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    FPR4 peptidylprolyl isomerase FPR4 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851170, updated on 18-Sep-2024

    Summary

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    Official Symbol
    FPR4
    Official Full Name
    peptidylprolyl isomerase FPR4
    Primary source
    SGD:S000004441
    Locus tag
    YLR449W
    See related
    AllianceGenome:SGD:S000004441; FungiDB:YLR449W; VEuPathDB:YLR449W
    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 macrolide binding activity and peptidyl-prolyl cis-trans isomerase activity. Involved in histone peptidyl-prolyl isomerization; negative regulation of histone H3-K36 methylation; and nucleosome assembly. Located in nucleus. Colocalizes with chromatin. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See FPR4 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (1030834..1032012)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene H(+)-transporting V0 sector ATPase subunit d Neighboring gene ribosomal 60S subunit protein L6B Neighboring gene hydroxymethylglutaryl-CoA reductase (NADPH) HMG2 Neighboring gene leucine-responsive transcriptional regulator LEU3

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p. Monneau YR, et al. Biomol NMR Assign, 2012 Oct. PMID 21898050
    2. The FK506-binding protein, Fpr4, is an acidic histone chaperone. Xiao H, et al. FEBS Lett, 2006 Aug 7. PMID 16846601
    3. A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing. Kuzuhara T, et al. Nat Struct Mol Biol, 2004 Mar. PMID 14981505
    4. Basic surface features of nuclear FKBPs facilitate chromatin binding. Leung A, et al. Sci Rep, 2017 Jun 19. PMID 28630422, Free PMC Article
    5. Nuclear FKBPs, Fpr3 and Fpr4 affect genome-wide genes transcription. Park SK, et al. Mol Genet Genomics, 2014 Apr. PMID 24297734

    See all (83) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The results thus provide a further demonstration for the elusive role of Fpr3 and Fpr4 in histone chaperones.
      Title: Nuclear FKBPs, Fpr3 and Fpr4 affect genome-wide genes transcription.
    2. Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization.
      Title: Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization.
    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 macrolide binding IDA
    Inferred from Direct Assay
    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
    acts_upstream_of_or_within maintenance of rDNA IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in nucleosome assembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in chromatin IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in chromatin IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleolus HDA PubMed 
    is_active_in nucleolus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 FPR4
    NP_013554.3
    • Nuclear peptidyl-prolyl cis-trans isomerase (PPIase); impacts expression of multiple genes via its role in nucleosome assembly; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones; role in rDNA maintenance; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; contains a nucleoplasmin-like fold and can form pentamers

    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_001144.5 Reference assembly

      Range
      1030834..1032012
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182337.3 → NP_013554.3  TPA: peptidylprolyl isomerase FPR4 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013554.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZ83, Q06205
      UniProtKB/TrEMBL
      A7A1W8, B3RHV7, B5VNY5, C8ZE56, N1P7H6
      Conserved Domains (2) summary
      COG0545
      Location:275 → 392
      FkpA; FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]
      pfam17800
      Location:10 → 164
      NPL; Nucleoplasmin-like domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q06205.1

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