CPR1 peptidylprolyl isomerase CPR1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CPR1
Official Full Name: peptidylprolyl isomerase CPR1
Primary source: SGD:S000002562
Locus tag: YDR155C
See related: AllianceGenome:SGD:S000002562; FungiDB:YDR155C; VEuPathDB:YDR155C
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: CPH1; CYP1
Summary: Enables cyclosporin A binding activity and peptidyl-prolyl cis-trans isomerase activity. Involved in ascospore formation and positive regulation of meiotic nuclear division. Located in mitochondrial intermembrane space and nucleus. Part of Set3 complex. Human ortholog(s) of this gene implicated in cholangiocarcinoma and human immunodeficiency virus infectious disease. Orthologous to several human genes including PPIA (peptidylprolyl isomerase A). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
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Genomic context

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See CPR1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (768512..769000, complement)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

CypA binds to the Tomato bushy stunt tombusvirus RNA and replication proteins, resulting in inhibition of virus repication.
Title: Cyclophilin A binds to the viral RNA and replication proteins, resulting in inhibition of tombusviral replicase assembly.
protein overexpression enhances stress acquisition
Title: A cyclophilin A CPR1 overexpression enhances stress acquisition in Saccharomyces cerevisiae.
Cpr1 and Ess1 interact with the tombusvirus p33 and inhibit viral replication in yeast model host.
Title: Cpr1 cyclophilin and Ess1 parvulin prolyl isomerases interact with the tombusvirus replication protein and inhibit viral replication in yeast model host.
Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae
Title: Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.
activates Pseudomonas syringiae AvrRpt2
Title: Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables cyclosporin A binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables mRNA binding	HDA more info	PubMed
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 DNA damage response	NAS Non-traceable Author Statement more info	PubMed
involved_in ascospore formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to starvation	NAS Non-traceable Author Statement more info	PubMed
involved_in negative regulation of meiotic nuclear division	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of meiotic nuclear division	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of meiotic nuclear division	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	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of Set3 complex	IDA Inferred from Direct Assay more info	PubMed
part_of Set3 complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	EXP Inferred from Experiment more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in mitochondrial intermembrane space	EXP Inferred from Experiment more info	PubMed
located_in mitochondrial intermembrane space	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial intermembrane space	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: peptidylprolyl isomerase CPR1

NP_010439.1

EC 5.2.1.8

Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds the drug cyclosporin A; N-terminally propionylated in vivo; protein abundance increases in response to DNA replication stress

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

NC_001136.10 Reference assembly

Range

768512..769000 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180462.1 → NP_010439.1 peptidylprolyl isomerase CPR1

See identical proteins and their annotated locations for NP_010439.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VSD6, P14832

UniProtKB/TrEMBL

A6ZYB4, B3LGC8, B5VG49, C7GX36, C8Z570, G2WAQ4, N1P4U3

Conserved Domains (1) summary

cd01926
Location:2 → 160

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 ...