PDR17_YEAST
ID PDR17_YEAST Reviewed; 350 AA.
AC P53844; D6W0S9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphatidylinositol transfer protein PDR17;
DE Short=PITP;
DE AltName: Full=Phosphatidylserine transport B pathway protein 2;
DE AltName: Full=Pleiotropic drug resistance protein 17;
DE AltName: Full=SEC14 homolog 3;
GN Name=PDR17; Synonyms=ISS1, PSTB2, SFH4; OrderedLocusNames=YNL264C;
GN ORFNames=N0815;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=9890948; DOI=10.1074/jbc.274.4.1934;
RA van den Hazel H.B., Pichler H., do Valle Matta M.A., Leitner E.,
RA Goffeau A., Daum G.;
RT "PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect
RT lipid biosynthesis and resistance to multiple drugs.";
RL J. Biol. Chem. 274:1934-1941(1999).
RN [6]
RP FUNCTION.
RX PubMed=10799527; DOI=10.1074/jbc.275.19.14446;
RA Wu W.-I., Routt S.M., Bankaitis V.A., Voelker D.R.;
RT "A new gene involved in the transport-dependent metabolism of
RT phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene
RT encoding the phosphatidylinositol/phosphatidylcholine transfer protein,
RT SEC14.";
RL J. Biol. Chem. 275:14446-14456(2000).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10848624; DOI=10.1091/mbc.11.6.1989;
RA Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M.,
RA Kirsch D.R., Bankaitis V.A.;
RT "Identification of a novel family of nonclassic yeast phosphatidylinositol
RT transfer proteins whose function modulates phospholipase D activity and
RT Sec14p-independent cell growth.";
RL Mol. Biol. Cell 11:1989-2005(2000).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12869188; DOI=10.1046/j.1432-1033.2003.03688.x;
RA Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M.,
RA Kohlwein S.D., Paltauf F., Daum G., Griac P.;
RT "Subcellular localization of yeast Sec14 homologues and their involvement
RT in regulation of phospholipid turnover.";
RL Eur. J. Biochem. 270:3133-3145(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH PSD2.
RX PubMed=20016005; DOI=10.1091/mbc.e09-06-0519;
RA Gulshan K., Shahi P., Moye-Rowley W.S.;
RT "Compartment-specific synthesis of phosphatidylethanolamine is required for
RT normal heavy metal resistance.";
RL Mol. Biol. Cell 21:443-455(2010).
CC -!- FUNCTION: Has phosphatidylinositol transfer activity. Involved in the
CC regulation of the phospholipid composition of plasma- and
CC endomembranes. Altering plasma membrane composition may provide a
CC possible mechanism for multidrug resistance. Contributes to efficient
CC phospholipase D1 activation and phospholipase B1 inhibition in the
CC regulation of phospholipid turnover. Forms a complex with
CC phosphatidylserine decarboxylase PSD2 that seems essential for
CC maintenance of vacuolar phosphatidylethanolamine (PE) levels
CC (PubMed:20016005). {ECO:0000269|PubMed:10799527,
CC ECO:0000269|PubMed:10848624, ECO:0000269|PubMed:20016005,
CC ECO:0000269|PubMed:9890948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000269|PubMed:10848624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000269|PubMed:10848624};
CC -!- SUBUNIT: Interacts with phosphatidylserine decarboxylase PSD2.
CC {ECO:0000269|PubMed:20016005}.
CC -!- INTERACTION:
CC P53844; P53037: PSD2; NbExp=3; IntAct=EBI-2076838, EBI-14018;
CC P53844; Q08984: YPL272C; NbExp=4; IntAct=EBI-2076838, EBI-3719178;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12869188,
CC ECO:0000269|PubMed:14562095}. Microsome {ECO:0000269|PubMed:12869188}.
CC -!- MISCELLANEOUS: Present with 5040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X92494; CAA63233.1; -; Genomic_DNA.
DR EMBL; Z71540; CAA96171.1; -; Genomic_DNA.
DR EMBL; AY692928; AAT92947.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10295.1; -; Genomic_DNA.
DR PIR; S60917; S60917.
DR RefSeq; NP_014135.1; NM_001183102.1.
DR AlphaFoldDB; P53844; -.
DR SMR; P53844; -.
DR BioGRID; 35575; 88.
DR ComplexPortal; CPX-1319; PSTB lipid transfer acceptor membrane complex.
DR DIP; DIP-2580N; -.
DR IntAct; P53844; 3.
DR MINT; P53844; -.
DR STRING; 4932.YNL264C; -.
DR SwissLipids; SLP:000000357; -.
DR iPTMnet; P53844; -.
DR MaxQB; P53844; -.
DR PaxDb; P53844; -.
DR PRIDE; P53844; -.
DR EnsemblFungi; YNL264C_mRNA; YNL264C; YNL264C.
DR GeneID; 855457; -.
DR KEGG; sce:YNL264C; -.
DR SGD; S000005208; PDR17.
DR VEuPathDB; FungiDB:YNL264C; -.
DR eggNOG; KOG1470; Eukaryota.
DR GeneTree; ENSGT00940000176626; -.
DR HOGENOM; CLU_014001_1_1_1; -.
DR InParanoid; P53844; -.
DR OMA; RPLFYMK; -.
DR BioCyc; YEAST:G3O-33260-MON; -.
DR PRO; PR:P53844; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53844; protein.
DR GO; GO:0071944; C:cell periphery; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IDA:ComplexPortal.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:SGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:SGD.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IC:ComplexPortal.
DR GO; GO:1901352; P:negative regulation of phosphatidylglycerol biosynthetic process; IGI:SGD.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:SGD.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IGI:SGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IGI:SGD.
DR GO; GO:0016126; P:sterol biosynthetic process; IGI:SGD.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Lipid transport; Microsome;
KW Reference proteome; Transport.
FT CHAIN 1..350
FT /note="Phosphatidylinositol transfer protein PDR17"
FT /id="PRO_0000210746"
FT DOMAIN 139..297
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
SQ SEQUENCE 350 AA; 40678 MW; C18F0D225A69DB86 CRC64;
MGLFSRKRDH TPAVPKEKLI PCDKIFLDPP AKYGNAPLLE PISEDQNEKY RAVLRHFQDD
DLKLPENLND LDNGTHANDR PLSDWEKFWL SRECFLRYLR ANKWNTANAI KGLTKTLVWR
REIGLTHGKE DKDPLTADKV AVENETGKQV ILGFDNAKRP LYYMKNGRQN TESSFRQVQE
LVYMMETATT VAPQGVEKIT VLVDFKSYKE PGIITDKAPP ISIARMCLNV MQDHYPERLA
KCVLINIPWF AWAFLKMMYP FLDPATKAKA IFDEPFENHI EPSQLDALYN GLLDFKYKHE
VYWPDMVKKV DDLRLKRFDR FLKFGGIVGL SEYDTKGQHD ELKYPVDMVI
