QDR2_YEAST
ID QDR2_YEAST Reviewed; 542 AA.
AC P40474; D6VVG6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Quinidine resistance protein 2;
GN Name=QDR2; OrderedLocusNames=YIL121W;
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;
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 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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15215105; DOI=10.1128/aac.48.7.2531-2537.2004;
RA Vargas R.C., Tenreiro S., Teixeira M.C., Fernandes A.R., Sa-Correia I.;
RT "Saccharomyces cerevisiae multidrug transporter Qdr2p (Yil121wp):
RT localization and function as a quinidine resistance determinant.";
RL Antimicrob. Agents Chemother. 48:2531-2537(2004).
RN [5]
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).
RN [6]
RP FUNCTION.
RX PubMed=17189489; DOI=10.1128/ec.00290-06;
RA Vargas R.C., Garcia-Salcedo R., Tenreiro S., Teixeira M.C., Fernandes A.R.,
RA Ramos J., Sa-Correia I.;
RT "Saccharomyces cerevisiae multidrug resistance transporter Qdr2 is
RT implicated in potassium uptake, providing a physiological advantage to
RT quinidine-stressed cells.";
RL Eukaryot. Cell 6:134-142(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-38 AND SER-40, AND
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).
CC -!- FUNCTION: Multidrug resistance transporter involved in resistance and
CC adaptation to quinidine and to the herbicide barban (4-chloro-2-butynyl
CC [3-chlorophenyl] carbamate). Implicated in potassium uptake.
CC {ECO:0000269|PubMed:15215105, ECO:0000269|PubMed:17189489}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15215105};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15215105}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; Z46833; CAA86871.1; -; Genomic_DNA.
DR EMBL; AY692735; AAT92754.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08432.1; -; Genomic_DNA.
DR PIR; S49888; S49888.
DR RefSeq; NP_012145.1; NM_001179469.1.
DR AlphaFoldDB; P40474; -.
DR BioGRID; 34870; 57.
DR DIP; DIP-5661N; -.
DR IntAct; P40474; 19.
DR MINT; P40474; -.
DR STRING; 4932.YIL121W; -.
DR TCDB; 2.A.1.2.31; the major facilitator superfamily (mfs).
DR iPTMnet; P40474; -.
DR MaxQB; P40474; -.
DR PaxDb; P40474; -.
DR PRIDE; P40474; -.
DR EnsemblFungi; YIL121W_mRNA; YIL121W; YIL121W.
DR GeneID; 854685; -.
DR KEGG; sce:YIL121W; -.
DR SGD; S000001383; QDR2.
DR VEuPathDB; FungiDB:YIL121W; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000176391; -.
DR HOGENOM; CLU_008455_8_4_1; -.
DR InParanoid; P40474; -.
DR OMA; MTANIYF; -.
DR BioCyc; YEAST:G3O-31374-MON; -.
DR PRO; PR:P40474; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40474; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IMP:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:SGD.
DR GO; GO:0060003; P:copper ion export; IMP:SGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="Quinidine resistance protein 2"
FT /id="PRO_0000173442"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 542 AA; 59618 MW; 96649B74E940F63E CRC64;
MAGATSSIIR ENDFEDELAE SMQSYNRETA DKLALTRTES VKPEPEITAP PHSRFSRSFK
TVLIAQCAFT GFFSTIAGAI YYPVLSVIER KFDIDEELVN VTVVVYFVFQ GLAPTFMGGF
ADSLGRRPVV LVAIVIYFGA CIGLACAQTY AQIIVLRCLQ AAGISPVIAI NSGIMGDVTT
RAERGGYVGY VAGFQVLGSA FGALIGAGLS SRWGWRAIFW FLAIGSGICF LASFLILPET
KRNISGNGSV TPKSYLNRAP ILVLPTVRKS LHLDNPDYET LELPTQLNLL APFKILKAYE
ICILMLVAGL QFAMYTTHLT ALSTALSKQY HLTVAKVGLC YLPSGICTLC SIVIAGRYLN
WNYRRRLKYY QNWLGKKRSK LLEEHDNDLN LVQRIIENDP KYTFNIFKAR LQPAFVTLLL
SSSGFCAYGW CITVKAPLAA VLCMSGFASL FSNCILTFST TLIVDLFPTK TSTATGCLNL
FRCILSAVFI AALSKMVEKM KFGGVFTFLG ALTSSSSILL FILLRKGKEL AFKRKKQELG
VN
