ID QDR1_YEAST Reviewed; 563 AA. AC P40475; D6VVG7; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 28-JAN-2026, entry version 151. DE RecName: Full=Quinidine resistance protein 1; GN Name=QDR1; OrderedLocusNames=YIL120W; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; DOI=10.1038/387s084; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [2] 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 [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11302822; DOI=10.1128/aac.45.5.1528-1534.2001; RA Nunes P.A., Tenreiro S., Sa-Correia I.; RT "Resistance and adaptation to quinidine in Saccharomyces cerevisiae: role RT of QDR1 (YIL120w), encoding a plasma membrane transporter of the major RT facilitator superfamily required for multidrug resistance."; RL Antimicrob. Agents Chemother. 45:1528-1534(2001). RN [4] RP TOPOLOGY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 208353 / W303-1A; RX PubMed=16847258; DOI=10.1073/pnas.0604075103; RA Kim H., Melen K., Oesterberg M., von Heijne G.; RT "A global topology map of the Saccharomyces cerevisiae membrane proteome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006). CC -!- FUNCTION: Multidrug resistance transporter involved in resistance and CC adaptation to quinidine and ketoconazole. CC {ECO:0000269|PubMed:11302822}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11302822}; CC Multi-pass membrane protein {ECO:0000269|PubMed:11302822}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family. CC {ECO:0000305}. 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; Z46833; CAA86872.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08433.1; -; Genomic_DNA. DR PIR; S49889; S49889. DR RefSeq; NP_012146.1; NM_001179468.1. DR AlphaFoldDB; P40475; -. DR SMR; P40475; -. DR BioGRID; 34871; 39. DR DIP; DIP-8146N; -. DR FunCoup; P40475; 45. DR IntAct; P40475; 1. DR STRING; 4932.YIL120W; -. DR PaxDb; 4932-YIL120W; -. DR EnsemblFungi; YIL120W_mRNA; YIL120W; YIL120W. DR GeneID; 854686; -. DR KEGG; sce:YIL120W; -. DR AGR; SGD:S000001382; -. DR SGD; S000001382; QDR1. DR VEuPathDB; FungiDB:YIL120W; -. DR eggNOG; KOG0255; Eukaryota. DR HOGENOM; CLU_008455_8_4_1; -. DR InParanoid; P40475; -. DR OMA; DIHPGKA; -. DR OrthoDB; 440553at2759; -. DR BioCyc; YEAST:G3O-31373-MONOMER; -. DR BioGRID-ORCS; 854686; 0 hits in 10 CRISPR screens. DR PRO; PR:P40475; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P40475; protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:SGD. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0030476; P:ascospore wall assembly; IGI:SGD. DR GO; GO:0055085; P:transmembrane transport; IMP:SGD. DR CDD; cd17323; MFS_Tpo1_MDR_like; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR23502; MAJOR FACILITATOR SUPERFAMILY; 1. DR PANTHER; PTHR23502:SF51; QUINIDINE RESISTANCE PROTEIN 1-RELATED; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW Cell membrane; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..563 FT /note="Quinidine resistance protein 1" FT /id="PRO_0000173441" FT TOPO_DOM 1..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 76..96 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 97..108 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 130..135 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 136..156 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 157..165 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 166..186 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 187..195 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 217..224 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 246..296 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 297..317 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 318..341 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 342..362 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 363..421 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 422..442 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 443..445 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 446..466 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 467..481 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 482..502 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 503..511 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 512..532 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 533..563 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..10 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 23..33 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..49 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 563 AA; 61759 MW; 5FDBA6F9F7C71C72 CRC64; MTKQQTSVMR NASIAKEERE GSDNNNVDRS SSDAISDNDA ERSNSHSEID NESNFDMVPY SRFSHKQKML LVVQCAFTGF FSTVAGSIYY PVLTIIERKF NITEELANVT IVVYFIFQGV APSIMGGLAD TFGRRPIVLW AILAYFCACI GLACAHNYAQ ILALRCLQAA GISPVIAINS GIMGDVTTKV ERGGYVGLVA GFQVVGTAFG ALIGAGLSSK WGWRAIFWFL AIGSGICLVF STLLMPETKR TLVGNGSVTP RSFLNRSLIL HVGSVKKTLH LDDPDPETLE PRTSVDFLAP LKILHIREID ILLSIAGLQF STWTTHQTAL TIVLSKKYNL SVAKIGLCFL PAGISTLTSI ISAGRYLNWS YRTRKVKYNR WIKEQELQLM EKYKGDKNKV AELIHSNSHY AFNLVEARLH PAFVTLLLSS IGFTAFGWCI SVKTPLAAVL CTSAFASLFS NCILTFSTTL IVDLFPSKAS TATGCLNLFR CLLSAIFIAA LTKMVEKMRY GGVFTFLSAI TSSSSLLLFY LLKNGKQLSF DRIRANDKSA GRSVGKNSEK VST //