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    CPR2 peptidylprolyl isomerase CPR2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856454, updated on 9-Dec-2024

    Summary

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    Official Symbol
    CPR2
    Official Full Name
    peptidylprolyl isomerase CPR2
    Primary source
    SGD:S000001099
    Locus tag
    YHR057C
    See related
    AllianceGenome:SGD:S000001099; FungiDB:YHR057C; VEuPathDB:YHR057C
    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
    CYP2
    Summary
    Enables peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in fungal-type vacuole. 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 CPR2 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (218226..218843, complement)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene ncRNA Neighboring gene metallothionein CUP1-2 Neighboring gene Rsc30p Neighboring gene mediator complex subunit MED6 Neighboring gene mitochondrial 37S ribosomal protein FYV4

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001140.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A second cyclophilin-related gene in Saccharomyces cerevisiae. Koser PL, et al. Nucleic Acids Res, 1990 Mar 25. PMID 2183199, Free PMC Article
    2. Heterologous expression of a salinity and developmentally regulated rice cyclophilin gene (OsCyp2) in E. coli and S. cerevisiae confers tolerance towards multiple abiotic stresses. Kumari S, et al. Mol Biotechnol, 2009 Jun. PMID 19214808
    3. Overexpression, purification, and characterization of yeast cyclophilins A and B. Zydowsky LD, et al. Protein Sci, 1992 Aug. PMID 1304384, Free PMC Article
    4. A yeast cyclophilin gene essential for lactate metabolism at high temperature. Davis ES, et al. Proc Natl Acad Sci U S A, 1992 Dec 1. PMID 1454795, Free PMC Article
    5. Retarded protein folding of the human Z-type α₁-antitrypsin variant is suppressed by Cpr2p. Jung CH, et al. Biochem Biophys Res Commun, 2014 Feb 28. PMID 24502947

    See all (33) 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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    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
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in endoplasmic reticulum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in fungal-type vacuole HDA PubMed 

    General protein information

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    Preferred Names
    peptidylprolyl isomerase CPR2
    NP_011924.1
    • Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema

    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_001140.6 Reference assembly

      Range
      218226..218843 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179187.1 → NP_011924.1  TPA: peptidylprolyl isomerase CPR2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011924.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DL06, P23285
      UniProtKB/TrEMBL
      A6ZSW3, B3LSH6, C7GTX6, C8Z9J5, G2WFC9, N1P106
      Conserved Domains (1) summary
      cl00197
      Location:37 → 197
      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
    P23285.1

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