ATRA_EMENI
ID ATRA_EMENI Reviewed; 1466 AA.
AC A0A1U8QT10; C8VLI2; Q5AS02;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=ABC multidrug transporter atrA;
GN Name=atrA {ECO:0000303|PubMed:19146970}; ORFNames=AN8928;
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, AND INDUCTION.
RX PubMed=9180695; DOI=10.1007/s004380050434;
RA Del Sorbo G., Andrade A.C., Van Nistelrooy J.G., Van Kan J.A., Balzi E.,
RA De Waard M.A.;
RT "Multidrug resistance in Aspergillus nidulans involves novel ATP-binding
RT cassette transporters.";
RL Mol. Gen. Genet. 254:417-426(1997).
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 basal
CC level of drugs susceptibility, including antibiotics, azole fungicides
CC and plant defense toxins. {ECO:0000269|PubMed:9180695}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9180695};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is strongly increased by imazalil
CC (PubMed:9180695). Expression is also strongly increased in the presence
CC of hygromycin and 4-nitroquinoline oxide (4-NQO) (PubMed:11872487).
CC Curiously, expression is repressed in the presence of camptothecin,
CC imazalil and itraconazole (PubMed:11872487).
CC {ECO:0000269|PubMed:11872487, ECO:0000269|PubMed:9180695}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) 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; BN001307; CBF84638.1; -; Genomic_DNA.
DR EMBL; AACD01000165; EAA64062.1; -; Genomic_DNA.
DR RefSeq; XP_682197.1; XM_677105.1.
DR AlphaFoldDB; A0A1U8QT10; -.
DR SMR; A0A1U8QT10; -.
DR STRING; 162425.CADANIAP00007936; -.
DR EnsemblFungi; CBF84638; CBF84638; ANIA_08928.
DR EnsemblFungi; EAA64062; EAA64062; AN8928.2.
DR GeneID; 2868201; -.
DR KEGG; ani:AN8928.2; -.
DR VEuPathDB; FungiDB:AN8928; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OMA; TGFVIRI; -.
DR OrthoDB; 56980at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 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; 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 PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1466
FT /note="ABC multidrug transporter atrA"
FT /id="PRO_0000449463"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1168..1188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1195..1215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1283..1303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1312..1332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1434..1454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 135..386
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 829..1071
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 865..872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1466 AA; 162817 MW; 8A11334F185D1FA3 CRC64;
MGVPDELPPG SSETDTIVSS SQPTNRSPMD LISEAESLNL RRIATNQSKA QCRPGSAAVP
SHDNPPNDDL EDATLDPNSA SFSLEKWLRA AVSDASQHGL STPSGGILFR NLTVSGSGSA
LQLQPTVGSV LTAPLRFASL LRHRRIEPRR ILHGFDGVMK TGELLLVLGR PGAGCSTFLK
TVCGETNGLH IDADSVLHYN GVSQQRMMKE FKGEVVYNQE VDKHFPHLTV RQTLEFAAAA
RTPAHRFQNM SRDEFASYAA SVVMAIFGLS HTHNTKVGND FVRGVSGGER KRVSIAEMAL
AMTPFAAWDN SSRGLDSATA LKFVQALRLS ADLAGAAHAV AIYQASQSIY EVFDKVTVLY
EGRMIFFGPT GTAKEYFERM GWVCPARQTT GDFLTSITNP LERKARAGME DVVPKTPKDF
EIYWRQSPEY KTLLGEMTEF ETQHPTGNDE QASAELRARK ENSQSRNSRA ASPYILSIPM
QIKLNTKRAY QRIWNDMSST MSTVVGQIVI ALITGSVFYD SPNTTAGFQS KGGTLFYAVL
LNALTAMSEI TSLYSQRPIV EKQASYAFYH PATEAIAGVV SDVPVKFLLA VAFNVIMYFL
ANLRREPAQF FIYFLMSFTV MFVMSAVFRT MAAVTKNAAQ AMGLAGVLML ALVVYTGYVL
PVPSMHPWFE WIHYLNPIYY AFEAMIANEF HGRDFDCIAF VPSYADLDGD SFSCSSLGSV
AGERMVSGDS YINFNYTYTY SHVWRNFGVL LAFLIGFMAI YFLASELNSS TTSTAEALVF
RRGHVPEYMR PGYTRPTDEE KAVTQSDIKP SSPSPTNTDL PLPPQRDIFT WKDISYDIEI
KGEPRRLLDD VSGWVKPGTL TALMGVSGAG KTTLLDVLAH RTTMGVITGD MFVNGKGLDA
SFQRKTGYVQ QQDLHLETAT VRESLRFSAL LRQPASVSIR EKHDYVESVI EMLGMGDFAE
AVVGTPGEGL NVEQRKLLTI GVELAAKPKL LLFLDEPTSG LDSQSSWAIC TFLRKLADSG
QAVLCTIHQP SAILFQEFDQ LLFLAKGGKT VYFGPIGPNS RTLLDYFESN GARKCDEAEN
PAEYMIEVVN AEVNDRGTDW FDVWKGSKEC QAVKEEIERI HEKKRGTAGA IEETDDGSTK
SEFAMPFWFQ LYVVTVRVFQ QYWRMPEYII SKGALAIVAG LFIGFSFYDA KTSLAGLQTL
VFSLFMVCAL FAPLVNQIMP LFITQRSLYE VRERPSKAYS WKAFLIANIL VEIPYQVLMG
ILTFVCYYYP VVGSSQGPDR EGLVLLFCIQ FYVYASTFAH MCIAAMPNAE TASPIVILLF
SMCLTFCGVM QPPDALPGFW IFMYRVSPFT YWVAGMATTQ VHGREVVCGE NELSIFDPPT
NQTCGQYMER YISVAGGQVL NPSATAGCEY CSLTVADEYL AASQIYWSDR WRNFGLIWVY
IGFNIFVATA VYYLFRVKKW NGRRKK
