PDR10_YEAST
ID PDR10_YEAST Reviewed; 1564 AA.
AC P51533; D6W325;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=ATP-dependent permease PDR10;
GN Name=PDR10; OrderedLocusNames=YOR328W;
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 [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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).
CC -!- INTERACTION:
CC P51533; P40030: ERG28; NbExp=2; IntAct=EBI-3761544, EBI-22518;
CC P51533; P32804: ZRT1; NbExp=2; IntAct=EBI-3761544, EBI-29677;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; Z49821; CAA89975.1; -; Genomic_DNA.
DR EMBL; Z75236; CAA99649.1; -; Genomic_DNA.
DR EMBL; Z75237; CAA99651.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11091.1; -; Genomic_DNA.
DR PIR; S55517; S55517.
DR RefSeq; NP_014973.1; NM_001183748.1.
DR AlphaFoldDB; P51533; -.
DR SMR; P51533; -.
DR BioGRID; 34713; 114.
DR IntAct; P51533; 23.
DR MINT; P51533; -.
DR STRING; 4932.YOR328W; -.
DR TCDB; 3.A.1.205.12; the atp-binding cassette (abc) superfamily.
DR PaxDb; P51533; -.
DR PRIDE; P51533; -.
DR EnsemblFungi; YOR328W_mRNA; YOR328W; YOR328W.
DR GeneID; 854506; -.
DR KEGG; sce:YOR328W; -.
DR SGD; S000005855; PDR10.
DR VEuPathDB; FungiDB:YOR328W; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176297; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P51533; -.
DR OMA; CAVSMYQ; -.
DR BioCyc; YEAST:G3O-33805-MON; -.
DR PRO; PR:P51533; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P51533; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISS:SGD.
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; 2.
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..1564
FT /note="ATP-dependent permease PDR10"
FT /id="PRO_0000093443"
FT TOPO_DOM 1..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 862..1304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1340..1360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1390..1410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1426..1446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1459..1479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1491..1511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1512..1564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..430
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 923..1166
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 959..966
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1564 AA; 176461 MW; 7CBE57D9133B8A01 CRC64;
MLQAPSSSNS GLNQGNAAPD GPPNETQPYE GLDAAAQEEI KELARTLTSQ SSLLSQEKRI
TGTGDPNTLT AASSSSLSRS IFASDIKGVN PILLDVNDPD YDETLDPRSE NFSSVRWVRN
MAQICENDSD FYKPFSLGCA WKDLSASGDS ADITYQGTFG NMPIKYLKMS WRCISRRLFH
RTHGKSEDND SGFQILKPMD GCINPGELLV VLGRPGAGCT TLLKSISVNT HGFKISPDTI
ITYNGFSNKE IKNHYRGEVV YNAESDIHIP HLTVFQTLYT VARLKTPRNR IKGVDRDTFA
KHMTEVAMAT YGLSHTADTK VGNDFVRGVS GGERKRVSIA EVSICGSKFQ CWDNATRGLD
SATALEFIKA LKTQATITKS AATVAIYQCS KDAYDLFDKV CVLYDGYQIF FGPSKQAKKY
FQRMGYVCPE RQTTADYLTS ITSPSERIKD KDMVKHGIMI PQTAYEMNQY WIQSEEYKQL
QVQVNKHLDT DSSQQREQIK NAHIAKQSKR ARPSSPYTVS FFLQVKYILI RDIWRIKNDP
SIQLFTVLSH AAMALILGSM FYEVMLSTTT TTFYYRGAAI FFAILFNAFS SLLEIFSLYE
TRPITEKHKT YSLYRPSADA FASTFSDVPT KLATAVTFNI PYYFLINLKR DAGAFFFYFL
INIITVFAMS HLFRCIGSVS KTLPQAMVPA SVLLLAFAMY TGFAIPRVQM LGWSKWISYI
NPLSYLFESL MINEFHGRNF PCAQYIPSGP NYVNATGDEV TCSALGSIPG NNYVSGDDFI
QTNYGYRHKN KWRSVGIGLA YIIFFLFLYL FFCEYNEGAK QNGEMLVFPH SVVKKMKKKG
IVSEKKKKNQ PTLSTSDAEK DVEMNNNSSA TDSRFLRDSD AAIMGNDKTV AKEHYSSPSS
SASQSNSFSK SDDIELSKSQ AIFHWKNLCY DIPIKNGKRR ILDNVDGWVK PGTLTALIGA
SGAGKTTLLD CLAERTTMGL ITGDVFVDGR PRDQSFPRSI GYCQQQDLHL KTATVRESLR
FSAYLRQADD VSIEEKDKYV EEVIEVLEMK LYADAIVGVP GEGLNVEQRK RLTIGVELAA
KPKLLVFLDE PTSGLDSQTA WSTCQLMKKL ASRGQAILCT IHQPSALLMQ EFDRLLFLQE
GGQTVYFGEL GKGCKTMINY FEAHGAHKCP PDANPAEWML EIVGAAPGTH ASQDYFAIWR
DSEEYREMQK ELDWMERELP KRTEGSSNEE QKEFATSTLY QIKLVSYRLF HQYWRTPFYL
WSKFFSTIVS ELFIGFTFFK ANTSLQGLQN QMLAIFMFTV VFNPILQQYL PLFVQQRELY
EARERPSRTF SWKAFIVSQI LVEIPWNLLA GTIAFFVYYY PVGFYRNASY ANQLHERGAL
FWLFACAFYV YISSMGVLVI SCIEIAENAA NLASLFFIMS LSFCGVLATP NILPRFWIFM
YRVSPLTYLI DALLSVGLAN ASVVCSSNEL LKIVPPSGMT CSEYMEPYMQ STGTGYLLDG
SSETECHFCQ FSSTNDYLAT VSSSYSRRWM NYGIFSAYIV FDYCAAIFLY WLVRVPKKSK
KLKK
