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    CPR3 peptidylprolyl isomerase CPR3 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854897, updated on 9-Dec-2024

    Summary

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    Official Symbol
    CPR3
    Official Full Name
    peptidylprolyl isomerase CPR3
    Primary source
    SGD:S000004543
    Locus tag
    YML078W
    See related
    AllianceGenome:SGD:S000004543; FungiDB:YML078W; VEuPathDB:YML078W
    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
    CYP3
    Summary
    Enables peptidyl-prolyl cis-trans isomerase activity. Involved in apoptotic process and protein folding. Located in mitochondrion. Human ortholog(s) of this gene implicated in cholangiocarcinoma and human immunodeficiency virus infectious disease. Orthologous to human PPIA (peptidylprolyl isomerase A). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See CPR3 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (111002..111550)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene tRNA dihydrouridine synthase Neighboring gene Cff1p Neighboring gene TRAPP subunit BET5 Neighboring gene War1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Cyclophilin catalyzes protein folding in yeast mitochondria. Matouschek A, et al. Proc Natl Acad Sci U S A, 1995 Jul 3. PMID 7603990, Free PMC Article
    2. Cyclophilin-promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme. von Ahsen O, et al. J Mol Biol, 2000 Mar 31. PMID 10731431
    3. Unfolding of CPR3 Gets Initiated at the Active Site and Proceeds via Two Intermediates. Shukla VK, et al. Biophys J, 2017 Feb 28. PMID 28256221, Free PMC Article
    4. R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. Scholz C, et al. FEBS Lett, 1999 Jan 29. PMID 10025965
    5. The yeast cyclophilin multigene family: purification, cloning and characterization of a new isoform. McLaughlin MM, et al. Gene, 1992 Feb 1. PMID 1547957

    See all (49) 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 apoptotic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 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
    		  
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    peptidylprolyl isomerase CPR3
    NP_013633.1
    • Mitochondrial peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; involved in protein refolding after import into mitochondria

    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_001145.3 Reference assembly

      Range
      111002..111550
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182437.1 → NP_013633.1  TPA: peptidylprolyl isomerase CPR3 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013633.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0K5, P25719
      UniProtKB/TrEMBL
      A6ZLY7, B3LLH8, B5VP51, C7GW13, C8ZEC7, G2WJX7, N1NXV9
      Conserved Domains (1) summary
      cd01926
      Location:23 → 180
      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 ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P25719.1

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