ABCF_ASPFU
ID ABCF_ASPFU Reviewed; 1471 AA.
AC Q4WDV4;
DT 02-JUN-2021, 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 F {ECO:0000303|PubMed:32209680};
GN Name=abcF {ECO:0000303|PubMed:32209680}; ORFNames=AFUA_5G00790;
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=32209680; DOI=10.1128/mbio.00338-20;
RA Esquivel B.D., Rybak J.M., Barker K.S., Fortwendel J.R., Rogers P.D.,
RA White T.C.;
RT "Characterization of the efflux capability and substrate specificity of
RT Aspergillus fumigatus PDR5-like ABC transporters expressed in Saccharomyces
RT cerevisiae.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter that shows a strong
CC substrate specificity for the azole class of drugs such as lotrimazole
CC (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC),
CC posaconazole (POS), econazole (ECON), metconazole (MET), miconazole
CC (MCZ), prochloraz (PCLZ), and tebuconazole (TEBZ).
CC {ECO:0000269|PubMed:32209680}.
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:32209680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917;
CC Evidence={ECO:0000269|PubMed:32209680};
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:32209680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504;
CC Evidence={ECO:0000269|PubMed:32209680};
CC -!- ACTIVITY REGULATION: The efflux inhibitor FK506 impairs the transport
CC activity. {ECO:0000269|PubMed:32209680}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:32209680};
CC Multi-pass membrane protein {ECO:0000255}.
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; AAHF01000011; EAL86223.1; -; Genomic_DNA.
DR RefSeq; XP_748261.1; XM_743168.1.
DR AlphaFoldDB; Q4WDV4; -.
DR SMR; Q4WDV4; -.
DR STRING; 330879.Q4WDV4; -.
DR EnsemblFungi; EAL86223; EAL86223; AFUA_5G00790.
DR GeneID; 3505690; -.
DR KEGG; afm:AFUA_5G00790; -.
DR VEuPathDB; FungiDB:Afu5g00790; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q4WDV4; -.
DR OMA; HFANANT; -.
DR OrthoDB; 37708at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
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; IPR017871; ABC_transporter-like_CS.
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; 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 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..1471
FT /note="ABC multidrug transporter F"
FT /id="PRO_0000452659"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1167..1187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1201..1221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1252..1272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1288..1308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1326..1346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1441..1461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 133..387
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..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..40
FT /note="Basic and acidic 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 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1471 AA; 164620 MW; D0435B1E78046C72 CRC64;
MALNSTDNRW STGEDTPSEA QLPDGEERLD AAPDEKVTAE DIDRRLTNLV RKISAQSRRS
HHSFLFGAGE NSSLNPQSPS FDARKWARAF YNARYRQDDG HPPRVVGVAF KNLNVFGYGS
PVDYQMSVGN ALLKVPTMVR QALGGGKQRV DILHDVEGLV LPGEQLCVLG PPGSGCSTFL
RTIAGETHGL NVDAASYINY HGISPKQMST AFRGEAIYTA EVDAHFPMLS VGDTLYFAAL
ARAPQVIPGG LSRQEYAKHL RDVIMAMFGI GHTINTRVGN DFVRGVSGGE RKRVTIAEAA
LGYSPLQCWD NSTRGLDSAN AVEFCRTLRT QSDVFGITSC VAIYQAPQAA YDLFDKVLVL
YEGWQIYFGA AHEAQAYFEQ LGFQCPESQT TADFLTSMCS PAERIVKPGF EHMAPRTPEE
FAQRWKESPQ RQSLLHAIEK YSTEHPLDGP DLHQFALSRR AEKSHRQREK SPYTLSYRGQ
VKLCLWREWQ RLKNDPSVTL AMLIGNFFEA LIIASIFYNL TGDTSSFYYR GALLFMMVLL
NAFASVLEIL TLYEKRTIVE KQSRYAYYHP SAEALSSFIM SLPYKFVNSS LVNLTLYFMS
NLRREPGPFF FFLLISTSMM LAMSMFFRWF ASLTKTIDQA LAPSSIILLA LVLYTGFTIP
VSYMRGWASW IRWLNPVSYG FEAVMINEFH GREFPCSSFV PSGPGYEDVS RTQRVCSTVG
ATSGSDVVSG DVFVRSSYGY VNSHRWRNFG IIIAMTVFLA VCHFVTTELV ASKRSKGEVL
VFRRGSAHIA RAKQGQRDEE QPSASAVPSE KYSEAPTPVE GVETQTSIFH WEDVCYDVKI
KNETRRILDH VDGWIKPGTL TALMGVSGAG KTTLLDVLAS RTTVGVVTGE TLVDGRQRDS
SFQRKTGYVQ QQDLHLATTT VREALEFSAL LRQPPQYSRE EKLEYVEKVI DLLHMRDYAD
AIVGVPGEGL NVERRKRLTI GVELAARPKL LLFLDEPTSG LDSQTSWSIC NLMETLTRNG
QAILCTIHQP SAMLFQRFDR LLLLAKGGKT VYFGEIGSGA RTLMDYFVRN GGPPCPKGAN
PAEHMLEVIG AAPGAHTDID WPAVWRNSPE YQQVRQELSR LRQLASQPSS VHSDDPSSYS
EFAAPFPAQL GQVGRRVFQQ YWRTPSYLYS KAILTVGSSI FIGFSFFKGD NTAQGLQNQV
FGVFVFLFVV IQLIFQIIPT FVTQRTLYES RERQSKTYSW QAFVLSNIAV EFAWNTIAAV
LCFLAWFYPV GLYRNAEYTD SVHSRSTLVF LIIWATFLFA SSFAHLLIAG VESAELASAL
ANIMGIMMYA FCGILAGPHA LPGFWIFMYR VNPFTYLVSG LLSASLGDAP MHCAANEFLA
FSPPANRTCG EYMEDYMALA GGYLLDSAAR GDEQCQYCRV DNTSQYLRNF SIDFATRWRD
FGLLWVYVAV NTFGAVFLYW LCRVPKGKKR L
