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    CPR6 peptidylprolyl isomerase CPR6 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850914, updated on 28-Oct-2024

    Summary

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    Official Symbol
    CPR6
    Official Full Name
    peptidylprolyl isomerase CPR6
    Primary source
    SGD:S000004206
    Locus tag
    YLR216C
    See related
    AllianceGenome:SGD:S000004206; FungiDB:YLR216C; VEuPathDB:YLR216C
    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
    CYP40
    Summary
    Enables peptidyl-prolyl cis-trans isomerase activity; ribosome binding activity; and unfolded protein binding activity. Involved in protein refolding. Located in cytoplasm. Orthologous to human PPID (peptidylprolyl isomerase D). [provided by Alliance of Genome Resources, Oct 2024]
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    Genomic context

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    See CPR6 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (572096..573211, complement)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene ferric/cupric-chelate reductase Neighboring gene cell proliferation protein CDC123 Neighboring gene Coa4p Neighboring gene Msc3p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Warth R, et al. Biol Chem, 1997 May. PMID 9191025
    2. Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth. Duina AA, et al. Yeast, 1996 Aug. PMID 8873448
    3. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. Richter K, et al. J Biol Chem, 2003 Mar 21. PMID 12525481
    4. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. Richter K, et al. J Mol Biol, 2004 Oct 1. PMID 15364569
    5. Three-step chromatographic purification of Cpr6, a cyclophilin from Saccharomyces cerevisiae. Mayr C. J Chromatogr B Biomed Sci Appl, 2000 Jan 14. PMID 10681067

    See all (99) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Basic amino acids in the c-terminus of Cpr6 are required for ribosome interaction.
      Title: The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.
    2. Mutation or inhibition of Hsp90 resulted in decreased accumulation of Ura2, indicating it is an Hsp90 client. Cpr6 interacted with Ura2 in the absence of stable Cpr6-Hsp90 interaction, suggesting a direct interaction.
      Title: Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.
    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 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 ribosome binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein folding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in protein peptidyl-prolyl isomerization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in intracellular membrane-bounded organelle IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    peptidylprolyl isomerase CPR6
    NP_013317.1
    • Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress

    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_001144.5 Reference assembly

      Range
      572096..573211 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182103.1 → NP_013317.1  TPA: peptidylprolyl isomerase CPR6 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013317.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VYL7, P53691, Q6Q5K7
      UniProtKB/TrEMBL
      B3RHA5, C7GIU5, C8ZDI0, G2WJ46
      Conserved Domains (3) summary
      cd01926
      Location:4 → 173
      cyclophilin_ABH_like; Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding ...
      sd00006
      Location:219 → 264
      TPR; TPR repeat [structural motif]
      pfam00515
      Location:311 → 341
      TPR_1; Tetratricopeptide repeat
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53691.1

    Gene LinkOut

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