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Quinidine resistance protein 1

 QDR1_YEAST              Reviewed;         563 AA.
P40475; D6VVG7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
28-MAR-2018, entry version 117.
RecName: Full=Quinidine resistance protein 1;
Name=QDR1; OrderedLocusNames=YIL120W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11302822; DOI=10.1128/AAC.45.5.1528-1534.2001;
Nunes P.A., Tenreiro S., Sa-Correia I.;
"Resistance and adaptation to quinidine in Saccharomyces cerevisiae:
role of QDR1 (YIL120w), encoding a plasma membrane transporter of the
major facilitator superfamily required for multidrug resistance.";
Antimicrob. Agents Chemother. 45:1528-1534(2001).
[4]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
-!- FUNCTION: Multidrug resistance transporter involved in resistance
and adaptation to quinidine and ketoconazole.
{ECO:0000269|PubMed:11302822}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11302822};
Multi-pass membrane protein {ECO:0000269|PubMed:11302822}.
-!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z46833; CAA86872.1; -; Genomic_DNA.
EMBL; BK006942; DAA08433.1; -; Genomic_DNA.
PIR; S49889; S49889.
RefSeq; NP_012146.1; NM_001179468.1.
ProteinModelPortal; P40475; -.
BioGrid; 34871; 37.
DIP; DIP-8146N; -.
IntAct; P40475; 1.
STRING; 4932.YIL120W; -.
PaxDb; P40475; -.
PRIDE; P40475; -.
EnsemblFungi; YIL120W; YIL120W; YIL120W.
GeneID; 854686; -.
KEGG; sce:YIL120W; -.
EuPathDB; FungiDB:YIL120W; -.
SGD; S000001382; QDR1.
GeneTree; ENSGT00620000088227; -.
HOGENOM; HOG000248839; -.
InParanoid; P40475; -.
OMA; MIFQGIT; -.
OrthoDB; EOG092C19MN; -.
BioCyc; YEAST:G3O-31373-MONOMER; -.
PRO; PR:P40475; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:SGD.
GO; GO:0030476; P:ascospore wall assembly; IGI:SGD.
GO; GO:0006855; P:drug transmembrane transport; IMP:SGD.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 3.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 563 Quinidine resistance protein 1.
/FTId=PRO_0000173441.
TOPO_DOM 1 75 Cytoplasmic. {ECO:0000255}.
TRANSMEM 76 96 Helical. {ECO:0000255}.
TOPO_DOM 97 108 Extracellular. {ECO:0000255}.
TRANSMEM 109 129 Helical. {ECO:0000255}.
TOPO_DOM 130 135 Cytoplasmic. {ECO:0000255}.
TRANSMEM 136 156 Helical. {ECO:0000255}.
TOPO_DOM 157 165 Extracellular. {ECO:0000255}.
TRANSMEM 166 186 Helical. {ECO:0000255}.
TOPO_DOM 187 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 216 Helical. {ECO:0000255}.
TOPO_DOM 217 224 Extracellular. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
TOPO_DOM 246 296 Cytoplasmic. {ECO:0000255}.
TRANSMEM 297 317 Helical. {ECO:0000255}.
TOPO_DOM 318 341 Extracellular. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TOPO_DOM 363 421 Cytoplasmic. {ECO:0000255}.
TRANSMEM 422 442 Helical. {ECO:0000255}.
TOPO_DOM 443 445 Extracellular. {ECO:0000255}.
TRANSMEM 446 466 Helical. {ECO:0000255}.
TOPO_DOM 467 481 Cytoplasmic. {ECO:0000255}.
TRANSMEM 482 502 Helical. {ECO:0000255}.
TOPO_DOM 503 511 Extracellular. {ECO:0000255}.
TRANSMEM 512 532 Helical. {ECO:0000255}.
TOPO_DOM 533 563 Cytoplasmic. {ECO:0000255}.
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


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