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    CPR7 peptidylprolyl isomerase CPR7 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853489, updated on 9-Dec-2024

    Summary

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    Official Symbol
    CPR7
    Official Full Name
    peptidylprolyl isomerase CPR7
    Primary source
    SGD:S000003793
    Locus tag
    YJR032W
    See related
    AllianceGenome:SGD:S000003793; FungiDB:YJR032W; VEuPathDB:YJR032W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables peptidyl-prolyl cis-trans isomerase activity and unfolded protein binding activity. Involved in protein refolding. Located in cytosol. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See CPR7 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (491081..492262)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Rbh2p Neighboring gene Arf family guanine nucleotide exchange factor GEA1 Neighboring gene Rav1p Neighboring gene Pet191p

    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. The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon. Zagulski M, et al. Yeast, 1995 Sep 30. PMID 8619316
    2. The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. Duina AA, et al. J Biol Chem, 1998 May 1. PMID 9556552
    3. The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase. Lin JY, et al. PLoS Pathog, 2012 Feb. PMID 22346747, Free PMC Article
    4. Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast. Miller CA. Cell Signal, 2002 Jul. PMID 11955954
    5. The crystal structure of the Hsp90 co-chaperone Cpr7 from Saccharomyces cerevisiae. Qiu Y, et al. J Struct Biol, 2017 Mar. PMID 28192191

    See all (84) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. We show that Cpr7 interacts with Ure2 and enhances its fibrillation. The requirement of Cpr7 is specific for [URE3] as its deletion does not antagonize both strong and weak variant of another yeast prion
      Title: Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.
    2. The Cyp40-like Cpr7p prolyl isomerase of yeast can effectively inhibit tombusvirus replication.
      Title: The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase.
    3. Neither Sti1 nor Cpr7 is necessary for prion propagation but the authors show that deletion of the STI1 and CPR7 genes leads to a significant reduction in the generation of [psi(-)] cells by Hsp104 overexpression.
      Title: Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation.
    Submit: New GeneRIF Correction

    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 RNA polymerase II CTD heptapeptide repeat P3 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables cyclosporin A binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables peptidyl-prolyl cis-trans isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables peptidyl-prolyl cis-trans isomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    peptidylprolyl isomerase CPR7
    NP_012566.1
    • Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants

    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
      491081..492262
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181690.1 → NP_012566.1  TPA: peptidylprolyl isomerase CPR7 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012566.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWK5, P47103, Q92323
      UniProtKB/TrEMBL
      A6ZPZ3, D3UF88, G2WH38, N1P019
      Conserved Domains (5) summary
      COG0457
      Location:233 → 383
      TPR; Tetratricopeptide (TPR) repeat [General function prediction only]
      sd00006
      Location:274 → 321
      TPR; TPR repeat [structural motif]
      pfam00515
      Location:330 → 363
      TPR_1; Tetratricopeptide repeat
      pfam13432
      Location:296 → 353
      TPR_16; Tetratricopeptide repeat
      cl00197
      Location:5 → 195
      cyclophilin; cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P47103.1

    Gene LinkOut

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