QDR3_YEAST
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 03-AUG-2022, entry version 156.
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}.
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; 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; 67.
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; P38227; -.
DR PRIDE; P38227; -.
DR EnsemblFungi; YBR043C_mRNA; YBR043C; YBR043C.
DR GeneID; 852331; -.
DR KEGG; sce:YBR043C; -.
DR SGD; S000000247; QDR3.
DR VEuPathDB; FungiDB:YBR043C; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_5_1; -.
DR InParanoid; P38227; -.
DR OMA; RENMWLA; -.
DR BioCyc; YEAST:G3O-29016-MON; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030476; P:ascospore wall assembly; IGI:SGD.
DR GO; GO:0010509; P:polyamine homeostasis; 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 Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 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
