Chaperonin Containing TCP1, Subunit 5 (Epsilon) (CCT5) ELISA Kit for Human

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 have been observed but have not been thoroughly characterized. In addition, three pseudogenes of this gene have been identified. [provided by RefSeq, Jun 2010]

CCT-epsilon: 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. Defects in CCT5 are the cause of hereditary sensory neuropathy autosomal recessive with spastic paraplegia (HSNSP). The disease is characterized by spastic paraplegia and progressive distal sensory neuropathy leading to mutilating ulcerations of the upper and lower limbs. Belongs to the TCP-1 chaperonin family.

Protein type: Chaperone

Chromosomal Location of Human Ortholog: 5p15.2

Cellular Component: chaperonin-containing T-complex; microtubule; centrosome; cytoplasm; nucleolus; cytosol

Molecular Function: protein binding; unfolded protein binding; beta-tubulin binding; G-protein beta-subunit binding; ATP binding

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

Disease: Neuropathy, Hereditary Sensory, With Spastic Paraplegia, Autosomal Recessive