ID   QDR3_YEAST              Reviewed;         689 AA.
AC   P38227; D6VQ43;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Quinidine resistance protein 3;
DE   AltName: Full=Acids quinidine resistance protein 2;
GN   Name=QDR3; Synonyms=AQR2; OrderedLocusNames=YBR043C; ORFNames=YBR0413;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 37.
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   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   [4]
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15649438; DOI=10.1016/j.bbrc.2004.12.097;
RA   Tenreiro S., Vargas R.C., Teixeira M.C., Magnani C., Sa-Correia I.;
RT   "The yeast multidrug transporter Qdr3 (Ybr043c): localization and role as a
RT   determinant of resistance to quinidine, barban, cisplatin, and bleomycin.";
RL   Biochem. Biophys. Res. Commun. 327:952-959(2005).
RN   [6]
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   [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-436, AND IDENTIFICATION BY
RP   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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). {ECO:0000269|PubMed:15649438}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15649438}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15649438}.
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z35912; CAA84985.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07163.2; -; Genomic_DNA.
DR   PIR; S45901; S45901.
DR   RefSeq; NP_009599.2; NM_001178391.2.
DR   AlphaFoldDB; P38227; -.
DR   BioGRID; 32744; 70.
DR   DIP; DIP-797N; -.
DR   IntAct; P38227; 3.
DR   MINT; P38227; -.
DR   STRING; 4932.YBR043C; -.
DR   TCDB; 2.A.1.2.43; the major facilitator superfamily (mfs).
DR   iPTMnet; P38227; -.
DR   MaxQB; P38227; -.
DR   PaxDb; 4932-YBR043C; -.
DR   PeptideAtlas; P38227; -.
DR   EnsemblFungi; YBR043C_mRNA; YBR043C; YBR043C.
DR   GeneID; 852331; -.
DR   KEGG; sce:YBR043C; -.
DR   AGR; SGD:S000000247; -.
DR   SGD; S000000247; QDR3.
DR   VEuPathDB; FungiDB:YBR043C; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_008455_8_5_1; -.
DR   InParanoid; P38227; -.
DR   OMA; IFSMATT; -.
DR   OrthoDB; 1510279at2759; -.
DR   BioCyc; YEAST:G3O-29016-MONOMER; -.
DR   BioGRID-ORCS; 852331; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P38227; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38227; 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:0015203; F:polyamine transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0030476; P:ascospore wall assembly; IGI:SGD.
DR   GO; GO:0010509; P:intracellular polyamine homeostasis; IMP: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   Gene3D; 1.20.1720.10; Multidrug resistance protein D; 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:SF5; QUINIDINE RESISTANCE PROTEIN 3; 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; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..689
FT                   /note="Quinidine resistance protein 3"
FT                   /id="PRO_0000173437"
FT   TOPO_DOM        1..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..265
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..475
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..510
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        511..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        533..558
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        559..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        578..586
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        610..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..648
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        649..668
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        669..689
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        37
FT                   /note="S -> T (in Ref. 1; CAA84985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   689 AA;  77287 MW;  AA2C5D2D7175F176 CRC64;
     MQAQGSQSNV GSLRSNCSDN SLPNNHVMMH CDESSGSPHS EHNDYSYEKT NLESTASNSR
     EHRDNQLSRL KSEEYVVPKN QRRGLLPQLA IIPEFKDARD YPPMMKKMIV FLIAFSSMMG
     PMGTSIIFPA INSITTEFKT SVIMVNVSIG VYLLSLGVFP LWWSSLSELE GRRTTYITSF
     ALLFAFNIGS ALAPDINSFI ALRMLCGAAS ASVQSVGAGT VADLYISEDR GKNLSYYYLG
     PLLAPLLSPI FGSLLVNRWP WRSTQWFMVI LSGCNVILLT VLLPETLRKQ DSKGAIAQIL
     AERRIQVDNN ERGEIQEDYQ RGEDETDRIE NQVATLSTEK HNYVGEVRDQ DSLDLESHSS
     PNTYDGRAGE TQLQRIYTEA SRSLYEYQLD DSGIDATTAQ VTRIRSTDPK LARSIRENSL
     RKLQTNLEEQ VKKVLSSNGG EIAPKQVSAV RKVWDTFFVY FIKPLKSLHF LEYPPVALAI
     TFSAISFSTV YFVNMTVEYK YSRPPYNFKP LYIGLLYIPN SVTYFFASIY GGRWVDMLLK
     RYKEKYGILA PEARISWNVV TSVISFPIAL LIFGWCLDKK CHWVTPLIGT ALFGYAAMMT
     IGATLSYLVD SLPGKGATGV ALNNLIRQIL AATAVFVTTP MLNGMGTGWA FTMLAFIVLG
     ASSVLIILKK HGDYWRENYD LQKLYDKID
//