The T Complex Polypeptide 1 (TCP-1) is approximately 60 kDa protein constitutively expressed in almost all eukaryotic cells, and is upregulated 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 (HSP70) 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 TCP-1 sequence shows nearly 40% identity to TF55, but only minimal similarity to HSP60 and GroEL.
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Protein Aliases: CCT-alpha; t-complex polypeptide 1; T-complex protein 1 subunit alpha; T-complex protein 1 subunit alpha A; T-complex protein 1 subunit alpha B; T-complex protein 1, alpha subunit; tailless complex polypeptide 1; Tailless complex polypeptide 1A; Tailless complex polypeptide 1B; TCP-1-A; TCP-1-alpha; TCP-1-B
Gene Aliases: AI528772; c-cpn; CCT; CCT-alpha; CCT1; CCTA; D6S230E; p63; Tcp-1; TCP-1-alpha; TCP1; Tp63; TRic
Molecular Function: chaperonin