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CPR7 peptidylprolyl isomerase CPR7 [ Saccharomyces cerevisiae S288C ]

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

Summary

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

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

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

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

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_001181690.1NP_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:233383
    TPR; Tetratricopeptide (TPR) repeat [General function prediction only]
    sd00006
    Location:274321
    TPR; TPR repeat [structural motif]
    pfam00515
    Location:330363
    TPR_1; Tetratricopeptide repeat
    pfam13432
    Location:296353
    TPR_16; Tetratricopeptide repeat
    cl00197
    Location:5195
    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 ...