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

    Gene ID: 853438, updated on 9-Dec-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, Dec 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 (80) 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

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