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CPR5 peptidylprolyl isomerase family protein CPR5 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851898, updated on 2-Nov-2024

Summary

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Official Symbol
CPR5
Official Full Name
peptidylprolyl isomerase family protein CPR5
Primary source
SGD:S000002712
Locus tag
YDR304C
See related
AllianceGenome:SGD:S000002712; FungiDB:YDR304C; VEuPathDB:YDR304C
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
CYP5
Summary
Predicted to enable cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Predicted to be involved in protein folding. Located in endoplasmic reticulum. 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, Nov 2024]
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Genomic context

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See CPR5 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (1071880..1072557, complement)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene mannose-ethanolamine phosphotransferase GPI11 Neighboring gene Rsc3p Neighboring gene bis(5'-adenosyl)-triphosphatase Neighboring gene Pfu1p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. Frigerio G, et al. J Mol Biol, 1993 Sep 5. PMID 8377189
  2. Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum. de Ruijter JC, et al. Microb Cell Fact, 2016 May 23. PMID 27216259, Free PMC Article
  3. Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: lipidome meets proteome. Grillitsch K, et al. Biochim Biophys Acta, 2011 Dec. PMID 21820081, Free PMC Article
  4. Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress. Igbaria A, et al. Proc Natl Acad Sci U S A, 2019 Jun 4. PMID 31101715, Free PMC Article
  5. 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

See all (34) 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 folding IEA
Inferred from Electronic Annotation
more info
  
involved_in protein peptidyl-prolyl isomerization IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum HDA PubMed 
is_active_in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in endoplasmic reticulum IDA
Inferred from Direct Assay
more info
 PubMed 
located_in endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
  
located_in endoplasmic reticulum lumen IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
peptidylprolyl isomerase family protein CPR5
NP_010590.3
  • Peptidyl-prolyl cis-trans isomerase (cyclophilin) of the ER; catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; transcriptionally induced in response to unfolded proteins in the ER; CPR5 has a paralog, CPR2, 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_001136.10 Reference assembly

    Range
    1071880..1072557 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180612.3 → NP_010590.3  TPA: peptidylprolyl isomerase family protein CPR5 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010590.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VST3, P35176
    UniProtKB/TrEMBL
    A6ZYQ2, B3LFZ2, B5VGI3, C7GQV4, C8Z5L5, G2WB42, N1P573
    Conserved Domains (1) summary
    cl00197
    Location:34 → 194
    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
P35176.1

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