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 02-SEP-2026, entry version 185. 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%3c1071::aid-yea4%3e3.0.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; DOI=10.1038/387s093; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P53860; -. DR SMR; P53860; -. DR BioGRID; 35607; 83. DR ComplexPortal; CPX-2148; Phosphatidylinositol transporter complex. DR DIP; DIP-5449N; -. DR FunCoup; P53860; 178. DR IntAct; P53860; 35. DR MINT; P53860; -. DR STRING; 4932.YNL231C; -. DR SwissLipids; SLP:000000356; -. DR iPTMnet; P53860; -. DR PaxDb; 4932-YNL231C; -. DR PeptideAtlas; P53860; -. DR EnsemblFungi; YNL231C_mRNA; YNL231C; YNL231C. DR GeneID; 855490; -. DR KEGG; sce:YNL231C; -. DR AGR; SGD:S000005175; -. DR SGD; S000005175; PDR16. DR VEuPathDB; FungiDB:YNL231C; -. DR eggNOG; KOG1470; Eukaryota. DR HOGENOM; CLU_014001_1_1_1; -. DR InParanoid; P53860; -. DR OMA; DIHARPC; -. DR OrthoDB; 75724at2759; -. DR BioCyc; YEAST:G3O-33231-MONOMER; -. DR BioGRID-ORCS; 855490; 1 hit in 10 CRISPR screens. DR EvolutionaryTrace; P53860; -. 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 FunFam; 3.40.525.10:FF:000013; Phosphatidylinositol transfer protein PDR16; 1. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 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 InterPro; IPR052578; PI_Transfer_CRAL-TRIO. DR PANTHER; PTHR45824; GH16843P; 1. DR PANTHER; PTHR45824:SF29; GH16843P; 1. 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; SSF52087; CRAL/TRIO domain; 1. DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1. DR PROSITE; PS50191; CRAL_TRIO; 1. DR PDBsum; 4FMM; -. DR PDBsum; 4J7P; -. DR PDBsum; 4J7Q; -. DR PDBsum; 4M8Z; -. 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 33..40 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 208..210 FT /evidence="ECO:0007829|PDB:4J7P" 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 //