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    PDR17 phosphatidylinositol transporter [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855457, updated on 17-May-2024

    Summary

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    Gene symbol
    PDR17
    Gene description
    phosphatidylinositol transporter
    Primary source
    FungiDB:YNL264C
    Locus tag
    YNL264C
    See related
    SGD:S000005208; AllianceGenome:SGD:S000005208; VEuPathDB:YNL264C
    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
    ISS1; SFH4
    Summary
    Enables phosphatidylinositol transfer activity. Involved in several processes, including Golgi to plasma membrane protein transport; phospholipid metabolic process; and regulation of phospholipid biosynthetic process. Located in cell periphery; cytosol; and endosome. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See PDR17 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (145563..146615, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene 1-phosphatidylinositol 4-kinase Neighboring gene Ist1p Neighboring gene protein transporter YIF1 Neighboring gene DNA polymerase epsilon catalytic subunit

    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. A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/phosphatidylcholine transfer protein, SEC14. Wu WI, et al. J Biol Chem, 2000 May 12. PMID 10799527
    2. Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer the ergosterol precursor lanosterol in addition to phosphatidylinositol. Šťastný D, et al. FEBS Lett, 2023 Feb. PMID 36482167
    3. Phosphatidylserine-induced dissociation of the heterodimeric PstB2p/Pbi1p complex in yeast phosphatidylserine trafficking system. Cho HJ, et al. Biochem Biophys Res Commun, 2019 Sep 17. PMID 31351588
    4. Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function. Pevalová Z, et al. Biochim Biophys Acta Mol Cell Biol Lipids, 2019 Oct. PMID 31302248
    5. The yeast Saccharomyces cerevisiae Pdr16p restricts changes in ergosterol biosynthesis caused by the presence of azole antifungals. Šimová Z, et al. Yeast, 2013 Jun. PMID 23606207

    See all (41) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. PstB2p (PDR17) forms a homodimer but exists as a 1:1 heterodimer in the presence of Pbi1p. Phosphatidylserine binding to PstB2p triggers the dissociation of the PstB2p-Pbi1p complex.
      Title: Phosphatidylserine-induced dissociation of the heterodimeric PstB2p/Pbi1p complex in yeast phosphatidylserine trafficking system.
    2. Mutated phosphatidylinositol (PI) transfer protein Pdr17E237A, K269A is defective in high affinity PI binding. Pdr17p binds a sterol in addition to PI in an assay using permeabilized cells. PI binding defective Pdr17E237A, K269A retains the ability to transfer PI in vitro.
      Title: Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function.
    3. model predicts that this process involves an acceptor membrane complex containing the C2 domains of Psd2p, PstB2p, and Pbi1p that ligate to Scs2p and phosphatidic acid present in the donor membrane
      Title: An assembly of proteins and lipid domains regulates transport of phosphatidylserine to phosphatidylserine decarboxylase 2 in Saccharomyces cerevisiae.
    4. Overexpression of PDR17 complemented the azole susceptible phenotype of the pdr16Delta strain and corrected the enhanced sterol alterations in pdr16Delta cells in the presence of azoles.
      Title: The yeast Saccharomyces cerevisiae Pdr16p restricts changes in ergosterol biosynthesis caused by the presence of azole antifungals.
    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 
    Process Evidence Code Pubs
    involved_in Golgi to plasma membrane protein transport IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in lipid transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in negative regulation of phosphatidylglycerol biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in phosphatidylserine metabolic process 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 positive regulation of phosphatidylcholine biosynthetic process IGI
    Inferred from Genetic Interaction
    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 cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endosome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    phosphatidylinositol transporter
    NP_014135.1
    • Phosphatidylinositol transfer protein (PITP); downregulates Plb1p-mediated turnover of phosphatidylcholine; forms a complex with Psd2p which appears essential for maintenance of vacuolar PE levels; found in the cytosol and microsomes; homologous to Pdr16p; deletion affects phospholipid composition

    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
      145563..146615 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183102.1 → NP_014135.1  TPA: phosphatidylinositol transporter [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014135.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0S9, P53844
      UniProtKB/TrEMBL
      A0A6A5Q872, A6ZRH9, B3LPA4, B5VQE8, C7GP98, C8ZFX5, G2WLK1, N1NXZ0
      Conserved Domains (2) summary
      pfam00650
      Location:146 → 291
      CRAL_TRIO; CRAL/TRIO domain
      pfam03765
      Location:49 → 115
      CRAL_TRIO_N; CRAL/TRIO, N-terminal domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53844.1

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