PDR16_YEAST
ID PDR16_YEAST Reviewed; 351 AA.
AC P53860; D6W0W1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Phosphatidylinositol transfer protein PDR16;
DE Short=PITP;
DE AltName: Full=Pleiotropic drug resistance protein 16;
DE AltName: Full=SEC14 homolog 3;
GN Name=PDR16; Synonyms=SFH3; OrderedLocusNames=YNL231C; ORFNames=N1158;
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].
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(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 PROTEIN SEQUENCE OF 240-292 AND 319-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14] {ECO:0007744|PDB:4FMM}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS), AND SUBUNIT.
RX PubMed=23519406; DOI=10.1107/s0907444912046161;
RA Yuan Y., Zhao W., Wang X., Gao Y., Niu L., Teng M.;
RT "Dimeric Sfh3 has structural changes in its binding pocket that are
RT associated with a dimer-monomer state transformation induced by substrate
RT binding.";
RL Acta Crystallogr. D 69:313-323(2013).
RN [15] {ECO:0007744|PDB:4J7P, ECO:0007744|PDB:4J7Q}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 15-345, AND SUBUNIT.
RX PubMed=23603387; DOI=10.1016/j.febslet.2013.04.009;
RA Yang H., Tong J., Leonard T.A., Im Y.J.;
RT "Structural determinants for phosphatidylinositol recognition by Sfh3 and
RT substrate-induced dimer-monomer transition during lipid transfer cycles.";
RL FEBS Lett. 587:1610-1616(2013).
RN [16] {ECO:0007744|PDB:4M8Z}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24403601; DOI=10.1091/mbc.e13-11-0634;
RA Ren J., Pei-Chen Lin C., Pathak M.C., Temple B.R., Nile A.H., Mousley C.J.,
RA Duncan M.C., Eckert D.M., Leiker T.J., Ivanova P.T., Myers D.S.,
RA Murphy R.C., Brown H.A., Verdaasdonk J., Bloom K.S., Ortlund E.A.,
RA Neiman A.M., Bankaitis V.A.;
RT "A phosphatidylinositol transfer protein integrates phosphoinositide
RT signaling with lipid droplet metabolism to regulate a developmental program
RT of nutrient stress-induced membrane biogenesis.";
RL Mol. Biol. Cell 25:712-727(2014).
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. Involved in the regulation
CC of sterol biosynthesis. Contributes to efficient phospholipase D1
CC activation in the regulation of phospholipid turnover. Regulates the
CC release of fatty acids from lipid droplets (PubMed:24403601).
CC {ECO:0000269|PubMed:10848624, ECO:0000269|PubMed:24403601,
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: Homodimer (PubMed:23519406). Apo-SFH3 forms a dimer through
CC the hydrophobic interaction of gating helices. Binding of
CC phosphatidylinositol leads to dissociation of the dimer into monomers
CC in a reversible manner (PubMed:23603387). {ECO:0000269|PubMed:23519406,
CC ECO:0000269|PubMed:23603387}.
CC -!- INTERACTION:
CC P53860; P53860: PDR16; NbExp=2; IntAct=EBI-29195, EBI-29195;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:12869188,
CC ECO:0000269|PubMed:24403601}. Microsome membrane
CC {ECO:0000269|PubMed:12869188}; Peripheral membrane protein. Endoplasmic
CC reticulum membrane; Peripheral membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 15361 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z69381; CAA93367.1; -; Genomic_DNA.
DR EMBL; Z71507; CAA96136.1; -; Genomic_DNA.
DR EMBL; AY558020; AAS56346.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10327.1; -; Genomic_DNA.
DR PIR; S63197; S63197.
DR RefSeq; NP_014168.1; NM_001183069.1.
DR PDB; 4FMM; X-ray; 2.34 A; A/B=1-351.
DR PDB; 4J7P; X-ray; 2.00 A; A/B=2-351.
DR PDB; 4J7Q; X-ray; 1.55 A; A/B=15-345.
DR PDB; 4M8Z; X-ray; 1.93 A; A/B=1-351.
DR PDBsum; 4FMM; -.
DR PDBsum; 4J7P; -.
DR PDBsum; 4J7Q; -.
DR PDBsum; 4M8Z; -.
DR AlphaFoldDB; P53860; -.
DR SMR; P53860; -.
DR BioGRID; 35607; 41.
DR ComplexPortal; CPX-2148; Phosphatidylinositol transporter complex.
DR DIP; DIP-5449N; -.
DR IntAct; P53860; 2.
DR MINT; P53860; -.
DR STRING; 4932.YNL231C; -.
DR SwissLipids; SLP:000000356; -.
DR iPTMnet; P53860; -.
DR MaxQB; P53860; -.
DR PaxDb; P53860; -.
DR PRIDE; P53860; -.
DR EnsemblFungi; YNL231C_mRNA; YNL231C; YNL231C.
DR GeneID; 855490; -.
DR KEGG; sce:YNL231C; -.
DR SGD; S000005175; PDR16.
DR VEuPathDB; FungiDB:YNL231C; -.
DR eggNOG; KOG1470; Eukaryota.
DR GeneTree; ENSGT00940000176626; -.
DR HOGENOM; CLU_014001_1_1_1; -.
DR InParanoid; P53860; -.
DR OMA; DIHARPC; -.
DR BioCyc; YEAST:G3O-33231-MON; -.
DR PRO; PR:P53860; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53860; protein.
DR GO; GO:0071944; C:cell periphery; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:1902556; C:phosphatidylinositol transporter complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:SGD.
DR GO; GO:0032934; F:sterol binding; IDA:SGD.
DR GO; GO:0043942; P:negative regulation of sexual sporulation resulting in formation of a cellular spore; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA: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 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid droplet; Lipid transport; Membrane; Microsome; Reference proteome;
KW Transport.
FT CHAIN 1..351
FT /note="Phosphatidylinositol transfer protein PDR16"
FT /id="PRO_0000210745"
FT DOMAIN 135..295
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:4J7Q"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4M8Z"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4FMM"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4J7Q"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 297..321
FT /evidence="ECO:0007829|PDB:4J7Q"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:4J7Q"
SQ SEQUENCE 351 AA; 40714 MW; 24C5B3262016F037 CRC64;
MFKRFSKKKE APEDPKNLIN IDKPIKELPA SIAIPKEKPL TGEQQKMYDE VLKHFSNPDL
KVYTSEKNKS EDDLKPLEEE EKAWLTRECF LRYLRATKWV LKDCIDRITM TLAWRREFGI
SHLGEEHGDK ITADLVAVEN ESGKQVILGY ENDARPILYL KPGRQNTKTS HRQVQHLVFM
LERVIDFMPA GQDSLALLID FKDYPDVPKV PGNSKIPPIG VGKEVLHILQ THYPERLGKA
LLTNIPWLAW TFLKLIHPFI DPLTREKLVF DEPFVKYVPK NELDSLYGGD LKFKYNHDVY
WPALVETARE KRDHYFKRFQ SFGGIVGLSE VDLRGTHEKL LYPVKSESST V
