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MDR2_ASPFU
ID   MDR2_ASPFU              Reviewed;         791 AA.
AC   Q4WPP6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=ABC multidrug transporter mdr2 {ECO:0000303|PubMed:9373135};
GN   Name=mdr2 {ECO:0000303|PubMed:9373135}; ORFNames=AFUA_4G10000;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=9373135; DOI=10.1016/s0378-1119(97)00281-3;
RA   Tobin M.B., Peery R.B., Skatrud P.L.;
RT   "Genes encoding multiple drug resistance-like proteins in Aspergillus
RT   fumigatus and Aspergillus flavus.";
RL   Gene 200:11-23(1997).
RN   [3]
RP   INDUCTION.
RX   PubMed=15504870; DOI=10.1128/aac.48.11.4405-4413.2004;
RA   da Silva Ferreira M.E., Capellaro J.L., dos Reis Marques E., Malavazi I.,
RA   Perlin D., Park S., Anderson J.B., Colombo A.L., Arthington-Skaggs B.A.,
RA   Goldman M.H., Goldman G.H.;
RT   "In vitro evolution of itraconazole resistance in Aspergillus fumigatus
RT   involves multiple mechanisms of resistance.";
RL   Antimicrob. Agents Chemother. 48:4405-4413(2004).
RN   [4]
RP   INDUCTION.
RX   PubMed=18838595; DOI=10.1128/aac.01431-07;
RA   Gautam P., Shankar J., Madan T., Sirdeshmukh R., Sundaram C.S., Gade W.N.,
RA   Basir S.F., Sarma P.U.;
RT   "Proteomic and transcriptomic analysis of Aspergillus fumigatus on exposure
RT   to amphotericin B.";
RL   Antimicrob. Agents Chemother. 52:4220-4227(2008).
RN   [5]
RP   INDUCTION.
RX   PubMed=21724936; DOI=10.1128/ec.05102-11;
RA   Gibbons J.G., Beauvais A., Beau R., McGary K.L., Latge J.P., Rokas A.;
RT   "Global transcriptome changes underlying colony growth in the opportunistic
RT   human pathogen Aspergillus fumigatus.";
RL   Eukaryot. Cell 11:68-78(2012).
RN   [6]
RP   INDUCTION.
RX   PubMed=28080217; DOI=10.1089/mdr.2016.0217;
RA   Li S.X., Song Y.J., Jiang L., Zhao Y.J., Guo H., Li D.M., Zhu K.J.,
RA   Zhang H.;
RT   "Synergistic effects of tetrandrine with posaconazole against Aspergillus
RT   fumigatus.";
RL   Microb. Drug Resist. 23:674-681(2017).
CC   -!- FUNCTION: Pleiotropic ABC efflux transporter that may be involved in
CC       A.fumigatus adaptation to azoles. {ECO:0000305|PubMed:9373135}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is up-regulated during biofilm growth
CC       (PubMed:21724936). Expression is also induced upon amphotericin B
CC       treatment (PubMed:18838595). Expression is down-regulated by
CC       tetrandrine and posaconazole in a synergistic manner (PubMed:28080217).
CC       Expression is increased in clinical azole-resistant isolates
CC       (PubMed:15504870). {ECO:0000269|PubMed:15504870,
CC       ECO:0000269|PubMed:18838595, ECO:0000269|PubMed:21724936,
CC       ECO:0000269|PubMed:28080217}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000005; EAL89788.1; -; Genomic_DNA.
DR   RefSeq; XP_751826.1; XM_746733.1.
DR   AlphaFoldDB; Q4WPP6; -.
DR   SMR; Q4WPP6; -.
DR   STRING; 746128.CADAFUBP00006530; -.
DR   EnsemblFungi; EAL89788; EAL89788; AFUA_4G10000.
DR   GeneID; 3509566; -.
DR   KEGG; afm:AFUA_4G10000; -.
DR   VEuPathDB; FungiDB:Afu4g10000; -.
DR   eggNOG; KOG0058; Eukaryota.
DR   HOGENOM; CLU_000604_84_3_1; -.
DR   InParanoid; Q4WPP6; -.
DR   OMA; WGTYLVK; -.
DR   OrthoDB; 684058at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015421; F:ABC-type oligopeptide transporter activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0090374; P:oligopeptide export from mitochondrion; IBA:GO_Central.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..791
FT                   /note="ABC multidrug transporter mdr2"
FT                   /id="PRO_0000445103"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        307..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          182..471
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          504..741
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          754..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         539..546
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        692
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   791 AA;  85169 MW;  EAA0F7C35CC3BCF0 CRC64;
     MRGIRSLPCW APGLSTKRIP PRELFADLFP NACVISARHS ARNGLIRQFS GCSGSISNSC
     NPRPYRSAIT SLLSANVCSK GVSAVQPRFL STVRLFSTSQ RSLEPKSNVK STGGQVVRPE
     LHQDQEHEDI EKGFELSERA AQAAQVNLSA KLAKDGAAGK KAGFKEIWRL LLIARPEAKK
     LALAFLFLLV SSGITMSIPF SIGKIMDTST KATTEGGNEL FGLSLPMFYG ALAGILTLGA
     AANYGRIIIL RIVGERIVAR LRSKLFRQTF VQDAEFFDAN RVGDLISRLS SDTIIVGKSI
     TQNLSDGLRA AVSGAAGFGL MAYVSLKLSS ILALLLPPIG LGAFFYGRAI RNLSRQIQRN
     LGTLTKIAEE RLGNVKTSQS FAGEVLEVRR YNNQVRKIFE LGKKESLISA TFFSSTGFAG
     NMTILALLYV GGGMVQSGAI TIGELTSFLM YTAYAGSSMF GLSSFYSELM KGVGAASRLF
     ELQDRQPTIS PTKGEKVASA RGPIRFENVT FSYPTRPAVP IFRDLNFEIP QGTNVAIVGP
     SGGGKSTIAS ILLRFYSPTE GRVLIGGKDI THMNAKSLRR KIGIVSQEPV LFSGTIAENI
     AYGKPQAKRS EIVAAARKAN CQFISDFPDG LDTQVGPRGA QLSGGQKQRI AIARALIKDP
     DILILDEATS ALDAESETLV NSALTALLRG NNTTISIAHR LSTIKRSDTI IVLGPDGRVA
     EQGSYEELSA RPDGAFTKLM EWQMSGGEVM DQLANTPANP VAQETSWDLQ SDDGTEISED
     TNIPSEPRTI D
 
 
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