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CCT3 chaperonin-containing T-complex subunit CCT3 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853438, updated on 2-Nov-2024

Summary

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Official Symbol
CCT3
Official Full Name
chaperonin-containing T-complex subunit CCT3
Primary source
SGD:S000003551
Locus tag
YJL014W
See related
AllianceGenome:SGD:S000003551; FungiDB:YJL014W; VEuPathDB:YJL014W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
BIN2; TCP3
Summary
Enables unfolded protein binding activity. Involved in protein folding. Part of chaperonin-containing T-complex. Orthologous to human CCT3 (chaperonin containing TCP1 subunit 3). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See CCT3 in Genome Data Viewer
Location:
chromosome: X
Exon count:
1
Sequence:
Chromosome: X; NC_001142.9 (407558..409162)

Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Mps3p Neighboring gene Tph3p Neighboring gene Mad3p Neighboring gene Vtc4p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A yeast TCP-1-like protein is required for actin function in vivo. Vinh DB, et al. Proc Natl Acad Sci U S A, 1994 Sep 13. PMID 7916461, Free PMC Article
  2. The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex. Lin P, et al. Proc Natl Acad Sci U S A, 1997 Sep 30. PMID 9380710, Free PMC Article
  3. Chaperone requirements for de novo folding of Saccharomyces cerevisiae septins. Hassell D, et al. Mol Biol Cell, 2022 Oct 1. PMID 35947497, Free PMC Article
  4. Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Chen X, et al. Proc Natl Acad Sci U S A, 1994 Sep 13. PMID 7916460, Free PMC Article
  5. Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae. Lin P, et al. Genetics, 1997 Dec. PMID 9409825, Free PMC Article

See all (79) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis.
    Title: Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis.
  2. The results from this controlled CCT-actin folding assay are consistent with a model where CCT and Ac(I) are in a binding pre-equilibrium with a rate-limiting binding step, followed by a faster ATP-driven processing to native actin.
    Title: Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
  
enables unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables unfolded protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in chaperone mediated protein folding independent of cofactor IEA
Inferred from Electronic Annotation
more info
  
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of chaperonin-containing T-complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of chaperonin-containing T-complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of chaperonin-containing T-complex IEA
Inferred from Electronic Annotation
more info
  
part_of chaperonin-containing T-complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
chaperonin-containing T-complex subunit CCT3
NP_012520.1
  • Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; capable of binding Q/N rich proteins and mediating their folding

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001142.9 Reference assembly

    Range
    407558..409162
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181448.1 → NP_012520.1  TPA: chaperonin-containing T-complex subunit CCT3 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012520.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VWG3, P39077
    UniProtKB/TrEMBL
    B5VLF7, C7GSP5, C8ZBJ7, G2WGZ7, N1P1E5
    Conserved Domains (1) summary
    TIGR02344
    Location:4 → 533
    chap_CCT_gamma; T-complex protein 1, gamma subunit
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P39077.2

Gene LinkOut

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