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ABCC_ASPFU
ID   ABCC_ASPFU              Reviewed;        1497 AA.
AC   E9RBG1; Q4WS17; Q6MY55;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ABC multidrug transporter C {ECO:0000303|PubMed:16622700};
GN   Name=abcC {ECO:0000303|PubMed:16622700};
GN   Synonyms=abcB {ECO:0000303|PubMed:24123268},
GN   abcG1 {ECO:0000303|PubMed:28264842}, atrE {ECO:0000303|PubMed:14998527},
GN   cdr1B {ECO:0000303|PubMed:23580559}; ORFNames=AFUA_1G14330;
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 [GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA   Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B.G., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
RN   [2]
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   [3]
RP   IDENTIFICATION, INDUCTION, AND FUNCTION.
RX   PubMed=16622700; DOI=10.1007/s00294-006-0073-2;
RA   da Silva Ferreira M.E., Malavazi I., Savoldi M., Brakhage A.A.,
RA   Goldman M.H., Kim H.S., Nierman W.C., Goldman G.H.;
RT   "Transcriptome analysis of Aspergillus fumigatus exposed to voriconazole.";
RL   Curr. Genet. 50:32-44(2006).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22509997; DOI=10.1111/j.1574-6968.2012.02575.x;
RA   Bowyer P., Mosquera J., Anderson M., Birch M., Bromley M., Denning D.W.;
RT   "Identification of novel genes conferring altered azole susceptibility in
RT   Aspergillus fumigatus.";
RL   FEMS Microbiol. Lett. 332:10-19(2012).
RN   [5]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=24123268; DOI=10.1128/ec.00171-13;
RA   Paul S., Diekema D., Moye-Rowley W.S.;
RT   "Contributions of Aspergillus fumigatus ATP-binding cassette transporter
RT   proteins to drug resistance and virulence.";
RL   Eukaryot. Cell 12:1619-1628(2013).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=23580559; DOI=10.1093/jac/dkt075;
RA   Fraczek M.G., Bromley M., Buied A., Moore C.B., Rajendran R., Rautemaa R.,
RA   Ramage G., Denning D.W., Bowyer P.;
RT   "The cdr1B efflux transporter is associated with non-cyp51a-mediated
RT   itraconazole resistance in Aspergillus fumigatus.";
RL   J. Antimicrob. Chemother. 68:1486-1496(2013).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28264842; DOI=10.1128/aac.02748-16;
RA   Paul S., Diekema D., Moye-Rowley W.S.;
RT   "Contributions of both ATP-Binding Cassette Transporter and Cyp51A Proteins
RT   Are Essential for Azole Resistance in Aspergillus fumigatus.";
RL   Antimicrob. Agents Chemother. 61:0-0(2017).
RN   [8]
RP   INDUCTION.
RX   PubMed=28052140; DOI=10.1371/journal.ppat.1006096;
RA   Hagiwara D., Miura D., Shimizu K., Paul S., Ohba A., Gonoi T., Watanabe A.,
RA   Kamei K., Shintani T., Moye-Rowley W.S., Kawamoto S., Gomi K.;
RT   "A novel Zn2-Cys6 transcription factor atrR plays a key role in an azole
RT   resistance mechanism of Aspergillus fumigatus by co-regulating cyp51A and
RT   cdr1B Expressions.";
RL   PLoS Pathog. 13:E1006096-E1006096(2017).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   AND INDUCTION.
RX   PubMed=32209680; DOI=10.1128/mbio.00338-20;
RA   Esquivel B.D., Rybak J.M., Barker K.S., Fortwendel J.R., Rogers P.D.,
RA   White T.C.;
RT   "Characterization of the efflux capability and substrate specificity of
RT   Aspergillus fumigatus PDR5-like ABC transporters expressed in Saccharomyces
RT   cerevisiae.";
RL   MBio 11:0-0(2020).
CC   -!- FUNCTION: Pleiotropic ABC efflux transporter that shows a strong
CC       substrate specificity for the azole class of drugs such as lotrimazole
CC       (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC),
CC       posaconazole (POS), tebuconazole (TEBZ), and voriconazole (VRC)
CC       (Probable) (PubMed:22509997, PubMed:23580559, PubMed:24123268,
CC       PubMed:28264842, PubMed:32209680). Is also able to transport rhodamine
CC       6G (R-6G), a known substrate for many ABC transporters
CC       (PubMed:32209680). Required for normal pathogenesis in a Galleria
CC       mellonella (greater wax moth) infection model (PubMed:24123268).
CC       {ECO:0000269|PubMed:22509997, ECO:0000269|PubMed:23580559,
CC       ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:28264842,
CC       ECO:0000269|PubMed:32209680, ECO:0000305|PubMed:16622700}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46081, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:32209680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917;
CC         Evidence={ECO:0000269|PubMed:32209680};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out)
CC         + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504;
CC         Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate +
CC         voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913;
CC         Evidence={ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:32209680};
CC   -!- ACTIVITY REGULATION: The efflux inhibitor FK506 impairs the transport
CC       activity. {ECO:0000269|PubMed:32209680}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24123268};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the atrR transcription
CC       factor (PubMed:28052140). Expression is induced upon voriconazole
CC       treatment (PubMed:16622700, PubMed:24123268). Expression is increased
CC       in clinical azole-resistant isolates (PubMed:23580559,
CC       PubMed:32209680). In particular F20140, F18304 and F18454 show over 25-
CC       fold greater basal expression levels, whereas F19980 (7.2-fold), F20063
CC       (6.5-fold), F20451 (3.6-fold), F18454 (5.1-fold) and F15483 (2.1-fold)
CC       also show significantly raised levels of basal expression
CC       (PubMed:23580559). {ECO:0000269|PubMed:16622700,
CC       ECO:0000269|PubMed:23580559, ECO:0000269|PubMed:24123268,
CC       ECO:0000269|PubMed:28052140, ECO:0000269|PubMed:32209680}.
CC   -!- DISRUPTION PHENOTYPE: Leads to decreased azole resistance, including
CC       itraconazole, posaconazole and voriconazole.
CC       {ECO:0000269|PubMed:22509997, ECO:0000269|PubMed:23580559,
CC       ECO:0000269|PubMed:24123268, ECO:0000269|PubMed:28264842}.
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; BX649607; CAF32148.1; -; Genomic_DNA.
DR   EMBL; AAHF01000004; EAL90765.1; -; Genomic_DNA.
DR   RefSeq; XP_752803.1; XM_747710.1.
DR   AlphaFoldDB; E9RBG1; -.
DR   SMR; E9RBG1; -.
DR   STRING; 746128.CADAFUBP00001360; -.
DR   EnsemblFungi; EAL90765; EAL90765; AFUA_1G14330.
DR   GeneID; 3509814; -.
DR   KEGG; afm:AFUA_1G14330; -.
DR   VEuPathDB; FungiDB:Afu1g14330; -.
DR   eggNOG; KOG0065; Eukaryota.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   InParanoid; E9RBG1; -.
DR   OMA; IAEATLC; -.
DR   OrthoDB; 37708at2759; -.
DR   PHI-base; PHI:4230; -.
DR   PHI-base; PHI:8901; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1497
FT                   /note="ABC multidrug transporter C"
FT                   /id="PRO_0000445098"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        557..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        632..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        665..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        777..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1192..1212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1226..1246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1273..1293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1313..1333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1352..1372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1464..1484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..412
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          853..1096
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         889..896
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        762
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1411
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1497 AA;  168184 MW;  706E5D1B5C097043 CRC64;
     MSLLGTINPN INPERTVAGR GTQEEEGEIA RVEHNHHNNA ASVSTDETVL ERSKEIGDED
     VAVEEVTRLA RQLTRQSTRF STSGNVENPF LETKEDSTLN PLSPNFKAKN WMKNLLALSS
     RDPERYPKRV AGVAFKNLSV HGYGSPTDYQ KDVFNSVLEV GTLVRRIMGT GKQKIQILRD
     FDGLVKSGEM LVVLGRPGSG CSTFLKTISG EMNGIYMDEK SYLNYQGISS KQMRKQFRGE
     AIYTAETDVH FPQLTVGDTL KFAALARAPR NRLPGVSREQ YAVHMRDVVM AMLGLTHTMN
     TRVGNDFVRG VSGGERKRVS IAEATLSGSP LQCWDNSTRG LDSANALEFC KTLNLMTKYA
     GATVAVAIYQ ASQSAYDVFD KVTVLYEGRQ IYFGRTDEAK EFFTNMGFEC PERQTTADFL
     TSLTSPAERV VKPGFEGKVP QTPDEFVRAW KSSEAYAKLM REIEEYDREF PIGGESLNQF
     IESRRAMQAK NQRVKSPYTI SVWQQIELCM IRGFQRLKGD SSLTMSQLIG NFIMALVIGS
     VFYNLPDDTS SFYARGALLF FAVLLNAFSS ALEILTLYAQ RPIVEKQARY AMYHPFAEAI
     ASMLCDMPYK ITNAIIFNLT LYFMTNLRRE PGAFFVFLLF SFVTTLTMSM LFRTMAASSR
     TLSQALVPAA ILILGLVIYT GFTIPTRNML GWSRWMNYID PIAYGFESLM VNEFHNRQFL
     CPDSAFVPSS GAYDSQPLAY RVCSTVGSVS GSRYVQGDDY LNQSFQYYKS HQWRNLGIMF
     GFMFFFMFTY LTATEYISES KSKGEVLLFR RGHAQPTGSH DVEKSPEVSS AAKTDEASSK
     EATGAIQRQE AIFQWKDVCY DIKIKGEPRR ILDHVDGWVK PGTCTALMGV SGAGKTTLLD
     VLATRVTMGV VSGEMLVDGR PRDQSFQRKT GYVQQQDLHL HTTTVREALR FSALLRQPAH
     VPRQEKIDYV EEVIKLLGME SYADAVVGVP GEGLNVEQRK RLTIGVELAA KPQLLLFLDE
     PTSGLDSQTS WSILDLIDTL TKHGQAILCT IHQPSAMLFQ RFDRLLFLAK GGKTVYFGEI
     GEKSSTLASY FERNGAPKLP PDANPAEWML EVIGAAPGSH SDIDWPAVWR DSPERRAVHE
     HLDELKRTLS QKPIDPSKAD PGSYDEFAAP FTIQLWECLL RVFSQYWRTP VYIYSKTALC
     VLTALYIGFS FFNAQNSAQG LQNQMFSIFM LMTIFGNLVQ QIMPNFCTQR SLYEVRERPS
     KTYSWKAFMA ANIIVELPWN TLMAFLIFVC WYYPIGLYRN AEPTDSVHER GALMFLLIWS
     FLLFTSTFAH MMIAGIELAE TGGNLANLLF SLCLIFCGVL APPQSLPGFW IFMYRVSPFT
     YLVSAMLSTG VSGTNAVCEP VEFLHFDPPS NMTCKDYMAD YISTRGGYLE NPSATSDCTF
     CTISSTDTFL SAVSSHYSDA WRNFGIMWAY IIFNIFAAVF IYWLARVPKG KRTKGST
 
 
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