MFS1_TRIRC
ID MFS1_TRIRC Reviewed; 536 AA.
AC F2SH39;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=MFS-type efflux pump MFS1 {ECO:0000303|PubMed:31501141};
GN Name=MFS1 {ECO:0000303|PubMed:31501141}; ORFNames=TERG_01623;
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
RN [2]
RP IDENTIFICATION, FUNCTION, AND INDUCTION.
RX PubMed=31501141; DOI=10.1128/aac.00863-19;
RA Monod M., Feuermann M., Salamin K., Fratti M., Makino M., Alshahni M.M.,
RA Makimura K., Yamada T.;
RT "Trichophyton rubrum azole resistance mediated by a new ABC transporter,
RT TruMDR3.";
RL Antimicrob. Agents Chemother. 0:0-0(2019).
RN [3]
RP FUNCTION.
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 ketoconazole, miconazole and voriconazole (PubMed:31501141). Confers
CC also increased resistance chloramphenicol and thiamphenicol, suggesting
CC that it acts as a pleiotropic drug transporter with a broad substrate
CC spectrum (Ref.3). Finally, increases the tolerance to cycloheximide
CC when expressed in S.cerevisiae, but not in dermatophyte species
CC (PubMed:31501141, Ref.3). {ECO:0000269|PubMed:31501141,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31501141};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Is slightly over-expressed in strain TIMM20092, an azole-
CC resistant strain isolated in Switzerland.
CC {ECO:0000269|PubMed:31501141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGD85348.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG700649; EGD85348.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_003236897.1; XM_003236849.1.
DR AlphaFoldDB; F2SH39; -.
DR SMR; F2SH39; -.
DR STRING; 5551.XP_003236897.1; -.
DR EnsemblFungi; EGD85348; EGD85348; TERG_01623.
DR GeneID; 10373353; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR InParanoid; F2SH39; -.
DR Proteomes; UP000008864; 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 2: Evidence at transcript level;
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_0000448446"
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; 56978 MW; E5DF30B3FBEAD7DB CRC64;
MTEKGADGAD 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
