ATRI_ASPFU
ID ATRI_ASPFU Reviewed; 1472 AA.
AC Q4WWW3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ABC multidrug transporter atrI;
GN Name=atrI {ECO:0000303|PubMed:26933209}; ORFNames=AFUA_3G07300;
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 [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 [2]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=26933209; DOI=10.1093/mmy/myw005;
RA Meneau I., Coste A.T., Sanglard D.;
RT "Identification of Aspergillus fumigatus multidrug transporter genes and
RT their potential involvement in antifungal resistance.";
RL Med. Mycol. 54:616-627(2016).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the basal
CC level of azole susceptibility (PubMed:26933209). Confers resistance to
CC fluconazole, itraconazole and voriconazole (PubMed:26933209).
CC {ECO:0000269|PubMed:26933209}.
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:26933209};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504;
CC Evidence={ECO:0000269|PubMed:26933209};
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:26933209};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913;
CC Evidence={ECO:0000269|PubMed:26933209};
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:26933209};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is increased in clinical azole-resistant
CC isolates. {ECO:0000269|PubMed:26933209}.
CC -!- DISRUPTION PHENOTYPE: Exhibits enhanced susceptibility to itraconazole,
CC however voriconazole susceptibility is less affected.
CC {ECO:0000269|PubMed:26933209}.
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; AAHF01000002; EAL92840.1; -; Genomic_DNA.
DR RefSeq; XP_754878.1; XM_749785.1.
DR AlphaFoldDB; Q4WWW3; -.
DR SMR; Q4WWW3; -.
DR STRING; 746128.CADAFUBP00004094; -.
DR EnsemblFungi; EAL92840; EAL92840; AFUA_3G07300.
DR GeneID; 3512111; -.
DR KEGG; afm:AFUA_3G07300; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q4WWW3; -.
DR OMA; IMPRFVT; -.
DR OrthoDB; 56980at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
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; 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; IPR043926; ABCG_dom.
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; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 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..1472
FT /note="ABC multidrug transporter atrI"
FT /id="PRO_0000445101"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1168..1188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1204..1224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1282..1302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1337..1357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1433..1453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 134..384
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 828..1070
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 864..871
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1472 AA; 164612 MW; 88B4FFB72AA0C45E CRC64;
MRRSNVVPVH SLTSSTNTGR DSRGEKYDEL TPVATRRASI SPDEARYLTQ LASRDNAVSR
VSTVADISLD DPALNPENKD FDLYKWLRKV VHVLNEEGVP RKEASIFFQH LRVSGTGAAL
QLQKTVADII TAPFRRETWN FRNKTSKTIL HDFNGMLHSG ELLIVLGRPG SGCSTFLKTL
SGELHGLNVD EKTVLHYSGI PQSTMIKEFK GEVVYNQEVD KHFPHLTVGQ TLEFAAAVRT
PSKRLGGMSR NEYAQMMTKV VMAVFGLSHT YNTKVGNDTV RGVPGGERKR VSIAEMALAG
APLAAWDNST RGLDSATALK FVESLRLAAD LNSSAHAVAI YQASQAIYDL FDKAVVLYEG
RQIYFGPASK AKAFFERQGW FCPPRQTTGD FLTSVTNPIE RQARPGMESQ VPRTAAEFEA
YWLESEEYKE LQREMAAFQG ETSSQGNEKL LEFQQRKRLA QASHTRPKSP YLLSIPMQIK
LNTKRAYQRV WNERTSTMTT FIGNTILALI VGSVFYGTPT ATAGFYAKGA TLFYAVLLNA
LTAMTEINSL YSQRPIVEKH ASFAFYHPAT EAIAGVVSDI PVKFLMAIAF NIILYFLSGL
RREPSQFFIY FLITFIIMFV MSAVFRTMAA ITRTVSQAMT LAGVLILMLV IYTGFVVPVN
YMHPWFKWIH YLNPIFYAFE ILIANEFHGR EFTCSQFIPV YPNLPGDSFV CSSRGAVAGR
RTVSGDAYIE ASYSYSYSHV WRNFGILIAF LIGFMVIYFV ATELNSATTS SAEVLVFRRG
HEPAHLKNGH EPGADEEAGA GKTVVSSSAE ENKQDQGITS IPPQQDIFTW RDVVYDIEIK
GEPRRLLDHV SGWVKPGTLT ALMGVSGAGK TTLLDVLAHR TTMGVITGDM FVNGKPLDSS
FQRKTGYVQQ QDLHLETATV RESLRFSAML RQPASVSKEE KYAYVEEVIK MLNMEDFAEA
VVGVPGEGLN VEQRKLLTIG VELAAKPKLL LFLDEPTSGL DSQSSWAICN FLRKLADAGQ
AILCTIHQPS AILFEQFDQL LFLARGGKTV YFGPIGENSQ TLLKYFESHG PRRCGDQENP
AEYMLEVVNA GTNPRGENWF DLWKASKEAA GVQAEIDRIH ESKRGEAESK DSTNPKDREH
EEFAMPFFKQ LPIVTVRVFQ QYWRLPMYIA AKMMLGICAG LFIGFSFFKA DTSLQGMQNV
IFSVFMLCAI FSSLVQQIIP LFITQRALYE VRERPSKTYS WKAFMIANII VEIPYQILMG
ILVFGCYYYA VNGVQSSDRQ GLVLLFCIQF FIYASTFADF VIAALPDAET AGAIVTLQFS
MALTFNGVMQ TPEALPGFWI FMYRVSPFTY WVGGMAATQL HGRAVKCSAA ETAIFNPPSG
LTCQEYMADY MAVAPGHLSN PNATSSCEFC SLSVADQYLA SVNIYWSERW RNFGIFWAYV
VFDIAVAVML YYCFRVKKWN FSFGKRKKSK AA
