ID   ATRD_EMEND              Reviewed;        1348 AA.
AC   Q9Y8G1;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=ABC multidrug transporter atrD;
GN   Name=atrD {ECO:0000303|PubMed:10954082}; Synonyms=abcD;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nascimento A.M., Terenzi M.F., Goldman M.H.S., Goldman G.H.;
RT   "Molecular characterization of ABC-transporter encoding genes in
RT   Aspergillus nidulans.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION
RP   PHENOTYPE, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   STRAIN=W6-096;
RX   PubMed=10954082; DOI=10.1007/pl00008697;
RA   Andrade A.C., Van Nistelrooy J.G., Peery R.B., Skatrud P.L., De Waard M.A.;
RT   "The role of ABC transporters from Aspergillus nidulans in protection
RT   against cytotoxic agents and in antibiotic production.";
RL   Mol. Gen. Genet. 263:966-977(2000).
RN   [3]
RP   INDUCTION.
RX   PubMed=11872487; DOI=10.1128/aem.68.3.1351-1357.2002;
RA   Semighini C.P., Marins M., Goldman M.H., Goldman G.H.;
RT   "Quantitative analysis of the relative transcript levels of ABC transporter
RT   Atr genes in Aspergillus nidulans by real-time reverse transcription-PCR
RT   assay.";
RL   Appl. Environ. Microbiol. 68:1351-1357(2002).
CC   -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the protection
CC       of the cells against a wide range of toxic compounds (PubMed:10954082).
CC       Confers resistance to the azole fenarimol via efflux transport
CC       (PubMed:10954082). May also be involved in the secretion of penicillin
CC       (PubMed:10954082). {ECO:0000269|PubMed:10954082}.
CC   -!- ACTIVITY REGULATION: Fenamirol efflux transporter activity is inhibited
CC       by the cyclosporin derivative PSC 833, nigericin, reserpine and
CC       valinomycin (PubMed:10954082). The effect of reserpine is transiant,
CC       while that of the cyclosporin derivative PSC 833, nigericin and
CC       valinomycin is proportional to the time of exposure (PubMed:10954082).
CC       Cyclohexinmide has inhibitory effect only when applied prior to
CC       addition of the fungicide (PubMed:10954082).
CC       {ECO:0000269|PubMed:10954082}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is strongly increased in the presence of
CC       cycloheximide, camptothecin, imazalil, itraconazole, hygromycin and 4-
CC       nitroquinoline oxide (4-NQO). {ECO:0000269|PubMed:10954082,
CC       ECO:0000269|PubMed:11872487}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the cellular accumulation of fenarimol
CC       (PubMed:10954082). Leads to increased susceptibility to cycloheximide,
CC       the cyclosporin derivative PSC 833, nigericin and valinomycin
CC       (PubMed:10954082). {ECO:0000269|PubMed:10954082}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC       Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF071411; AAD43626.1; -; Genomic_DNA.
DR   EMBL; AF173826; AAF29805.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y8G1; -.
DR   SMR; Q9Y8G1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1348
FT                   /note="ABC multidrug transporter atrD"
FT                   /id="PRO_0000449467"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        778..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        825..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        892..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        925..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1015..1035
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        1042..1062
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          118..408
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          443..688
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          779..1068
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1103..1341
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         478..485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1138..1145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        877
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1088
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1348 AA;  147469 MW;  7B0506AB631D0218 CRC64;
     MSPLETNPLS PETAMREPAE TSTTEEQAST PHAADEKKIL SDLSAPSSTT ATPADKEHRP
     KSSSSNNAVS VNEVDALIAH LPEDERQVLK TQLEEIKVNI SFFGLWRYAT KMDILIMVIS
     TICAIAAGAA LPLFTILFGS LASTFQRIML YQISYDEFYD ELTKNVLYFV YLGIGEFVTV
     YVSTVGFIYT GEHATQKIRE YYLESILRQN IGYFDKLGAG EVTTRITADT NLIQDGISEK
     VGLTLTALAT FVTAFIIAYV KYWKLALICS STIVALVLTM GGGSQFIIKY SKKSLDSYGA
     GGTVAEEVIS SIRNATAFGT QDKLAKQYEV HLDEAEKWGT KNQIVMGFMI GAMFGLMYSN
     YGLGFWMGSR FLVDGAVDVG DILTVLMAIL IGSFSLGNVS PNAQAFTNAV AAAAKIFGTI
     DRQSPLDPYS NEGKTLDHFE GHIELRNVKH IYPSRPEVTV MEDVSLSMPA GKTTALVGPS
     GSGKSTVVGL VERFYMPVRG TVLLDGHDIK DLNLRWLRQQ ISLVSQEPVL FGTTIYKNIR
     HGLIGTKYEN ESEDKVRELI ENAAKMANAH DFITALPEGY ETNVGQRGFL LSGGQKQRIA
     IARAVVSDPK ILLLDEATSA LDTKSEGVVQ AALERAAEGR TTIVIAHRLS TIKTAHNIVV
     LVNGKIAEQG THDELVDRGG AYRKLVEAQR INEQKEADAL EDADAEDLTN ADIAKIKTAS
     SASSDLDGKP TTIDRTGTHK SVSSAILSKR PPETTPKYSL WTLLKFVASF NRPEIPYMLI
     GLVFSVLAGG GQPTQAVLYA KAISTLSLPE SQYSKLRHDA DFWSLMFFVV GIIQFITQST
     NGAAFAVCSE RLIRRARSTA FRTILRQDIA FFDKEENSTG ALTSFLSTET KHLSGVSGVT
     LGTILMTSTT LGAAIIIALA IGWKLALVCI SVVPVLLACG FYRFYMLAQF QSRSKLAYEG
     SANFACEATS SIRTVASLTR ERDVWEIYHA QLDAQGRTSL ISVLRSSLLY ASSQALVFFC
     VALGFWYGGT LLGHHEYDIF RFFVCFSEIL FGAQSAGTVF SFAPDMGKAK NAAAEFRRLF
     DRKPQIDNWS EEGEKLETVE GEIEFRNVHF RYPTRPEQPV LRGLDLTVKP GQYVALVGPS
     GCGKSTTIAL LERFYDAIAG SILVDGKDIS KLNINSYRSF LSLVSQEPTL YQGTIKENIL
     LGIVEDDVPE EFLIKACKDA NIYDFIMSLP EGFNTVVGSK GGMLSGGQKQ RVAIARALLR
     DPKILLLDEA TSALDSESEK VVQAALDAAA RGRTTIAVAH RLSTIQKADV IYVFDQGKIV
     ESGTHSELVQ KKGRYYELVN LQSLGKGH