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P53860

- PDR16_YEAST

UniProt

P53860 - PDR16_YEAST

Protein

Phosphatidylinositol transfer protein PDR16

Gene

PDR16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover.2 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. phosphatidylinositol transporter activity Source: SGD

    GO - Biological processi

    1. negative regulation of sexual sporulation resulting in formation of a cellular spore Source: SGD
    2. phospholipid biosynthetic process Source: SGD
    3. phospholipid transport Source: SGD
    4. response to drug Source: SGD
    5. sterol biosynthetic process Source: SGD

    Keywords - Biological processi

    Lipid transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33231-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol transfer protein PDR16
    Short name:
    PITP
    Alternative name(s):
    Pleiotropic drug resistance protein 16
    SEC14 homolog 3
    Gene namesi
    Name:PDR16
    Synonyms:SFH3
    Ordered Locus Names:YNL231C
    ORF Names:N1158
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL231c.
    SGDiS000005175. PDR16.

    Subcellular locationi

    GO - Cellular componenti

    1. cell periphery Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. lipid particle Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Lipid droplet, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Phosphatidylinositol transfer protein PDR16PRO_0000210745Add
    BLAST

    Proteomic databases

    MaxQBiP53860.
    PaxDbiP53860.
    PeptideAtlasiP53860.

    Expressioni

    Gene expression databases

    GenevestigatoriP53860.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-29195,EBI-29195

    Protein-protein interaction databases

    BioGridi35607. 28 interactions.
    DIPiDIP-5449N.
    IntActiP53860. 2 interactions.
    MINTiMINT-539790.
    STRINGi4932.YNL231C.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 213
    Helixi42 – 5615
    Beta strandi61 – 644
    Beta strandi74 – 763
    Helixi79 – 846
    Helixi87 – 9610
    Helixi101 – 11818
    Helixi125 – 1273
    Helixi133 – 1364
    Helixi137 – 1404
    Beta strandi144 – 1507
    Beta strandi156 – 1605
    Helixi162 – 1643
    Helixi171 – 18616
    Beta strandi195 – 2006
    Helixi221 – 23111
    Beta strandi237 – 2448
    Helixi247 – 25610
    Helixi257 – 2593
    Helixi262 – 2654
    Beta strandi268 – 2725
    Helixi274 – 2763
    Helixi280 – 2823
    Helixi285 – 2873
    Beta strandi289 – 2935
    Helixi297 – 32125
    Helixi330 – 3334

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FMMX-ray2.34A/B1-351[»]
    4J7PX-ray2.00A/B2-351[»]
    4J7QX-ray1.55A/B15-345[»]
    ProteinModelPortaliP53860.
    SMRiP53860. Positions 16-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 295161CRAL-TRIOPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG242743.
    GeneTreeiENSGT00390000018675.
    HOGENOMiHOG000176881.
    OMAiNEACLVR.
    OrthoDBiEOG70PC7T.

    Family and domain databases

    Gene3Di3.40.525.10. 1 hit.
    InterProiIPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    [Graphical view]
    PfamiPF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view]
    SMARTiSM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view]
    SUPFAMiSSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEiPS50191. CRAL_TRIO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53860-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKRFSKKKE APEDPKNLIN IDKPIKELPA SIAIPKEKPL TGEQQKMYDE    50
    VLKHFSNPDL KVYTSEKNKS EDDLKPLEEE EKAWLTRECF LRYLRATKWV 100
    LKDCIDRITM TLAWRREFGI SHLGEEHGDK ITADLVAVEN ESGKQVILGY 150
    ENDARPILYL KPGRQNTKTS HRQVQHLVFM LERVIDFMPA GQDSLALLID 200
    FKDYPDVPKV PGNSKIPPIG VGKEVLHILQ THYPERLGKA LLTNIPWLAW 250
    TFLKLIHPFI DPLTREKLVF DEPFVKYVPK NELDSLYGGD LKFKYNHDVY 300
    WPALVETARE KRDHYFKRFQ SFGGIVGLSE VDLRGTHEKL LYPVKSESST 350
    V 351
    Length:351
    Mass (Da):40,714
    Last modified:October 1, 1996 - v1
    Checksum:i24C5B3262016F037
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z69381 Genomic DNA. Translation: CAA93367.1.
    Z71507 Genomic DNA. Translation: CAA96136.1.
    AY558020 Genomic DNA. Translation: AAS56346.1.
    BK006947 Genomic DNA. Translation: DAA10327.1.
    PIRiS63197.
    RefSeqiNP_014168.1. NM_001183069.1.

    Genome annotation databases

    EnsemblFungiiYNL231C; YNL231C; YNL231C.
    GeneIDi855490.
    KEGGisce:YNL231C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z69381 Genomic DNA. Translation: CAA93367.1 .
    Z71507 Genomic DNA. Translation: CAA96136.1 .
    AY558020 Genomic DNA. Translation: AAS56346.1 .
    BK006947 Genomic DNA. Translation: DAA10327.1 .
    PIRi S63197.
    RefSeqi NP_014168.1. NM_001183069.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FMM X-ray 2.34 A/B 1-351 [» ]
    4J7P X-ray 2.00 A/B 2-351 [» ]
    4J7Q X-ray 1.55 A/B 15-345 [» ]
    ProteinModelPortali P53860.
    SMRi P53860. Positions 16-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35607. 28 interactions.
    DIPi DIP-5449N.
    IntActi P53860. 2 interactions.
    MINTi MINT-539790.
    STRINGi 4932.YNL231C.

    Proteomic databases

    MaxQBi P53860.
    PaxDbi P53860.
    PeptideAtlasi P53860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL231C ; YNL231C ; YNL231C .
    GeneIDi 855490.
    KEGGi sce:YNL231C.

    Organism-specific databases

    CYGDi YNL231c.
    SGDi S000005175. PDR16.

    Phylogenomic databases

    eggNOGi NOG242743.
    GeneTreei ENSGT00390000018675.
    HOGENOMi HOG000176881.
    OMAi NEACLVR.
    OrthoDBi EOG70PC7T.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33231-MONOMER.

    Miscellaneous databases

    NextBioi 979472.

    Gene expression databases

    Genevestigatori P53860.

    Family and domain databases

    Gene3Di 3.40.525.10. 1 hit.
    InterProi IPR001251. CRAL-TRIO_dom.
    IPR011074. CRAL/TRIO_N_dom.
    [Graphical view ]
    Pfami PF00650. CRAL_TRIO. 1 hit.
    PF03765. CRAL_TRIO_N. 1 hit.
    [Graphical view ]
    SMARTi SM01100. CRAL_TRIO_N. 1 hit.
    SM00516. SEC14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46938. SSF46938. 1 hit.
    SSF52087. SSF52087. 1 hit.
    PROSITEi PS50191. CRAL_TRIO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
      Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
      Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Bienvenut W.V., Peters C.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 240-292 AND 319-334, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs."
      van den Hazel H.B., Pichler H., do Valle Matta M.A., Leitner E., Goffeau A., Daum G.
      J. Biol. Chem. 274:1934-1941(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth."
      Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M., Kirsch D.R., Bankaitis V.A.
      Mol. Biol. Cell 11:1989-2005(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover."
      Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M., Kohlwein S.D., Paltauf F., Daum G., Griac P.
      Eur. J. Biochem. 270:3133-3145(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDR16_YEAST
    AccessioniPrimary (citable) accession number: P53860
    Secondary accession number(s): D6W0W1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 15361 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3