Search by BoMiProt ID - Bomi86

Primary Information

BoMiProt ID Bomi86
Protein Name T-complex protein 1 subunit beta
Organism Bos taurus
Uniprot IDQ3ZBH0
Milk FractionExosome
Ref Sequence ID NP_001029411.1
Aminoacid Length 535
Molecular Weight 57475
FASTA Sequence Download
Gene Name CCT2
Gene ID 505313
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

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-1ß? 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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
CATH Matched CATH superfamily
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.
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.<0235:ecctcp>;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.
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.