PDR15_YEAST
ID PDR15_YEAST Reviewed; 1529 AA.
AC Q04182; D6VT38;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=ATP-dependent permease PDR15;
GN Name=PDR15; OrderedLocusNames=YDR406W; ORFNames=D9509.24;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 INDUCTION.
RX PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT "A general strategy to uncover transcription factor properties identifies a
RT new regulator of drug resistance in yeast.";
RL J. Biol. Chem. 278:11427-11432(2003).
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 -!- INTERACTION:
CC Q04182; P32901: PTR2; NbExp=2; IntAct=EBI-13072, EBI-20799497;
CC Q04182; P32804: ZRT1; NbExp=2; IntAct=EBI-13072, EBI-29677;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Transcriptionally regulated by PDR8.
CC {ECO:0000269|PubMed:12529331}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; U32274; AAB64846.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12248.1; -; Genomic_DNA.
DR PIR; S69688; S69688.
DR RefSeq; NP_010694.1; NM_001180714.1.
DR AlphaFoldDB; Q04182; -.
DR SMR; Q04182; -.
DR BioGRID; 32466; 51.
DR DIP; DIP-8040N; -.
DR IntAct; Q04182; 43.
DR MINT; Q04182; -.
DR STRING; 4932.YDR406W; -.
DR iPTMnet; Q04182; -.
DR MaxQB; Q04182; -.
DR PaxDb; Q04182; -.
DR PRIDE; Q04182; -.
DR EnsemblFungi; YDR406W_mRNA; YDR406W; YDR406W.
DR GeneID; 852015; -.
DR KEGG; sce:YDR406W; -.
DR SGD; S000002814; PDR15.
DR VEuPathDB; FungiDB:YDR406W; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176297; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q04182; -.
DR OMA; YYPVGFN; -.
DR BioCyc; YEAST:G3O-29950-MON; -.
DR PHI-base; PHI:2815; -.
DR PRO; PR:Q04182; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04182; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:SGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00956; 3a01205; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1529
FT /note="ATP-dependent permease PDR15"
FT /id="PRO_0000093446"
FT TOPO_DOM 1..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..642
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..783
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1241..1312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1313..1333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1334..1340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1341..1361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1362..1368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1369..1389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1390..1396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1397..1417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1418..1492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1493..1513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1514..1529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 171..420
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 884..1127
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 920..927
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1529 AA; 172256 MW; D5B58FB2E0534974 CRC64;
MSSDIRDVEE RNSRSSSSSS SSNSAAQSIG QHPYRGFDSE AAERVHELAR TLTSQSLLYT
ANSNNSSSSN HNAHNADSRS VFSTDMEGVN PVFTNPDTPG YNPKLDPNSD QFSSTAWVQN
MANICTSDPD FYKPYSLGCV WKNLSASGDS ADVSYQSTFA NIVPKLLTKG LRLLKPSKEE
DTFQILKPMD GCLNPGELLV VLGRPGSGCT TLLKSISSNS HGFKIAKDSI VSYNGLSSSD
IRKHYRGEVV YNAESDIHLP HLTVYQTLFT VARMKTPQNR IKGVDREAYA NHVTEVAMAT
YGLSHTRDTK VGNDLVRGVS GGERKRVSIA EVAICGARFQ CWDNATRGLD SATALEFIRA
LKTQADIGKT AATVAIYQCS QDAYDLFDKV CVLDDGYQLY FGPAKDAKKY FQDMGYYCPP
RQTTADFLTS ITSPTERIIS KEFIEKGTRV PQTPKDMAEY WLQSESYKNL IKDIDSTLEK
NTDEARNIIR DAHHAKQAKR APPSSPYVVN YGMQVKYLLI RNFWRMKQSA SVTLWQVIGN
SVMAFILGSM FYKVMKKNDT STFYFRGAAM FFAILFNAFS CLLEIFSLYE TRPITEKHRT
YSLYHPSADA FASVLSEMPP KLITAVCFNI IFYFLVDFRR NGGVFFFYFL INVIATFTLS
HLFRCVGSLT KTLQEAMVPA SMLLLAISMY TGFAIPKTKI LGWSIWIWYI NPLAYLFESL
MINEFHDRRF PCAQYIPAGP AYQNITGTQR VCSAVGAYPG NDYVLGDDFL KESYDYEHKH
KWRGFGIGMA YVVFFFFVYL ILCEYNEGAK QKGEMVVFLR SKIKQLKKEG KLQEKHRPGD
IENNAGSSPD SATTEKKILD DSSEGSDSSS DNAGLGLSKS EAIFHWRDLC YDVPIKGGQR
RILNNVDGWV KPGTLTALMG ASGAGKTTLL DCLAERVTMG VITGNIFVDG RLRDESFPRS
IGYCQQQDLH LKTATVRESL RFSAYLRQPS SVSIEEKNRY VEEVIKILEM QQYSDAVVGV
AGEGLNVEQR KRLTIGVELA ARPKLLVFLD EPTSGLDSQT AWDTCQLMRK LATHGQAILC
TIHQPSAILM QQFDRLLFLQ KGGQTVYFGD LGEGCKTMID YFESKGAHKC PPDANPAEWM
LEVVGAAPGS HATQDYNEVW RNSDEYKAVQ EELDWMEKNL PGRSKEPTAE EHKPFAASLY
YQFKMVTIRL FQQYWRSPDY LWSKFILTIF NQVFIGFTFF KADRSLQGLQ NQMLSIFMYT
VIFNPILQQY LPSFVQQRDL YEARERPSRT FSWLAFFLSQ IIVEIPWNIL AGTIAYCIYY
YAVGFYANAS AAGQLHERGA LFWLFSIAFY VYIGSMGLLM ISFNEVAETA AHMGTLLFTM
ALSFCGVMAT PKVMPRFWIF MYRVSPLTYM IDALLALGVA NVDVKCSNYE MVKFTPPSGT
TCGDYMASYI KLAGTGYLSD PSATDICSFC AVSTTNAFLA TFSSHYYRRW RNYGIFICYI
AFDYIAATFL YWLSRVPKKN GKISEKPKK
