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    Cct3 chaperonin containing TCP1 subunit 3 [ Mus musculus (house mouse) ]

    Gene ID: 12462, updated on 9-Dec-2024

    Summary

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    Official Symbol
    Cct3provided by MGI
    Official Full Name
    chaperonin containing TCP1 subunit 3provided by MGI
    Primary source
    MGI:MGI:104708
    See related
    Ensembl:ENSMUSG00000001416 AllianceGenome:MGI:104708
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    Cctg; TriC-P5; Tcp1-rs3
    Summary
    Predicted to enable protein folding chaperone and unfolded protein binding activity. Acts upstream of or within binding activity of sperm to zona pellucida. Located in cell body. Part of chaperonin-containing T-complex and zona pellucida receptor complex. Is expressed in several structures, including branchial arch; fronto-nasal process; and limb. Orthologous to human CCT3 (chaperonin containing TCP1 subunit 3). [provided by Alliance of Genome Resources, Dec 2024]
    Expression
    Ubiquitous expression in CNS E11.5 (RPKM 119.9), placenta adult (RPKM 98.5) and 28 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Cct3 in Genome Data Viewer
    Location:
    3 F1; 3 38.79 cM
    Exon count:
    14
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 3 NC_000069.7 (88204442..88229073)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 3 NC_000069.6 (88297135..88321766)

    Chromosome 3 - NC_000069.7Genomic Context describing neighboring genes Neighboring gene Rhesus blood group-associated B glycoprotein Neighboring gene STARR-seq mESC enhancer starr_08178 Neighboring gene STARR-seq mESC enhancer starr_08179 Neighboring gene TSSK6 activating co-chaperone Neighboring gene glycosylated lysosomal membrane protein Neighboring gene transmembrane protein 79

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

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    Related articles in PubMed

    1. Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. Pappenberger G, et al. J Mol Biol, 2002 May 17. PMID 12083524
    2. A Tetrahymena orthologue of the mouse chaperonin subunit CCT gamma and its coexpression with tubulin during cilia recovery. Soares H, et al. J Biol Chem, 1994 Nov 18. PMID 7961900
    3. Cellular chaperonin CCTγ contributes to rabies virus replication during infection. Zhang J, et al. J Virol, 2013 Jul. PMID 23637400, Free PMC Article
    4. The cytosolic chaperonin subunit TRiC-P5 begins to be expressed at the two-cell stage in mouse embryos. Sévigny G, et al. Biochem Biophys Res Commun, 1995 Nov 2. PMID 7488101
    5. Structure of the gene coding for the mouse TRiC-P5 subunit of the cytosolic chaperonin TRiC. Sévigny G, et al. Genomics, 1996 Jan 1. PMID 8808286

    See all (74) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Cellular chaperonin CCTgamma contributes to rabies virus replication during infection.
      Title: Cellular chaperonin CCTγ contributes to rabies virus replication during infection.
    Submit: New GeneRIF Correction

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Endonuclease-mediated (2) 
    • Transgenic (1) 

    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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    Markers

    Homology

    Gene Ontology Provided by MGI

    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 protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein folding chaperone ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within binding of sperm to zona pellucida IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in chaperone mediated protein folding independent of cofactor IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in chaperone-mediated protein folding ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in positive regulation of establishment of protein localization to telomere ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in positive regulation of telomere maintenance via telomerase IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in positive regulation of telomere maintenance via telomerase ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in protein stabilization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein stabilization ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in cell body IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in microtubule IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in microtubule ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in myelin sheath HDA PubMed 
    part_of zona pellucida receptor complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    T-complex protein 1 subunit gamma
    Names
    CCT-gamma
    TCP-1-gamma
    chaperonin containing Tcp1, subunit 3 (gamma)
    chaperonin subunit 3 (gamma)
    matricin

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_009836.1 → NP_033966.1  T-complex protein 1 subunit gamma

      See identical proteins and their annotated locations for NP_033966.1

      Status: PROVISIONAL

      Source sequence(s)
      Z31556
      Consensus CDS
      CCDS17468.1
      UniProtKB/Swiss-Prot
      P80318
      UniProtKB/TrEMBL
      Q3U4U6, Q3UJP4
      Related
      ENSMUSP00000001452.8, ENSMUST00000001452.14
      Conserved Domains (2) summary
      cd03337
      Location:6 → 525
      TCP1_gamma; TCP-1 (CTT or eukaryotic type II) chaperonin family, gamma subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins ...
      TIGR02344
      Location:6 → 529
      chap_CCT_gamma; T-complex protein 1, gamma subunit

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

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

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000069.7 Reference GRCm39 C57BL/6J

      Range
      88204442..88229073
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P80318.1 GenPept UniProtKB/Swiss-Prot:P80318

    Gene LinkOut

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