T-complex protein 1 subunit zeta (CCT6A)

The protein contains 531 amino acids for an estimated molecular weight of 58024 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). 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:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. 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.
  3. 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.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. 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.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

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.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 34

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VariantDescription
dbSNP:rs33922584

The reference OMIM entry for this protein is 104613

Chaperonin containing t-complex polypeptide 1, subunit 6a; cct6a
Cct6
T-complex homolog tcp20; tcp20
Histidine transport regulator 3; htr3
Amino acid transport defect-complementing

CLONING

Segel et al. (1992) used complementation of yeast to isolate a member of a class of genes that carry out the probable function of protecting a regulator protein from indigenous degradation. Although yeast cells normally synthesize amino acids, mutants with biosynthetic defects require uptake of exogenous amino acids for growth. Yeast can import a wide range of amino acids by the general amino acid permease (GAP) which, however, can be repressed with ammonium sulfate. Thus, Saccharomyces cerevisiae with a defect in histidine biosynthesis and histidine uptake does not grow on histidine-containing medium when GAP is repressed by ammonium. Human cDNA clones can directly complement the synthetic or transport defects or indirectly prevent the ammonium repression. The deduced amino acid sequence encoded by one of these cDNA clones in the experiments of Segel et al. (1992) suggested that a chaperonin-like protein was responsible for complementation by preventing ammonium repression. The amino acid sequence encoded by this cDNA clone, designated HTR3 by them (presumably for 'histidine transport regulator'), was related to that of the T-complex proteins (e.g., TCP1, 186980). However, further studies by Li et al. (1994) revealed that the lack of ammonium repression of general amino acid permease also involved secondary mutations which arose in the yeast transformant. Thus the specific action of HTR3 on the yeast amino acid permease was uncertain. Li et al. (1994) reported the nucleotide and amino acid sequences of the human homolog of yeast Tcp20. They found that the TCP20 (CCT6A) protein shows approximately 30% identity to TCP1, a known subunit of the hetero-oligomeric TRiC (see, for example, 600114). Western blot analysis of purified bovine TRiC with a TCP20-specific antibody indicated that TCP20 is also a subunit of TRiC. Gene disruption studies showed that Tcp20, like Tcp1, is an essential gene in yeast.

GENE FUNCTION

Segel et al. (1992) proposed that HTR3, TCP1, and others constitute a class of chaperonins that are cytoplasmic proteins. Although a distinct class, the cytoplasmic chaperonins have a weak but significant sequence similarity to the chaperonin proteins (e.g., 118190). ... More on the omim web site

Subscribe to this protein entry history

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 104613 was added.