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PDR18_YEAST
ID   PDR18_YEAST             Reviewed;        1333 AA.
AC   P53756; D6W1P5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 179.
DE   RecName: Full=ABC transporter ATP-binding protein/permease PDR18;
DE   AltName: Full=Pleiotropic drug resistance protein 18;
GN   Name=PDR18; OrderedLocusNames=YNR070W; ORFNames=N3568;
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=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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).
CC   -!- INTERACTION:
CC       P53756; P40219: OSW5; NbExp=2; IntAct=EBI-28581, EBI-3681488;
CC       P53756; P20107: ZRC1; NbExp=2; IntAct=EBI-28581, EBI-29667;
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; Z71685; CAA96352.1; -; Genomic_DNA.
DR   EMBL; Z71686; CAA96354.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10611.1; -; Genomic_DNA.
DR   PIR; S63403; S63403.
DR   RefSeq; NP_014468.3; NM_001183247.4.
DR   AlphaFoldDB; P53756; -.
DR   SMR; P53756; -.
DR   BioGRID; 35896; 33.
DR   DIP; DIP-7300N; -.
DR   IntAct; P53756; 6.
DR   MINT; P53756; -.
DR   STRING; 4932.YNR070W; -.
DR   TCDB; 3.A.1.205.31; the atp-binding cassette (abc) superfamily.
DR   MaxQB; P53756; -.
DR   PaxDb; P53756; -.
DR   PRIDE; P53756; -.
DR   EnsemblFungi; YNR070W_mRNA; YNR070W; YNR070W.
DR   GeneID; 855807; -.
DR   KEGG; sce:YNR070W; -.
DR   SGD; S000005353; PDR18.
DR   VEuPathDB; FungiDB:YNR070W; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   GeneTree; ENSGT00940000176297; -.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; P53756; -.
DR   OMA; NQVCTIV; -.
DR   BioCyc; YEAST:G3O-33374-MON; -.
DR   PRO; PR:P53756; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53756; protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA: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:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR   GO; GO:0055092; P:sterol homeostasis; 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; 2.
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; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1333
FT                   /note="ABC transporter ATP-binding protein/permease PDR18"
FT                   /id="PRO_0000093466"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1071..1091
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1092..1112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1150..1170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1178..1198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1210..1230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1235..1255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..281
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          729..971
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         765..772
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        958
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1333 AA;  149750 MW;  61B4758E0245CB70 CRC64;
     MECVSVEGLD SSFLEGQTFG DILCLPWTII KGIRERKNRN KMKIILKNVS LLAKSGEMVL
     VLGRPGAGCT SFLKSAAGET SQFAGGVTTG HISYDGIPQK EMMQHYKPDV IYNGEQDVHF
     PHLTVKQTLD FAISCKMPAK RVNNVTKEEY ITANREFYAK IFGLTHTFDT KVGNDFISGV
     SGGERKRVSI AEALAAKGSI YCWDNATRGL DSSTALEFAR AIRTMTNLLG TTALVTVYQA
     SENIYETFDK VTVLYAGRQI FCGKTTEAKD YFENMGYLCP PRQSTAEYLT AITDPNGLHE
     IKPGFEYQVP HTADEFEKYW LDSPEYARLK GEIQKYKHEV NTEWTKKTYN ESMAQEKSKG
     TRKKSYYTVS YWEQIRLCTI RGFLRIYGDK SYTVINTCAA IAQAFITGSL FYQAPSSTLG
     AFSRSGVLFF SLLYYSLMGL ANISFEHRPI LQKHKVYSLY HPSAEALAST ISSFPFRMIG
     LTFFIIILYF LAGLHRSAGA FFTMYLLLTM CSEAITSLFQ MVSSLCDTLS QANSIAGVVM
     LSIAMYSTYM IQLPSMHPWF KWISYILPIR YAFESMLNAE FHGRHMDCGG TLVPSGPGFE
     NILPENQVCA FVGSRPGQSW VLGDDYLRAQ YQYEYKNTWR NFGIMWCFLI GYIVLRAVFT
     EYKSPVKSGG DALVVKKGTK NAIQRSWSSK NDEENLNASI ATQDMKEIAS SNDDSTSADF
     EGLESTGVFI WKNVSFTIPH SSGQRKLLDS VSGYCVPGTL TALIGESGAG KTTLLNTLAQ
     RNVGTITGDM LVDGLPMDAS FKRRTGYVQQ QDLHVAELTV KESLQFSARM RRPQSIPDAE
     KMEYVEKIIS ILEMQEFSEA LVGEIGYGLN VEQRKKLSIG VELVGKPDLL LFLDEPTSGL
     DSQSAWAVVK MLKRLALAGQ SILCTIHQPS ATLFEQFDRL LLLGKGGQTI YFGEIGKNSS
     SVIKYFEKNG ARKCQQNENP AEYILEAIGA GATASVQQNW PDIWQKSHEY ANINEKINDM
     IKDLSSTTLH KTATRASKYA TSYSYQFHHV LKRSSLTFWR NLNYIMAKMM LLMISGLFIG
     FTFFHVGVNA IGLQNSLFAC FMAIVISAPA TNQIQERATV AKELYEVRES KSNMFHWSLL
     LITHYLNELP YHLLFSTIFF VSSYFPLGVF TEASRSSVFY LNYAILFQLY YIGLALMILY
     MSPNLQSANV IVGFILSFLL SFCGAVQPAS LMPGFWTFMW KLSPYTYFLQ NLVGLLMHDK
     PVRCSKKELS LFNPPVGQTC GEFTKPFFEF GTGYIANPDA TADCAYCQYK VGDEYLARIN
     ASFSYLWRNF GFI
 
 
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