ATRD_EMENI
ID ATRD_EMENI Reviewed; 1343 AA.
AC Q5BAY0; A0A1U8QYB9; C8VN48;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ABC multidrug transporter atrD;
GN Name=atrD {ECO:0000303|PubMed:10954082}; ORFNames=ANIA_02300;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
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 [4]
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}.
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DR EMBL; AACD01000038; EAA64411.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86562.1; -; Genomic_DNA.
DR RefSeq; XP_659904.1; XM_654812.1.
DR AlphaFoldDB; Q5BAY0; -.
DR SMR; Q5BAY0; -.
DR STRING; 162425.CADANIAP00008993; -.
DR EnsemblFungi; CBF86562; CBF86562; ANIA_02300.
DR EnsemblFungi; EAA64411; EAA64411; AN2300.2.
DR GeneID; 2875050; -.
DR KEGG; ani:AN2300.2; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q5BAY0; -.
DR OMA; RSDANFW; -.
DR OrthoDB; 186078at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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 GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1343
FT /note="ABC multidrug transporter atrD"
FT /id="PRO_0000449468"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 887..907
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 920..942
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 115..403
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 438..683
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 774..1063
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1098..1336
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 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1133..1140
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 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1343 AA; 146935 MW; DB0C1AFDB8F0745B CRC64;
MSPLETNPLS PETAMREPAE TSTTEEQAST PHAADEKKIL SDLSAPSSTT ATPADKEHRP
KSSSSNNAVS VNEVDALIAH LPEDERQVLK TQLEEIKVNI SFFGLWRYAT KMDILIMVIS
TICAIAAGAA LPLFTAPSTF QRIMLYQISY DEFYDELTKN VLYFVYLGIG EFVTVYVSTV
GFIYTGEHAT QKIREYYLES ILRQNIGYFD KLGAGEVTTR ITADTNLIQD GISEKVGLTL
TALATFVTAF IIAYVKYWKL ALICSSTIVA LVLTMGGGSQ FIIKYSKKSL DSYGAGGTVA
EEVISSIRNA TAFGTQDKLA KQYEVHLDEA EKWGTKNQIV MGFMIGAMFG LMYSNYGLGF
WMGSRFLVDG AVDVGDILTV LMAILIGSFS LGNVSPNAQA FTNAVAAAAK IFGTIDRQSP
LDPYSNEGKT LDHFEGHIEL RNVKHIYPSR PEVTVMEDVS LSMPAGKTTA LVGPSGSGKS
TVVGLVERFY MPVRGTVLLD GHDIKDLNLR WLRQQISLVS QEPVLFGTTI YKNIRHGLIG
TKYENESEDK VRELIENAAK MANAHDFITA LPEGYETNVG QRGFLLSGGQ KQRIAIARAV
VSDPKILLLD EATSALDTKS EGVVQAALER AAEGRTTIVI AHRLSTIKTA HNIVVLVNGK
IAEQGTHDEL VDRGGAYRKL VEAQRINEQK EADALEDADA EDLTNADIAK IKTASSASSD
LDGKPTTIDR TGTHKSVSSA ILSKRPPETT PKYSLWTLLK FVASFNRPEI PYMLIGLVFS
VLAGGGQPTQ AVLYAKAIST LSLPESQYSK LRHDADFWSL MFFVVGIIQF ITQSTNGAAF
AVCSERLIRR ARSTAFRTIL RQDIAFFDKE ENSTGALTSF LSTETKHLSG VSGVTLGTIL
MTSTTLGAAI IIALAIGWKL ALVCISVVPV LLACGFYRFY MLAQFQSRSK LAYEGSANFA
CEATSSIRTV ASLTRERDVW EIYHAQLDAQ GRTSLISVLR SSLLYASSQA LVFFCVALGF
WYGGTLLGHH EYDIFRFFVC FSEILFGAQS AGTVFSFAPD MGKAKNAAAE FRRLFDRKPQ
IDNWSEEGEK LETVEGEIEF RNVHFRYPTR PEQPVLRGLD LTVKPGQYVA LVGPSGCGKS
TTIALLERFY DAIAGSILVD GKDISKLNIN SYRSFLSLVS QEPTLYQGTI KENILLGIVE
DDVPEEFLIK ACKDANIYDF IMSLPEGFNT VVGSKGGMLS GGQKQRVAIA RALLRDPKIL
LLDEATSALD SESEKVVQAA LDAAARGRTT IAVAHRLSTI QKADVIYVFD QGKIVESGTH
SELVQKKGRY YELVNLQSLG KGH
