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    CPR8 peptidylprolyl isomerase family protein CPR8 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855762, updated on 28-Oct-2024

    Summary

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    Official Symbol
    CPR8
    Official Full Name
    peptidylprolyl isomerase family protein CPR8
    Primary source
    SGD:S000005311
    Locus tag
    YNR028W
    See related
    AllianceGenome:SGD:S000005311; FungiDB:YNR028W; VEuPathDB:YNR028W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in fungal-type vacuole. [provided by Alliance of Genome Resources, Oct 2024]
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    Genomic context

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    See CPR8 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (676177..677103)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Sar family guanine nucleotide exchange factor SEC12 Neighboring gene putative pyridoxal kinase BUD17 Neighboring gene GTP-dependent zinc transferase Neighboring gene dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. 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
    2. The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications. Philippsen P, et al. Nature, 1997 May 29. PMID 9169873
    3. ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Jain S, et al. Cell, 2016 Jan 28. PMID 26777405, Free PMC Article
    4. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. McClellan AJ, et al. Cell, 2007 Oct 5. PMID 17923092
    5. Interrogation of γ-tubulin alleles using high-resolution fitness measurements reveals a distinct cytoplasmic function in spindle alignment. Shulist K, et al. Sci Rep, 2017 Sep 12. PMID 28900268, Free PMC Article

    See all (18) 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 

    General protein information

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    Preferred Names
    peptidylprolyl isomerase family protein CPR8
    NP_014425.3
    • 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; CPR8 has a paralog, CPR4, 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_001146.8 Reference assembly

      Range
      676177..677103
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183205.3 → NP_014425.3  TPA: peptidylprolyl isomerase family protein CPR8 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014425.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W1K2, E9P900, P53728
      UniProtKB/TrEMBL
      G2WL84, N1NXR9
      Conserved Domains (1) summary
      cl00197
      Location:65 → 210
      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
    P53728.1

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