PDR11_YEAST
ID PDR11_YEAST Reviewed; 1411 AA.
AC P40550; D6VVR7; Q03092;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=ATP-dependent permease PDR11;
GN Name=PDR11; OrderedLocusNames=YIL013C;
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 IDENTIFICATION, AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=7629127; DOI=10.1074/jbc.270.30.18150;
RA Decottignies A., Lambert L., Catty P., Degand H., Epping E.A.,
RA Moye-Rowley W.S., Balzi E., Goffeau A.;
RT "Identification and characterization of SNQ2, a new multidrug ATP binding
RT cassette transporter of the yeast plasma membrane.";
RL J. Biol. Chem. 270:18150-18157(1995).
RN [4]
RP FUNCTION.
RX PubMed=12077145; DOI=10.1074/jbc.m204707200;
RA Wilcox L.J., Balderes D.A., Wharton B., Tinkelenberg A.H., Rao G.,
RA Sturley S.L.;
RT "Transcriptional profiling identifies two members of the ATP-binding
RT cassette transporter superfamily required for sterol uptake in yeast.";
RL J. Biol. Chem. 277:32466-32472(2002).
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).
CC -!- FUNCTION: Transporter involved in the uptake of sterol.
CC {ECO:0000269|PubMed:12077145}.
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; Z38113; CAA86236.1; -; Genomic_DNA.
DR EMBL; Z46881; CAA86980.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08533.1; -; Genomic_DNA.
DR PIR; S48442; S48442.
DR RefSeq; NP_012252.1; NM_001179363.1.
DR AlphaFoldDB; P40550; -.
DR SMR; P40550; -.
DR BioGRID; 34978; 89.
DR DIP; DIP-8310N; -.
DR IntAct; P40550; 7.
DR MINT; P40550; -.
DR STRING; 4932.YIL013C; -.
DR TCDB; 3.A.1.205.8; the atp-binding cassette (abc) superfamily.
DR CarbonylDB; P40550; -.
DR PaxDb; P40550; -.
DR EnsemblFungi; YIL013C_mRNA; YIL013C; YIL013C.
DR GeneID; 854802; -.
DR KEGG; sce:YIL013C; -.
DR SGD; S000001275; PDR11.
DR VEuPathDB; FungiDB:YIL013C; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176496; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; P40550; -.
DR OMA; PYCFLAT; -.
DR BioCyc; YEAST:G3O-31289-MON; -.
DR PRO; PR:P40550; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40550; 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:0035376; P:sterol import; IMP: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; 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; 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; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7629127"
FT CHAIN 2..1411
FT /note="ATP-dependent permease PDR11"
FT /id="PRO_0000093444"
FT TOPO_DOM 2..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1139..1175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1176..1196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1197..1204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1205..1225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1226..1230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1252..1355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1356..1376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1377..1411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..273
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 751..979
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 782..789
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1411 AA; 160538 MW; 83D040F42BB04526 CRC64;
MSLSKYFNPI PDASVTFDGA TVQLEESLGA VQNDEESASE FKNVGHLEIS DITFRANEGE
VVLVLGNPTS ALFKGLFHGH KHLKYSPEGS IRFKDNEYKQ FASKCPHQII YNNEQDIHFP
YLTVEQTIDF ALSCKFHIPK QERIEMRDEL LKEFGLSHVK KTYVGNDYVR GVSGGERKRI
SIIETFIANG SVYLWDNSTK GLDSATALEF LSITQKMAKA TRSVNFVKIS QASDKIVSKF
DKILMLGDSF QVFYGTMEEC LTHFHDTLQI KKNPNDCIIE YLTSILNFKF KETSNSIVGL
DTPSVVSEEN QALNINNETD LHTLWIQSPY YKHWKAITSK TVQECTRKDV NPDDISPIFS
IPLKTQLKTC TVRAFERIIG DRNYLISQFV SVVVQSLVIG SLFYNIPLTT IGSFSRGSLT
FFSILFFTFL SLADMPASFQ RQPVVRKHVQ LHFYYNWVET LATNFFDCCS KFILVVIFTI
ILYFLAHLQY NAARFFIFLL FLSVYNFCMV SLFALTALIA PTLSMANLLA GILLLAIAMY
ASYVIYMKDM HPWFIWIAYL NPAMFAMEAI LSNELFNLKL DCHESIIPRG EYYDNISFSH
KACAWQGATL GNDYVRGRDY LKSGLKYTYH HVWRNFGIII GFLCFFLFCS LLAAEYITPL
FTRENLLRWN NYLKRYCPFL NSQKKNNKSA ITNNDGVCTP KTPIANFSTS SSSVPSVSHQ
YDTDYNIKHP DETVNNHTKE SVAMETQKHV ISWKNINYTI GDKKLINDAS GYISSGLTAL
MGESGAGKTT LLNVLSQRTE SGVVTGELLI DGQPLTNIDA FRRSIGFVQQ QDVHLELLTV
RESLEISCVL RGDGDRDYLG VVSNLLRLPS EKLVADLSPT QRKLLSIGVE LVTKPSLLLF
LDEPTSGLDA EAALTIVQFL KKLSMQGQAI LCTIHQPSKS VISYFDNIYL LKRGGECVYF
GSLPNACDYF VAHDRRLTFD REMDNPADFV IDVVGSGSTN IPMDDAEKPT SSKIDEPVSY
HKQSDSINWA ELWQSSPEKV RVADDLLLLE EEARKSGVDF TTSVWSPPSY MEQIKLITKR
QYICTKRDMT YVFAKYALNA GAGLFIGFSF WRTKHNINGL QDAIFLCFMM LCVSSPLINQ
VQDKALQSKE VYIAREARSN TYHWTVLLIA QTIVELPLAI SSSTLFFLCC YFCCGFETSA
RVAGVFYLNY ILFSMYYLSF GLWLLYSAPD LQTAAVFVAF LYSFTASFCG VMQPYSLFPR
FWTFMYRVSP YTYFIETFVS LLLHDREVNC STSEMVPSQP VMGQTCGQFM KPFIDEFGGK
LHINNTYTVC AYCMYTVGDD FLAQENMSYH HRWRNFGFEW VFVCFNIAAM FVGFYLTYIK
KIWPSVIDGI KKCIPSMRRS KTSHNPNEQS V
