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    PDR16 phosphatidylinositol transporter [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855490, updated on 27-Dec-2024

    Summary

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    Official Symbol
    PDR16
    Official Full Name
    phosphatidylinositol transporter
    Primary source
    SGD:S000005175
    Locus tag
    YNL231C
    See related
    AllianceGenome:SGD:S000005175; FungiDB:YNL231C; VEuPathDB:YNL231C
    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
    SFH3
    Summary
    Enables phosphatidylinositol transfer activity and sterol binding activity. Involved in several processes, including lipid biosynthetic process; negative regulation of sexual sporulation resulting in formation of a cellular spore; and phospholipid transport. Located in cell periphery; lipid droplet; and nucleus-vacuole junction. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See PDR16 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (215987..217042, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Bni4p Neighboring gene exosome non-catalytic core subunit CSL4 Neighboring gene elongin A Neighboring gene glutathione peroxidase

    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. Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles. Yang H, et al. FEBS Lett, 2013 Jun 5. PMID 23603387
    2. Phosphatidylinositol binding of Saccharomyces cerevisiae Pdr16p represents an essential feature of this lipid transfer protein to provide protection against azole antifungals. Holič R, et al. Biochim Biophys Acta, 2014 Oct. PMID 25066473, Free PMC Article
    3. Overexpression of PDR16 Confers Amphotericin B Resistance in a PMP3-Dependent Manner in Yeast Saccharomyces cerevisiae. Kalra S, et al. Microb Drug Resist, 2024 Jul. PMID 38727600
    4. Crystallization and preliminary X-ray diffraction analysis of Sfh3, a member of the Sec14 protein superfamily. Ren J, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011 Oct 1. PMID 22102037, Free PMC Article
    5. Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding. Yuan Y, et al. Acta Crystallogr D Biol Crystallogr, 2013 Mar. PMID 23519406

    See all (61) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Overexpression of a lipid-binding defective mutant of phosphatidylinositol transporter (PDR16) does not confer the resistance to aureobasidin A (AbA), indicating that the lipid-binding activity is essential for acquiring resistance to AbA. In AbA-treated cells, but not in cells in which AUR1 is repressed by the tetracycline-regulatable promoter, the reductions of complex sphingolipid levels are suppressed by the PDR16.
      Title: Overexpression of PDR16 confers resistance to complex sphingolipid biosynthesis inhibitor aureobasidin A in yeast Saccharomyces cerevisiae.
    2. The increased susceptibility to azoles, and enhanced changes in sterol biosynthesis upon exposure to azoles of the pdr16Delta strain compared to wt strain, are not the results of increased intracellular concentration of azoles in the pdr16Delta cells.
      Title: The yeast Saccharomyces cerevisiae Pdr16p restricts changes in ergosterol biosynthesis caused by the presence of azole antifungals.
    3. The dimeric structure of Sfh3 (Sec14 family homologue 3 in yeast) is reported for the first time and differs from the Sec14 proteins reported to date.
      Title: Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding.
    4. Substrate induced dimer-monomer transformation is an essential part of lipid transfer cycles by Sfh3.
      Title: Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles.
    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 phosphatidylinositol transfer activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables phosphatidylinositol transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphatidylinositol transfer activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables phosphatidylinositol transfer activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables sterol binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intermembrane lipid transfer IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in negative regulation of sexual sporulation resulting in formation of a cellular spore IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in phospholipid biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in phospholipid transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in phospholipid transport IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in phospholipid transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to xenobiotic stimulus IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in sterol biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cell periphery IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    located_in cytosol HDA PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in lipid droplet IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in lipid droplet IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus-vacuole junction IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane HDA PubMed 

    General protein information

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    Preferred Names
    phosphatidylinositol transporter
    NP_014168.1
    • Phosphatidylinositol transfer protein (PITP); controlled by the multiple drug resistance regulator Pdr1p; localizes to lipid particles and microsomes; controls levels of various lipids, may regulate lipid synthesis; homologous to Pdr17p; 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

    1. NC_001146.8 Reference assembly

      Range
      215987..217042 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183069.1 → NP_014168.1  TPA: phosphatidylinositol transporter [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014168.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0W1, P53860
      UniProtKB/TrEMBL
      A6ZRL1, B3LP72, B5VQH9, C7GPC8
      Conserved Domains (2) summary
      pfam00650
      Location:142 → 290
      CRAL_TRIO; CRAL/TRIO domain
      pfam03765
      Location:47 → 109
      CRAL_TRIO_N; CRAL/TRIO, N-terminal domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53860.1

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