CCT7

This 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. Alternate transcriptional splice variants encoding different isoforms have been found for this gene, but only two of them have been characterized to date. [provided by RefSeq]

chaperonin containing TCP1, subunit 7 (eta)

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444).
The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444).
The TRiC complex plays a role in the folding of actin and tubulin (Probable).

Binding of sperm to zona pellucida Source: Ensembl
Positive regulation of establishment of protein localization to telomere Source: BHF-UCL
Positive regulation of protein localization to Cajal body Source: BHF-UCL
Positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
Positive regulation of telomere maintenance via telomerase Source: BHF-UCL
Protein folding Source: FlyBase
Protein stabilization Source: BHF-UCL
Toxin transport Source: Ensembl

Cytoplasm