CCT8 Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. Belongs to the TCP-1 chaperonin family. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.

Protein type: Chaperone; Motility/polarity/chemotaxis

Chromosomal Location of human Ortholog: 21q21.3

Cellular Component: azurophil granule lumen; cell body; centrosome; chaperonin-containing T-complex; cilium; cytoplasm; cytosol; extracellular region; ficolin-1-rich granule lumen; intermediate filament cytoskeleton; microtubule; nucleoplasm; secretory granule lumen; zona pellucida receptor complex

Molecular Function: ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; protein binding; protein folding chaperone; unfolded protein binding

Biological Process: binding of sperm to zona pellucida; chaperone-mediated protein folding; positive regulation of establishment of protein localization to telomere; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization

Reference #: P50990 (UniProtKB)

Alt. Names/Synonyms: C21orf112; CCT-theta; CCT8; CCTQ; Chaperonin containing T-complex polypeptide 1 subunit 8; chaperonin containing TCP1 subunit 8; chaperonin containing TCP1, subunit 8 (theta); D21S246; KIAA0002; PRED71; Renal carcinoma antigen NY-REN-15; T-complex protein 1 subunit theta; T-complex protein 1, theta subunit; TCP-1-theta; TCPQ

Gene Symbols: CCT8

Molecular weight: 59,621 Da

Basal Isoelectric point: 5.42 Predict pI for various phosphorylation states

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CCT8

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