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    CPR5 peptidylprolyl isomerase family protein CPR5 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851898, updated on 9-Dec-2024

    Summary

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    Official Symbol
    CPR5
    Official Full Name
    peptidylprolyl isomerase family protein CPR5
    Primary source
    SGD:S000002712
    Locus tag
    YDR304C
    See related
    AllianceGenome:SGD:S000002712; FungiDB:YDR304C; VEuPathDB:YDR304C
    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
    CYP5
    Summary
    Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in endoplasmic reticulum. Human ortholog(s) of this gene implicated in osteogenesis imperfecta type 9. Orthologous to human PPIB (peptidylprolyl isomerase B) and PPIC (peptidylprolyl isomerase C). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See CPR5 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1071880..1072557, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene mannose-ethanolamine phosphotransferase GPI11 Neighboring gene Rsc3p Neighboring gene bis(5'-adenosyl)-triphosphatase Neighboring gene Pfu1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. Frigerio G, et al. J Mol Biol, 1993 Sep 5. PMID 8377189
    2. Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum. de Ruijter JC, et al. Microb Cell Fact, 2016 May 23. PMID 27216259, Free PMC Article
    3. Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: lipidome meets proteome. Grillitsch K, et al. Biochim Biophys Acta, 2011 Dec. PMID 21820081, Free PMC Article
    4. Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress. Igbaria A, et al. Proc Natl Acad Sci U S A, 2019 Jun 4. PMID 31101715, Free PMC Article
    5. All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Dolinski K, et al. Proc Natl Acad Sci U S A, 1997 Nov 25. PMID 9371805, Free PMC Article

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidyl-prolyl cis-trans isomerase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in biological_process ND
    No biological Data available
    more info
    		  
    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 regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum HDA PubMed 
    is_active_in endoplasmic reticulum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum lumen IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    peptidylprolyl isomerase family protein CPR5
    NP_010590.3
    • Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, that arose from the whole genome duplication

    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_001136.10 Reference assembly

      Range
      1071880..1072557 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180612.3 → NP_010590.3  TPA: peptidylprolyl isomerase family protein CPR5 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010590.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VST3, P35176
      UniProtKB/TrEMBL
      A6ZYQ2, B3LFZ2, B5VGI3, C7GQV4, C8Z5L5, G2WB42, N1P573
      Conserved Domains (1) summary
      cl00197
      Location:34 → 194
      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
    P35176.1

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