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    CPR4 peptidylprolyl isomerase family protein CPR4 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850433, updated on 18-Sep-2024

    Summary

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    Official Symbol
    CPR4
    Official Full Name
    peptidylprolyl isomerase family protein CPR4
    Primary source
    SGD:S000000665
    Locus tag
    YCR069W
    See related
    AllianceGenome:SGD:S000000665; FungiDB:YCR069W; VEuPathDB:YCR069W
    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
    CYP4; SCC3; YCR070W
    Summary
    Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding and protein peptidyl-prolyl isomerization. Located in fungal-type vacuole. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See CPR4 in Genome Data Viewer
    Location:
    chromosome: III
    Exon count:
    1
    Sequence:
    Chromosome: III; NC_001135.5 (239055..240011)

    Chromosome III - NC_001135.5Genomic Context describing neighboring genes Neighboring gene GTPase-activating protein SED4 Neighboring gene triglyceride lipase ATG15 Neighboring gene mitochondrial 54S ribosomal protein IMG2 Neighboring gene Rsa4p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001135.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae. Franco L, et al. Yeast, 1991 Dec. PMID 1803821
    2. Chromosome loading of cohesin depends on conserved residues in Scc3. Pathania A, et al. Curr Genet, 2021 Jun. PMID 33404730
    3. Cohesin rings devoid of Scc3 and Pds5 maintain their stable association with the DNA. Kulemzina I, et al. PLoS Genet, 2012. PMID 22912589, Free PMC Article
    4. 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
    5. The complete DNA sequence of yeast chromosome III. Oliver SG, et al. Nature, 1992 May 7. PMID 1574125

    See all (19) 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 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 peptidyl-prolyl isomerization 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 fungal-type vacuole HDA PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    peptidylprolyl isomerase family protein CPR4
    NP_009995.1
    • Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, 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_001135.5 Reference assembly

      Range
      239055..240011
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178780.1 → NP_009995.1  TPA: peptidylprolyl isomerase family protein CPR4 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009995.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VR72, P25334, P25658
      UniProtKB/TrEMBL
      B3LUC7, B5VF01, G2WA79, N1P7W8
      Conserved Domains (1) summary
      cd00317
      Location:67 → 219
      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
    P25334.1

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