T-Complex 1 (TCP1) Human Recombinant Protein

The protein encoded by this gene is 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, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found. [provided by RefSeq, Jun 2010]

CCT-alpha: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Belongs to the TCP-1 chaperonin family.

Protein type: Motility/polarity/chemotaxis; Chaperone

Chromosomal Location of Human Ortholog: 6q25.3-q26

Cellular Component: Golgi apparatus; chaperonin-containing T-complex; centrosome; microtubule; pericentriolar material; acrosome; nuclear heterochromatin; cytosol

Molecular Function: protein binding; ubiquitin protein ligase binding; unfolded protein binding; ATP binding

Biological Process: tubulin folding; 'de novo' posttranslational protein folding; cellular protein metabolic process; protein folding; binding of sperm to zona pellucida