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CPR3 peptidylprolyl isomerase CPR3 [ Saccharomyces cerevisiae S288C ]

Gene ID: 854897, updated on 4-Jan-2025

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, Jan 2025]
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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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