Description
Product Characteristics: T-complex polypeptide-1 (TCP1) is a ~60 kDa protein constitutively expressed in almost all eukaryotic cells, and is up-regulated during spermatogenesis. It is found in the cytosol as a subunit of a hetero-oligomeric chaperone that is known to be involved in the folding of actin and tubulin. The family of proteins termed chaperonins act to recognize and stabilize polypeptide intermediates during folding, assembly and disassembly, and share many characteristics with Heat Shock Protein 70 (HSP 70) including high abundance, induction by environmental stress, and ATPase activity. The chaperonin family includes the mitochondrial HSP60, Escherichia coli GroEL, the plastid Rubisco-subunit binding protein, and the archaebacterial protein TF55. The TCP1 sequence shows nearly 40 % identity to TF55, but only minimal similarity to HSP60 and GroEL.
Target Information: 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, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found. [provided by RefSeq, Jun 2010]