCP1, subunit 8 (theta); chaperonin subunit 8 (theta); Renal carcinoma antigen NY-REN-15; T-complex protein 1 subunit theta; TCP-1-theta
Gene Aliases: AI132397; C21orf112; CCT8; CCTQ; D21S246; fa22h09; KIAA0002; PRED71; Tcpq; wu:fa22h09; zgc:56059