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CPR7 peptidylprolyl isomerase CPR7 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853489, updated on 18-Sep-2024

Summary

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Official Symbol
CPR7
Official Full Name
peptidylprolyl isomerase CPR7
Primary source
SGD:S000003793
Locus tag
YJR032W
See related
AllianceGenome:SGD:S000003793; FungiDB:YJR032W; VEuPathDB:YJR032W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables peptidyl-prolyl cis-trans isomerase activity and unfolded protein binding activity. Involved in cellular response to heat and protein refolding. Located in cytosol. Orthologous to human PPID (peptidylprolyl isomerase D). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See CPR7 in Genome Data Viewer
Location:
chromosome: X
Exon count:
1
Sequence:
Chromosome: X; NC_001142.9 (491081..492262)

Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Rbh2p Neighboring gene Arf family guanine nucleotide exchange factor GEA1 Neighboring gene Rav1p Neighboring gene Pet191p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase. Lin JY, et al. PLoS Pathog, 2012 Feb. PMID 22346747, Free PMC Article
  2. The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. Duina AA, et al. J Biol Chem, 1998 May 1. PMID 9556552
  3. The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon. Zagulski M, et al. Yeast, 1995 Sep 30. PMID 8619316
  4. The crystal structure of the Hsp90 co-chaperone Cpr7 from Saccharomyces cerevisiae. Qiu Y, et al. J Struct Biol, 2017 Mar. PMID 28192191
  5. Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast. Miller CA. Cell Signal, 2002 Jul. PMID 11955954

See all (80) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We show that Cpr7 interacts with Ure2 and enhances its fibrillation. The requirement of Cpr7 is specific for [URE3] as its deletion does not antagonize both strong and weak variant of another yeast prion
    Title: Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.
  2. The Cyp40-like Cpr7p prolyl isomerase of yeast can effectively inhibit tombusvirus replication.
    Title: The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase.
  3. Neither Sti1 nor Cpr7 is necessary for prion propagation but the authors show that deletion of the STI1 and CPR7 genes leads to a significant reduction in the generation of [psi(-)] cells by Hsp104 overexpression.
    Title: Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation.
Submit: New GeneRIF Correction

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 IDA
Inferred from Direct Assay
more info
 PubMed 
enables peptidyl-prolyl cis-trans isomerase activity IEA
Inferred from Electronic Annotation
more info
  
enables unfolded protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
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 protein peptidyl-prolyl isomerization IEA
Inferred from Electronic Annotation
more info
  
involved_in protein refolding IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

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Preferred Names
peptidylprolyl isomerase CPR7
NP_012566.1
  • Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants

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_001142.9 Reference assembly

    Range
    491081..492262
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181690.1 → NP_012566.1  TPA: peptidylprolyl isomerase CPR7 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012566.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VWK5, P47103, Q92323
    UniProtKB/TrEMBL
    A6ZPZ3, D3UF88, G2WH38, N1P019
    Conserved Domains (5) summary
    COG0457
    Location:233 → 383
    TPR; Tetratricopeptide (TPR) repeat [General function prediction only]
    sd00006
    Location:274 → 321
    TPR; TPR repeat [structural motif]
    pfam00515
    Location:330 → 363
    TPR_1; Tetratricopeptide repeat
    pfam13432
    Location:296 → 353
    TPR_16; Tetratricopeptide repeat
    cl00197
    Location:5 → 195
    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
P47103.1

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