|Protein Name||T-complex protein 1 subunit beta|
|Ref Sequence Id||NP_001029411.1|
|Amino Acid Lenth||535|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Presence in other biological fluids/tissue/cells||abundant in the eukaryotic cytosol; TCP-1 is highly expressed in mouse testis|
|Protein Function||Assists the folding of some proteins in cytosol; chaperone activity may be essential for the folding and assembly of various newly synthesized polypeptides; plays a role in the organization of the neuronal cytoskeleton; TCP-1-like cytosolic chaperonin is involved in hepatitis B virus capsid assembly; may play a role in the nucleus as a molecular chaperone and may interact with the nuclear matrix; TCP-1ß𝛽 is one molecular chaperonin, which is highly expressed during hyperglycemiainduced endoplasmic reticulum (ER) stress and helps to fold not only the cytoskeletal-related proteins but also dozens of other proteins|
|Biochemical Properties||Hetero-oligomeric in nature; has 16-18 subunits in a particle; CCT is composed of two superimposed rings, each with eight different subunits - CCT α,ß,ɣ,δ,ε,ζ,θ and η; hydrolysis rate of TRiC (bovine testis equivalent of CCT) at 37°C is 3.3 pM/min in assays containing 0.24 pM TRiC; CCT makes complexes with newly synthesized actin, tubulin and some other proteins in vivo and calculated that the half-life time of actin folding by CCT is 2-3 min and that of tubulin is 5- 10 min; Mg2+ and K+ are known to be important for chaperonin functions, including those of CCT; Caz+ may be important for CCT function as well|
|PTMs||CCT subunits have no bulky post-translational modifications|
|PDB ID||3IYG, 3KTT, 4A0O, 4A0V, 4A0W, 4A13, 4B2T,|
|Additional Comments||member of the chaperonin family which includes GroEL, 60-kDa heat shock protein (Hsp60), Rubisco subunit binding protein (RBP) and thermophilic factor 55 (TF55); other forms present - TCPD_BOVIN, TCPH_BOVIN, TCPG_BOVIN, TCPQ_BOVIN|
|Bibliography||1. Chen, H., You, H., Wang, L., Zhang, X., Zhang, J., & He, W. (2016). Chaperonin-containing T-complex Protein 1 Subunit ζ Serves as an Autoantigen Recognized by Human Vδ2 γδ T Cells in Autoimmune Diseases. The Journal of Biological Chemistry, 291(38), 19985–19993. https://doi.org/10.1074/jbc.M115.700070. |
2. Grantham, J., Ruddock, L. W., Roobol, A., & Carden, M. J. (2002). Eukaryotic chaperonin containing T-complex polypeptide 1 interacts with filamentous actin and reduces the initial rate of actin polymerization in vitro. Cell Stress & Chaperones, 7(3), 235–242. https://doi.org/10.1379/1466-1268(2002)007<0235:ecctcp>2.0.co;2.
3. Wu, C.-Z., Chang, L.-C., Lin, Y.-F., Hung, Y.-J., Pei, D., & Chen, J.-S. (2015). Chaperonin-containing t-complex protein-1 subunit β as a possible biomarker for the phase of glomerular hyperfiltration of diabetic nephropathy. Disease Markers, 2015, 548101. https://doi.org/10.1155/2015/548101.
4. Liu, Y., Jiang, M., Li, C., Yang, P., Sun, H., Tao, D., … Ma, Y. (2011). Human t-complex protein 11 (TCP11), a testis-specific gene product, is a potential determinant of the sperm morphology. The Tohoku Journal of Experimental Medicine, 224(2), 111–117. https://doi.org/10.1620/tjem.224.111.