GLIA_ASPFU
ID GLIA_ASPFU Reviewed; 542 AA.
AC E9R876; Q4WMJ2; Q5QCN3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=MFS gliotoxin efflux transporter gliA {ECO:0000303|PubMed:15979823};
DE AltName: Full=Gliotoxin biosynthesis protein A {ECO:0000303|PubMed:15979823};
GN Name=gliA {ECO:0000303|PubMed:15979823}; ORFNames=AFUA_6G09710;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=15979823; DOI=10.1016/j.femsle.2005.05.046;
RA Gardiner D.M., Howlett B.J.;
RT "Bioinformatic and expression analysis of the putative gliotoxin
RT biosynthetic gene cluster of Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 248:241-248(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=15707846; DOI=10.1016/j.fgb.2004.12.001;
RA Gardiner D.M., Jarvis R.S., Howlett B.J.;
RT "The ABC transporter gene in the sirodesmin biosynthetic gene cluster of
RT Leptosphaeria maculans is not essential for sirodesmin production but
RT facilitates self-protection.";
RL Fungal Genet. Biol. 42:257-263(2005).
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24847038; DOI=10.1093/mmy/myu007;
RA Wang D.N., Toyotome T., Muraosa Y., Watanabe A., Wuren T., Bunsupa S.,
RA Aoyagi K., Yamazaki M., Takino M., Kamei K.;
RT "GliA in Aspergillus fumigatus is required for its tolerance to gliotoxin
RT and affects the amount of extracellular and intracellular gliotoxin.";
RL Med. Mycol. 52:506-518(2014).
RN [5]
RP INDUCTION.
RX PubMed=24784729; DOI=10.1371/journal.pgen.1004336;
RA Schoberle T.J., Nguyen-Coleman C.K., Herold J., Yang A., Weirauch M.,
RA Hughes T.R., McMurray J.S., May G.S.;
RT "A novel C2H2 transcription factor that regulates gliA expression
RT interdependently with GliZ in Aspergillus fumigatus.";
RL PLoS Genet. 10:E1004336-E1004336(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26150413; DOI=10.1128/ec.00055-15;
RA Owens R.A., O'Keeffe G., Smith E.B., Dolan S.K., Hammel S., Sheridan K.J.,
RA Fitzpatrick D.A., Keane T.M., Jones G.W., Doyle S.;
RT "Interplay between gliotoxin resistance, secretion, and the
RT methyl/methionine cycle in Aspergillus fumigatus.";
RL Eukaryot. Cell 14:941-957(2015).
CC -!- FUNCTION: Efflux pump that provides the dual role of gliotoxin export
CC and self-protection by allowing the fungus to evade the harmful effect
CC of its own gliotoxin production (PubMed:15979823, PubMed:15707846,
CC PubMed:24847038, PubMed:26150413). Moreover, it contributes also to the
CC virulence through gliotoxin secretion (PubMed:24847038).
CC {ECO:0000269|PubMed:24847038, ECO:0000269|PubMed:26150413,
CC ECO:0000305|PubMed:15707846, ECO:0000305|PubMed:15979823}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is also under the control of the gipA
CC transcription factor (PubMed:24784729). {ECO:0000269|PubMed:24784729}.
CC -!- DISRUPTION PHENOTYPE: Increases the susceptibility to gliotoxin
CC (PubMed:24847038). Leads to complete deficient gliotoxin secretion but
CC still retains the ability to efflux bisdethiobis(methylthio)gliotoxin
CC (BmGT) (PubMed:26150413). Leads to increased survival of infected mice
CC (PubMed:24847038). {ECO:0000269|PubMed:24847038,
CC ECO:0000269|PubMed:26150413}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AY728089; AAV83489.1; -; Genomic_DNA.
DR EMBL; AY838877; AAW03302.1; -; Genomic_DNA.
DR EMBL; AAHF01000006; EAL88822.1; -; Genomic_DNA.
DR RefSeq; XP_750860.1; XM_745767.1.
DR AlphaFoldDB; E9R876; -.
DR SMR; E9R876; -.
DR EnsemblFungi; EAL88822; EAL88822; AFUA_6G09710.
DR GeneID; 3508165; -.
DR KEGG; afm:AFUA_6G09710; -.
DR VEuPathDB; FungiDB:Afu6g09710; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR InParanoid; E9R876; -.
DR OMA; ICAVANN; -.
DR OrthoDB; 627633at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IMP:AspGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..542
FT /note="MFS gliotoxin efflux transporter gliA"
FT /id="PRO_0000437732"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 542 AA; 57490 MW; 5145EDDC65002AAA CRC64;
MSRPSIEESK QELSSSPNDS VMGKDPAPEE EMQYPSGFAL SVIMAGLLAA IFLISLDTTI
VSTAIPRITD EFHTVADIGW YGSAFFLTLA SFQGTWGKIY RYFPLKLSFL AAVLLFEVGS
LICAVAKNSV TLIVGRAIAG IGAAGISSGS YTILAFSVHP RRRAAMTGAI GASFAVAAVA
GPLIGGAFTS HTTWRWCFWI NLPIGGVSAG LIAIFFKAPP QARAKDVPYK EILLQMDPSG
IVLLLGAILC FLLALQWGGS AKAWGNADVV GTLVGFGLLL IAFAINELWL QEKAMIPPRL
FKGQTILFSS LFTFFFSGSF YLLLYYLPTY FQSVKGASAS DSGVRTLPLV LGDGLFATLS
GAVLGIIGYY MPLLTLGGVL TTVASGLLYT LDLDSGANAW IGYQAMAGIG IGLAIQVPMM
ASQAVVRVED LSTVSAIVLF FQCMGGAIFV QAGQAAFTNK LVQEVQRHLP NISAARVTST
GATELQSEFH GHELQVILEA YVAGLKDAFI VAIVLAGIAT LLSFGSGWRS VKSKKEEPKA
QP
