ATRF_ASPFN
ID ATRF_ASPFN Reviewed; 1535 AA.
AC B8NDS8;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=ABC multidrug transporter atrF {ECO:0000303|PubMed:23886435};
GN Name=atrF {ECO:0000303|PubMed:23886435}; ORFNames=AFLA_055690;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP INDUCTION.
RX PubMed=23886435; DOI=10.1016/j.diagmicrobio.2013.04.022;
RA Natesan S.K., Lamichchane A.K., Swaminathan S., Wu W.;
RT "Differential expression of ATP-binding cassette and/or major facilitator
RT superfamily class efflux pumps contributes to voriconazole resistance in
RT Aspergillus flavus.";
RL Diagn. Microbiol. Infect. Dis. 76:458-463(2013).
RN [3]
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30126960; DOI=10.1128/aac.01216-18;
RA Ukai Y., Kuroiwa M., Kurihara N., Naruse H., Homma T., Maki H., Naito A.;
RT "Contributions of yap1 mutation and subsequent atrF upregulation to
RT voriconazole resistance in Aspergillus flavus.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter involved in the basal
CC level of azole susceptibility (PubMed:30126960). Confers resistance to
CC voriconazole (PubMed:30126960). {ECO:0000269|PubMed:30126960}.
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:0000305|PubMed:30126960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913;
CC Evidence={ECO:0000305|PubMed:30126960};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30126960};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is highly up-regulated in the presence of
CC miconazole (PubMed:23886435, PubMed:30126960). Expression is controled
CC by the AP-1-like transcription factor yap1 (PubMed:30126960). The
CC promoter contains a putative Yap1 response element YRE (5'-TTAGTAA-3')
CC from -462 to -456 relative to the start codon (PubMed:30126960).
CC {ECO:0000269|PubMed:23886435, ECO:0000269|PubMed:30126960}.
CC -!- DISRUPTION PHENOTYPE: Leads to voriconazole sensitivity of the yap1-
CC mutated voriconazole-resistant strain. {ECO:0000269|PubMed:30126960}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED51306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963477; EED51306.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002378313.1; XM_002378272.1.
DR AlphaFoldDB; B8NDS8; -.
DR SMR; B8NDS8; -.
DR STRING; 332952.B8NDS8; -.
DR EnsemblFungi; EED51306; EED51306; AFLA_055690.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_4_1; -.
DR Proteomes; UP000001875; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
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; 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; 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; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1535
FT /note="ABC multidrug transporter atrF"
FT /id="PRO_0000449469"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1212..1232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1246..1266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1295..1315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1320..1340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1384..1406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1477..1497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1503..1523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 185..427
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 879..1117
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 915..922
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1535 AA; 171877 MW; 6CD4622C9D254B01 CRC64;
MADDHRQPEA SSNTAANPYN HPVASEHTLG SLNTTSTSET DASADADARW GERNQGDPVS
RRGAMEEFEE MRREVTKLSL HRTRSAKDAR RRSRAEGRDE EKALEDEQAS STDEYRGGFD
LNEFLMGGHL ERRTTAGEPA KKVGVAFKNV TVKGVETGAS FVRTLPDAVV GTFGPDLYKI
ICRFVPALHF GKRPPVRDLL HDFSGAVREG EMMLVLGRPG AGCSTFLKTI ANDREAFAGV
EGEVSYGGLS AEEQHKHFRG EVNYNQEDDQ HFPNLTVWQT LKFSLINKTK KHDKASIPII
IDALLKMFGI THTKNTLVGN EYVRGVSGGE RKRVSIAETL ATKSSVVCWD NSTRGLDAST
ALDYAKSLRI MTDVSKRTTL VTLYQAGESI YELMDKVLVI DAGRMLYQGP ANEAKQYFVD
LGFYCPEQST TADFLTSLCD PNARQFQPGR EASTPKTAEE LEAIFKQSEA YKQIWNEVCA
YEKLLQDTNQ EDTRRFQKTV AQSKSKTVSK KSPYTVSIVR QVAACVQREF WLLWGDKTSL
YTKYFIIVSN GLIVSSLFYG ESLDTSGAFS RGGALFFSIL FLVLQLTELM PAVSGRGIVA
RHKDYAFYRP SAVAIARVVV DFPAIFCMVV PFTIIVYFMT GLDVEASKFF IYFLFVYTTT
FCITSLYRMF AALSPTIDDA VRFAGIALNV LILFVGYVIP KQGLIDGSIW FGWLFYVNPL
SYSYEAVLTN EFSNRVMSCA PSQLVPQGPG VDPRYQGCAL TGSELGKADV AGSRYLQESF
QFTRHHLWRN FGVVIAFTVL YLLVTVIAAE VLSFVGGGGG ALVFKKSKRS TKLKAQNGKG
NDEEQVQNTG DNAALSRGEA KSSSSGEAMQ RLSASDRVFT WSNVEYTVPY GNGTRKLLNG
VNGYAKPGLM IALMGASGAG KTTLLNTLAQ RQKMGVVTGD MLVDGHPLGT EFQRGTGFCE
QMDLHDNTAT IREALEFSAI LRQDRNTPRQ EKLDYVDQII DLLELEDIQD AIIGSLNVEQ
KKRVTIGVEL AAKPSLLLFL DEPTSGLDSQ AAFSIVRFLK KLSQAGQAIL CTIHQPSSML
IQQFDMVLAL NPGGNTFYFG PIGPEGRDVI KYFADRGVVC PPSKNVAEFI LETAAKATKK
DGRAIDWNEE WRNSEQNRRI LDEIQQIREE RSKIPIADKG VEYEFAAPTW TQTVLLTERL
FRQYWRDPSY YYGKLFVSVI IGIFNGFTFW MLDNSISSMQ NRMFSIFLII LIPPIVLNSI
VPKFYINRAL WEAREYPSRI YGWFAFCTAN VVCEIPMAIV SALIYWLLWY YPVGFPTDSS
SAGYVFLMSM LFFLFQASWG QWICAFAPSF TVISNVLPFF FVMVNLFNGI VRPYKDYPVF
WKYWMYYVNP VTWWLRGVIS SVFPSVDIEC ASKEATHFDP PPGSTCQQYA GNFVSNIAGV
GYLVNPDATE DCQYCPFANG TEYMHTLNVH DGDKWRCFGI FLAFVIINWA LVYFFIYTVR
VRGWSFGMGY LFGGVGVMIE GVKKVFSKKS EKEQN
