ID   ATRH_ASPOR              Reviewed;        1481 AA.
AC   Q2UD41;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=ABC multidrug transporter atrH {ECO:0000303|PubMed:30011258};
GN   Name=atrH {ECO:0000303|PubMed:30011258}; ORFNames=AO090012000328;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=30011258; DOI=10.1080/09168451.2018.1497941;
RA   Miura D., Sugiyama K., Ito A., Ohba-Tanaka A., Tanaka M., Shintani T.,
RA   Gomi K.;
RT   "The PDR-type ABC transporters AtrA and AtrG are involved in azole drug
RT   resistance in Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 82:1840-1848(2018).
CC   -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the basal
CC       level of azole susceptibility. {ECO:0000269|PubMed:30011258}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30011258};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is slightly up-regulated in the presence of
CC       miconazole. {ECO:0000269|PubMed:30011258}.
CC   -!- DISRUPTION PHENOTYPE: Does not significantly affect miconazole
CC       susceptibility. {ECO:0000269|PubMed:30011258}.
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; AP007161; BAE60524.1; -; Genomic_DNA.
DR   RefSeq; XP_001727363.1; XM_001727311.2.
DR   AlphaFoldDB; Q2UD41; -.
DR   SMR; Q2UD41; -.
DR   STRING; 510516.Q2UD41; -.
DR   EnsemblFungi; BAE60524; BAE60524; AO090012000328.
DR   GeneID; 5987837; -.
DR   KEGG; aor:AO090012000328; -.
DR   VEuPathDB; FungiDB:AO090012000328; -.
DR   HOGENOM; CLU_000604_35_0_1; -.
DR   OMA; SIFHWQD; -.
DR   Proteomes; UP000006564; Chromosome 4.
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..1481
FT                   /note="ABC multidrug transporter atrH"
FT                   /id="PRO_0000449471"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        758..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1174..1194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1210..1230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1249..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1298..1318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1327..1347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1358..1378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1446..1466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          134..396
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          838..1081
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         874..881
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1481 AA;  166662 MW;  6BEB048C18E9C2E4 CRC64;
     MALPREERSL HGHANIHVNQ TTGPAIDKAE SSDTIGADSE DGIEQEGQAK ITTLARTLSR
     ISQTNSGTEG LNPFLNTSDP ELDPNSDQFN SRKWTKTLLH ITSRDPERYP RRTAGVSFRN
     LNAFGYGTAA DYQATVSNVW LKAAGWLRGL FGNGNKVRID ILRNFEGFVN SGEMLVVLGR
     PGSGCSTFLK TIAGETHGLW LDKGTDIQYQ GISWDEMHSR FRGEVMYQAE TEIHFPQLTA
     GDTLLFAAKA RAPANRLPGV SRDQYATHMR DVVMAMLGLT HTMNTLVGNE FIRGVSGGER
     KRVSIAETTL CGSPLQCWDN STRGLDSSTA LEFVKNLRLS TDYTGSTAIV AIYQASQAIY
     DVFDKVIVLY EGRQIYFGRA RDAKRFFIEM GFDCPERQTT GDFLTSLTSP TERLVRKGYE
     HLVPRTPDEF AARWRDSLER KQLLADIEAF QNEFPLGGSK KEEFSRSRAA EKAKNTRASS
     PYTLSYSMQI KLCLQRGFLR LKGDMSMTLS TVIGNSILAL IISSVFYNLN ETTDSYFSRG
     ALLFFAILLN AFASALEMLT LWQQRPIVEK HDKYALYHPS AEAISSLIVD LPAKAPVSIV
     FNLILYFMTN LRRTPGHFFV FYLFSVTTTL TMSNVFRWIA AVSRSLAQAE VPASIFMMIL
     MIYTGFTIPV RDMHPWFRWL NYINPIAYSF ESLMINEFAG RKFHCATYVP SGPGYDNAPL
     DSKICSGKGA VAGQDYIDGD RYLEVAFEYY PSHLWRNFGI LLGFLFFSLV AYIVASELVR
     AKPSKGEILV FPRGKIPAFA KKVHREADPE DVLTSEKLKV GSEQDDHVGA IVKQTSIFHW
     QDVCYDIKIK GQDRRILDHV DGWVKPGTLT ALMGVTGAGK TSLLDVLANR VTMGVITGEM
     LVDGRMRDDS FQRKTGYVQQ QDLHLETSTV REALIFSALL RQPASTPRKE KLAYVEEVIK
     MLNMEEYAEA VVGVLGEGLN VEQRKRLTIG VEIAAKPDLL LFFDEPTSGL DSQTAWSICS
     LMRKLVDHGQ AILCTIHQPS AILMQQFDRL LFLAKGGKTV YFGDLGPNMR TLIKYFEDKG
     SPKCPPNANP AEWMLEVIGA APGSRADQDW SDVWKHSRER AQVQQELLQM KQELLQRPQP
     PRTAGYGEFA MPLWAQFFIC LQRVFQQYWR CPSYIYAKAA MCIIPPLFIG FTFWREPTSI
     QGMQNEMFSI FMLLVIFPNL VQQMMPYFAM QRSLYEVRER PSKAYSWKAF MLASIVVELP
     WNMLMAVPAY FCWYYPIGLF RNAYPTDSVT ERGGTMFLLV LIFMLFTSTF SSMMIAGIDH
     PETASNIAQL MFSMCLIFCG VLASPDVLPR FWIFMWRASP FSYLVGSVLA VGIAGAPVHC
     SDIEVLHIPP PGGQNCSGYL EAFTTMAKST LLNPEADSDC QVCSLSTTDQ FLAGVHIKYS
     ELWRNVGILF VYIVFNTVAA VFLYWLVRVP KKRALKKAKK E