ID   MFS2_TRIRC              Reviewed;         595 AA.
AC   F2T0J9;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=MFS-type efflux pump MFS2 {ECO:0000303|PubMed:31501141};
GN   Name=MFS2 {ECO:0000303|PubMed:31501141}; ORFNames=TERG_08336;
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).
CC   -!- FUNCTION: MFS-type efflux pump involved in the modulation
CC       susceptibility to fluconazole and voriconazole, 2 azoles with similar
CC       molecular structure. {ECO:0000269|PubMed:31501141}.
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, and azole-
CC       resistant strain isolated in Switzerland.
CC       {ECO:0000269|PubMed:31501141}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC       Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily. {ECO:0000305}.
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DR   EMBL; GG700660; EGD92121.1; -; Genomic_DNA.
DR   RefSeq; XP_003231249.1; XM_003231201.1.
DR   AlphaFoldDB; F2T0J9; -.
DR   SMR; F2T0J9; -.
DR   EnsemblFungi; EGD92121; EGD92121; TERG_08336.
DR   GeneID; 10377525; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_008455_11_6_1; -.
DR   InParanoid; F2T0J9; -.
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..595
FT                   /note="MFS-type efflux pump MFS2"
FT                   /id="PRO_0000448447"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   595 AA;  64811 MW;  F95D506B36C35650 CRC64;
     MADANAMEGE KSIPTKIPHW RQVTDPGAVT PEIINYPYPG SGTEADPYLV QWIPSDPRNP
     MNYSAVKKWS ITFVVAIATL AVALISSAYT GGAIEIAQEF HADAEVITLG VSLFVLGFAI
     GPLIWAPMSE LFGRQLLFFG TYLALTAFNA GAAGSPNMAT LLVLRFFAGS FGSSPLTNAG
     GVIADMFPAS HRGLAMGIFA IAPFLGPVLG PVIGGFLGES AGWRWVEGFL AIFSGVVWII
     GSIFLPETYP PVLLRKRAQR LSKLTGKVYA SRMDIEQGKL SIGQAFKTAL MRPWILLFRE
     PIVLLLSTYM AIVYGTLYML FSAFPVVYQQ HRGWSPGIGG LAFLGVLGGI LAAMVINLLD
     NKRYAKVSKE YNGFAPPEER LPVAIIGGIA IPIGLFWFAW TNGPQIHWIV SIIASAPFGF
     GMVLVFLSLM NYLIDAYTIY AASVLAANSV LRSLFGAAFP LFTRYMYQNL GIHWASTIPA
     FLALACVPFP FLFYIYGANI RKRCKFAGEA DAFMQKLMQA NSAHLESDLE VSEAGPIPRR
     NSLEAREVLD RIQSARSGLT RTRTAATVEY EGNPYDIDRV NTGLSRVSTT NSQTR