MFS1_ARTBC
ID MFS1_ARTBC Reviewed; 536 AA.
AC D4AXV8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=MFS-type efflux pump MFS1 {ECO:0000303|Ref.2};
GN Name=MFS1 {ECO:0000303|Ref.2}; ORFNames=ARB_01027;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX DOI=10.3390/jof7070542;
RA Yamada T., Yaguchi T., Salamin K., Guenova E., Feuermann M., Monod M.;
RT "MFS1, a pleiotropic transporter in dermatophytes that plays a key role in
RT their intrinsic resistance to chloramphenicol and fluconazole.";
RL J. Fungi 7:542-542(2021).
CC -!- FUNCTION: MFS-type efflux pump involved in the modulation
CC susceptibility to azoles, including fluconazole, itraconazole,
CC miconazole and voriconazole (Ref.2). Confers also increased resistance
CC chloramphenicol and thiamphenicol, suggesting that it acts as a
CC pleiotropic drug transporter with a broad substrate spectrum (Ref.2).
CC Finally, increases the tolerance to cycloheximide when expressed in
CC S.cerevisiae, but not in dermatophyte species (Ref.2).
CC {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|Ref.2}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased tolerance to the azoles
CC fluconazole, itraconazole, voriconaole, miconazole, as well as to the
CC antibiotics chloramphenicol and thiamphenicol. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE32136.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000017; EFE32136.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_003012776.1; XM_003012730.1.
DR STRING; 663331.D4AXV8; -.
DR EnsemblFungi; EFE32136; EFE32136; ARB_01027.
DR GeneID; 9522854; -.
DR KEGG; abe:ARB_01027; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OMA; WALNAYN; -.
DR Proteomes; UP000008866; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..536
FT /note="MFS-type efflux pump MFS1"
FT /id="PRO_0000454038"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 536 AA; 57066 MW; E5DF3453EBE0EC4B CRC64;
MTEKDTDGAD GLTKAKSNAV SEDYETVNHV TGLKLAVIVT GLCLSVLLVA LDNTIIATAI
PKITDQFHAL EDIGWYGSSY LLTICAFQLI FGKIYTFFPV KWVFLIAITI FEIGSAICGA
APNSTALIIG RAVAGIGSAG IFSGALIIIA YSIPLEKRPA YTGAIGGMYG IASVAGPLMG
GAFTDHISWR WCFYINLPIG AVTILSILIF LKHPKQKLDN NQTWKARLLK LDPIGTAFFM
PSIICLLLAL QWGGTKYPWN NGRIIALFVV FAVLISGFIY FQIRGGDSAT VPPRILKKRS
IASGAFFLFT IGSAFFIMVY YLPIWFQAIK GASATSSGIM NIPMVLSLVV LSIASGITVT
AIGYYAPLYY VSTVLTSIGA GLLTTFTTET SKGKWIGYQI IFGAGVGTGL QLSIIAAQAV
LPLEDVAVGT VIMMFCQTLG GALFVSVGQN VFTNLLVKGV VNAAPGLDPQ VVLRVGATQL
KNMIPPQFLD GVQVAYNDAL TKTWYVATAL AALSVIGSVG MEWKSVKGKK IEPAAA
