CCT3

CCT3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1GML, 1GN1
Identifiers
Aliases	CCT3, CCT-gamma, CCTG, PIG48, TCP-1-gamma, TRIC5, chaperonin containing TCP1 subunit 3
External IDs	OMIM: 600114 MGI: 104708 HomoloGene: 4373 GeneCards: CCT3
Gene location (Human) Chr. Chromosome 1 (human) Band 1q22 Start 156,308,968 bp End 156,367,873 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 F1|3 38.79 cM Start 88,204,423 bp End 88,229,074 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in embryo islet of Langerhans ganglionic eminence right adrenal gland smooth muscle tissue left adrenal gland appendix lymph node rectum stromal cell of endometrium Top expressed in primitive streak otic placode Paneth cell maxillary prominence saccule condyle somite spermatocyte abdominal wall medial ganglionic eminence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein folding chaperone activity protein binding ATP binding unfolded protein binding RNA binding Cellular component cell body myelin sheath plasma membrane zona pellucida receptor complex chaperonin-containing T-complex microtubule cytoskeleton extracellular exosome cytoplasm cytosol Biological process positive regulation of protein localization to Cajal body pore complex assembly protein stabilization positive regulation of telomere maintenance via telomerase toxin transport protein folding positive regulation of telomerase RNA localization to Cajal body binding of sperm to zona pellucida 'de novo' protein folding chaperone-mediated protein folding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7203 12462 Ensembl ENSG00000163468 ENSMUSG00000001416 UniProt P49368 Q5SZW8 P80318 RefSeq (mRNA) NM_001008800 NM_001008883 NM_005998 NM_009836 RefSeq (protein) NP_001008800 NP_005989 NP_033966 Location (UCSC) Chr 1: 156.31 – 156.37 Mb Chr 3: 88.2 – 88.23 Mb PubMed search
Wikidata
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T-complex protein 1 subunit gamma is a protein that in humans is encoded by the CCT3 gene.

Function

This gene encodes a molecular chaperone that is member of the TRiC complex. 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, encoding different isoforms, have been characterized.

Interactions

CCT3 has been shown to interact with PPP4C.

External links

• Human CCT3 genome location and CCT3 gene details page in the UCSC Genome Browser.

Further reading

• Kubota H, Hynes G, Carne A, Ashworth A, Willison K (Feb 1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 (2): 89–99. Bibcode:1994CBio....4...89K. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530. S2CID 31300131.
• Sévigny G, Joly EC, Bibor-Hardy V, Lemieux N (Aug 1994). "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band 1q23 by fluorescence in situ hybridization". Genomics. 22 (3): 634–6. doi:10.1006/geno.1994.1438. PMID 8001976.
• Walkley NA, Demaine AG, Malik AN (Jan 1996). "Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma". The Biochemical Journal. 313 (Pt 2): 381–9. doi:10.1042/bj3130381. PMC 1216920. PMID 8573069.
• Feldman DE, Thulasiraman V, Ferreyra RG, Frydman J (Dec 1999). "Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC". Molecular Cell. 4 (6): 1051–61. doi:10.1016/S1097-2765(00)80233-6. PMID 10635329.
• Wong N, Chan A, Lee SW, Lam E, To KF, Lai PB, Li XN, Liew CT, Johnson PJ (Mar 2003). "Positional mapping for amplified DNA sequences on 1q21-q22 in hepatocellular carcinoma indicates candidate genes over-expression". Journal of Hepatology. 38 (3): 298–306. doi:10.1016/S0168-8278(02)00412-9. PMID 12586295.
• Yuryev A, Wennogle LP (Feb 2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis". Genomics. 81 (2): 112–25. doi:10.1016/S0888-7543(02)00008-3. PMID 12620389.
• Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (Oct 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Experimental Cell Research. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
• Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (Dec 2003). "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". The Journal of Biological Chemistry. 278 (51): 51901–10. doi:10.1074/jbc.M309655200. PMID 14532270.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.