Alternative titles; symbols
HGNC Approved Gene Symbol: CCT3
Cytogenetic location: 1q22 Genomic coordinates (GRCh38): 1:156,308,968-156,338,292 (from NCBI)
Molecular chaperones are proteins capable of folding or assembling nascent proteins in a higher order structure. A molecular chaperone called TCP1 ring complex (TRiC) plays a role in actin and tubulin folding. TRiC is composed of 2 heteromeric subunits of 6 to 9 different proteins. The cytoplasmic T-complex protein-1 (TCP1; 186980), an abundant testicular germ cell protein, has been found in this complex. Other components of TRiC, such as TRIC5, are TCP1-related proteins (Sevigny et al., 1994).
Joly et al. (1994) cloned a mouse cDNA corresponding to tryptic fragments of the bovine TRiCP5 subunit described by Frydman et al. (1992). The mouse TRiCP5 shares 48% nucleotide and 34% amino acid homology with mouse Tcp1. It is a cytosolic protein also found in the nuclear matrix of several cultured human cell lines. Furthermore, like TCP1, it is highly expressed in testis.
Sevigny et al. (1994) cloned a partial human cDNA clone homologous to mouse TRiCP5.
Walkley et al. (1996) cloned the human cDNA from a kidney library. The 1.9-kb cDNA encodes a predicted 544-amino acid protein that is 98% similar to the mouse sequence and 75% similar to the yeast gene. The mRNA is expressed in a variety of human tissues and at high levels in mouse testis.
Sevigny et al. (1996) cloned the gene coding for the mouse P5 subunit.
Feldman et al. (1999) demonstrated that the folding and assembly of the VHL protein (608537) into a complex with its partner proteins, elongin B (600787) and elongin C (600788), is directly mediated by the chaperonin TRiC. Their results defined a novel role for TRiC in mediating oligomerization.
Sevigny et al. (1996) determined that the mouse Tric5 gene contains 14 exons distributed within 25 kb of genomic DNA. Sevigny et al. (1996) used primer extension to demonstrate multiple transcription start points for the Tric5 gene. This was considered consistent with the lack of any obvious TATA box upstream of the transcription start points.
Sevigny et al. (1994) mapped the TRIC5 gene to chromosome 1q23 by fluorescence in situ hybridization. The fact that the human TRIC5 gene is not on chromosome 6 like other TCP1-related proteins implied to Sevigny et al. (1994) that the genes coding the TCP1-related proteins present in the TCP1 ring complex are probably not organized in a cluster and thus are not synchronously regulated by a cis-acting control region such as the LCR involved in the regulation of globin synthesis.
Sevigny et al. (1996) showed that the mouse genome contains 1 Tric5 gene and 1 Tric5 pseudogene located on chromosomes 3F and 5B, respectively.
Feldman, D. E., Thulasiraman, V., Ferreyra, R. G., Frydman, J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Molec. Cell 4: 1051-1061, 1999. [PubMed: 10635329] [Full Text: https://doi.org/10.1016/s1097-2765(00)80233-6]
Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J. S., Tempst, P., Hartl, F.-U. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 11: 4767-4778, 1992. [PubMed: 1361170] [Full Text: https://doi.org/10.1002/j.1460-2075.1992.tb05582.x]
Joly, E. C., Sevigny, G., Todorov, I. T., Bibor-Hardy, V. cDNA encoding a novel TCP1-related protein. Biochim. Biophys. Acta 1217: 224-226, 1994. [PubMed: 8110840] [Full Text: https://doi.org/10.1016/0167-4781(94)90041-8]
Sevigny, G., Joly, E. C., Bibor-Hardy, V., Lemieux, N. Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization. Genomics 22: 634-636, 1994. [PubMed: 8001976] [Full Text: https://doi.org/10.1006/geno.1994.1438]
Sevigny, G., Lemieux, N., Steyaert, A., Bibor-Hardy, V. Structure of the gene coding for the mouse TRiC-P5 subunit of the cytosolic chaperonin TRiC. Genomics 31: 107-110, 1996. [PubMed: 8808286] [Full Text: https://doi.org/10.1006/geno.1996.0015]
Walkley, N. A., Demaine, A. G., Malik, A. N. Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT-gamma. Biochem. J. 313: 381-389, 1996. [PubMed: 8573069] [Full Text: https://doi.org/10.1042/bj3130381]