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    FPR1 peptidylprolyl isomerase FPR1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855587, updated on 2-Nov-2024

    Summary

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    Official Symbol
    FPR1
    Official Full Name
    peptidylprolyl isomerase FPR1
    Primary source
    SGD:S000005079
    Locus tag
    YNL135C
    See related
    AllianceGenome:SGD:S000005079; FungiDB:YNL135C; VEuPathDB:YNL135C
    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
    FKB1; RBP1
    Summary
    Enables several functions, including DNA-binding transcription activator activity, RNA polymerase II-specific; macrolide binding activity; and peptidyl-prolyl cis-trans isomerase activity. Involved in several processes, including RNA metabolic process; regulation of chaperone-mediated protein folding; and regulation of homoserine biosynthetic process. Located in mitochondrion and nucleus. Is active in cytoplasm. Human ortholog(s) of this gene implicated in Graves' disease. Orthologous to human FKBP1A (FKBP prolyl isomerase 1A); FKBP1B (FKBP prolyl isomerase 1B); and FKBP1C (FKBP prolyl isomerase family member 1C). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See FPR1 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (371882..372226, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene mitochondrial 37S ribosomal protein NAM9 Neighboring gene Eaf7p Neighboring gene uncharacterized protein Neighboring gene Fyv6p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis. Rotonda J, et al. J Biol Chem, 1993 Apr 15. PMID 7681823
    2. Screening of small molecule interactor library by using in-cell NMR spectroscopy (SMILI-NMR). Xie J, et al. J Med Chem, 2009 Jun 11. PMID 19422228, Free PMC Article
    3. Cloning and sequence analysis of a rapamycin-binding protein-encoding gene (RBP1) from Candida albicans. Ferrara A, et al. Gene, 1992 Apr 1. PMID 1563628
    4. FKB1 encodes a nonessential FK 506-binding protein in Saccharomyces cerevisiae and contains regions suggesting homology to the cyclophilins. Wiederrecht G, et al. Proc Natl Acad Sci U S A, 1991 Feb 1. PMID 1704127, Free PMC Article
    5. FPR1 is essential for rapamycin-induced lifespan extension in Saccharomyces cerevisiae. Yalcin G, et al. Biochem Biophys Res Commun, 2023 Apr 23. PMID 36857903

    See all (138) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. FPR1 is essential for rapamycin-induced lifespan extension in Saccharomyces cerevisiae.
      Title: FPR1 is essential for rapamycin-induced lifespan extension in Saccharomyces cerevisiae.
    2. Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.
      Title: Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.
    3. Physiological function of FKBP12, a primary target of rapamycin/FK506: a newly identified role in transcription of ribosomal protein genes in yeast.
      Title: Physiological function of FKBP12, a primary target of rapamycin/FK506: a newly identified role in transcription of ribosomal protein genes in yeast.
    4. Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiae.
      Title: Fpr1, a primary target of rapamycin, functions as a transcription factor for ribosomal protein genes cooperatively with Hmo1 in Saccharomyces cerevisiae.
    5. mutation or inhibition of FKBP12 dysregulates the homoserine synthetic pathway by perturbing aspartokinase feedback inhibition by threonine
      Title: FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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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

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables DNA-binding transcription activator activity, RNA polymerase II-specific IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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
    		  
    enables protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein folding chaperone IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chromatin organization IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in nonfunctional rRNA decay IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in positive regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of homoserine biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in transcription by RNA polymerase II IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 

    General protein information

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    Preferred Names
    peptidylprolyl isomerase FPR1
    NP_014264.1
    • Peptidyl-prolyl cis-trans isomerase (PPIase); binds to FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; associates with promoters of ribosomal protein genes; acts as chaperone to prevent protein aggregation; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A

    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_001146.8 Reference assembly

      Range
      371882..372226 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182973.1 → NP_014264.1  TPA: peptidylprolyl isomerase FPR1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014264.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W147, P20081
      UniProtKB/TrEMBL
      A6ZRU8, B3LNZ2, C7GKB2, C8ZG95, G2WLX1, N1NZB8
      Conserved Domains (1) summary
      COG0545
      Location:1 → 114
      FkpA; FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P20081.2

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