Recombinant Human T-complex protein 1 subunit eta (CCT7)

Uniprot Id

Q99832

Target Species

Human

Target Name

CCT7

Target Full Name

T-complex protein 1 subunit eta

Target Function

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. The TRiC complex plays a role in the folding of actin and tubulin.

Target Subcellular Location

Cytoplasm.

Target Protein Families

TCP-1 chaperonin family

Target Synonyms

CCT ETA; CCT-eta; CCT7; CCTETA; Ccth; Chaperonin containing t complex polypeptide 1 eta subunit; Chaperonin containing TCP1 subunit 7 (eta); Chaperonin containing TCP1 subunit 7; HIV 1 Nef interacting protein; HIV-1 Nef-interacting protein; Nip7 1; T complex protein 1 eta subunit; T-complex protein 1 subunit eta, N-terminally processed; TCP-1-eta; TCP1eta; TCPH_HUMAN

Target Background

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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6.