Recombinant Human T-complex protein 1 subunit delta (CCT4)

Uniprot Id

P50991

Target Species

Human

Target Name

CCT4

Target Full Name

T-complex protein 1 subunit delta

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. 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.

Target Subcellular Location

Cytoplasm. Melanosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, cilium basal body.

Target Protein Families

TCP-1 chaperonin family

Target Synonyms

CCT4; CCTD; SRB; T-complex protein 1 subunit delta; TCP-1-delta; CCT-delta; Stimulator of TAR RNA-binding

Target Background

The chaperonin containing TCP1 (MIM 186980) complex (CCT), also called the TCP1 ring complex, consists of 2 back-to-back rings, each containing 8 unique but homologous subunits, such as CCT4. CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP-driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin (see MIM 102560) and tubulin (see MIM 191130), as well as alpha-transducin (MIM 139330) (Won et al., 1998 [PubMed 9819444]).