T-complex protein 1 subunit gamma (CCT3)
The protein contains 545 amino acids for an estimated molecular weight of 60534 Da.
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). The TRiC complex plays a role in the folding of actin and tubulin (Probable). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs2230194 |
Biological Process
'de novo' posttranslational protein folding
'de novo' protein folding
Binding of sperm to zona pellucida
Cellular protein metabolic process
Chaperone-mediated protein folding
Pore complex assembly
Positive regulation of establishment of protein localization to telomere
Positive regulation of protein localization to Cajal body
Positive regulation of telomerase RNA localization to Cajal body
Positive regulation of telomere maintenance via telomerase
Protein folding
Protein stabilization
Toxin transport
Cellular Component
Cell body
Chaperonin-containing T-complex
Cytoplasm
Cytoskeleton
Cytosol
Extracellular exosome
Microtubule
Myelin sheath
Plasma membrane
Zona pellucida receptor complex
Molecular Function
ATP binding
ATPase
Poly(A) RNA binding
Protein folding chaperone
RNA binding
Unfolded protein binding
The reference OMIM entry for this protein is 600114
Chaperonin containing t-complex polypeptide 1, subunit 3; cct3
Chaperonin containing tcp1, subunit 3
Cct-gamma; cctg
Tcp1 ring complex, polypeptide 5; tric5
DESCRIPTION
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).CLONING
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.GENE FUNCTION
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.GENE STRUCTURE
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.MAPPING
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. ... More on the omim web site
Oct. 2, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600114 was added.