CCT7

Chaperonin containing TCP1, subunit 7 (eta)
Identifiers
Symbols	CCT7 ; CCTETA; CCTH; NIP7-1; TCP1ETA
External IDs	OMIM: 605140 MGI: 107184 HomoloGene: 4694 GeneCards: CCT7 Gene
Gene ontology Molecular function • protein binding • ATP binding • identical protein binding • unfolded protein binding Cellular component • zona pellucida receptor complex • cytoplasm • mitochondrion • cytosol • chaperonin-containing T-complex • microtubule • cell body • extracellular exosome Biological process • protein folding • binding of sperm to zona pellucida • cellular protein metabolic process • 'de novo' posttranslational protein folding • toxin transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10574	12468
Ensembl	ENSG00000135624	ENSMUSG00000030007
UniProt	Q99832	P80313
RefSeq (mRNA)	NM_001009570	NM_007638
RefSeq (protein)	NP_001009570	NP_031664
Location (UCSC)	Chr 2: 73.23 – 73.25 Mb	Chr 6: 85.45 – 85.47 Mb
PubMed search

T-complex protein 1 subunit eta is a protein that in humans is encoded by the CCT7 gene.^[1][2]

Function

This gene encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). 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 found for this gene, but only two of them have been characterized to date.^[2]

Interactions

CCT7 has been shown to interact with PPP4C.^[3][4]

References

1. Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI (Dec 1998). "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT". Molecular and Cellular Biology 18 (12): 7584–9. PMC: 109339. PMID 9819444.
2. "Entrez Gene: CCT7 chaperonin containing TCP1, subunit 7 (eta)".
3. Chen GI, Tisayakorn S, Jorgensen C, D'Ambrosio LM, Goudreault M, Gingras AC (Oct 2008). "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry 283 (43): 29273–84. doi:10.1074/jbc.M803443200. PMC: 2662017. PMID 18715871.
4. Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R (Nov 2005). "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics 4 (11): 1725–40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.

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. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Hynes G, Celis JE, Lewis VA, Carne A, U S, Lauridsen JB, Willison KR (Nov 1996). "Analysis of chaperonin-containing TCP-1 subunits in the human keratinocyte two-dimensional protein database: further characterisation of antibodies to individual subunits". Electrophoresis 17 (11): 1720–7. doi:10.1002/elps.1150171109. PMID 8982604. Check date values in: |year= / |date= mismatch (help)
• Liou AK, Willison KR (Jul 1997). "Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes". The EMBO Journal 16 (14): 4311–6. doi:10.1093/emboj/16.14.4311. PMC: 1170057. PMID 9250675.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Yokota S, Yanagi H, Yura T, Kubota H (Sep 2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle". European Journal of Biochemistry / FEBS 268 (17): 4664–73. doi:10.1046/j.1432-1327.2001.02393.x. PMID 11532003.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (Oct 2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Research 11 (10): 1758–65. doi:10.1101/gr.180101. PMC: 311163. PMID 11591653.
• 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. Check date values in: |year= / |date= mismatch (help)
• Hanafy KA, Martin E, Murad F (Nov 2004). "CCTeta, a novel soluble guanylyl cyclase-interacting protein". The Journal of Biological Chemistry 279 (45): 46946–53. doi:10.1074/jbc.M404134200. PMID 15347653.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
• Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (Dec 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical Research Communications 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.