BMRP_CANAX
ID BMRP_CANAX Reviewed; 564 AA.
AC P28873;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Benomyl/methotrexate resistance protein;
GN Name=MDR1; Synonyms=BMR;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11651 / B792 / 171D;
RX PubMed=2062311; DOI=10.1007/bf00259685;
RA Fling M.E., Kopf J., Tamarkin A., Gorman J.A., Smith H.A., Koltin Y.;
RT "Analysis of a Candida albicans gene that encodes a novel mechanism for
RT resistance to benomyl and methotrexate.";
RL Mol. Gen. Genet. 227:318-329(1991).
CC -!- FUNCTION: Probable transporter. Confers resistance to benomyl and
CC methotrexate.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; X53823; CAA37820.1; -; Genomic_DNA.
DR PIR; S16304; S16304.
DR AlphaFoldDB; P28873; -.
DR ChEMBL; CHEMBL2007621; -.
DR TCDB; 2.A.1.2.6; the major facilitator superfamily (mfs).
DR VEuPathDB; FungiDB:C6_03170C_A; -.
DR VEuPathDB; FungiDB:CAWG_05053; -.
DR PHI-base; PHI:26; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..564
FT /note="Benomyl/methotrexate resistance protein"
FT /id="PRO_0000173431"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 60..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62930 MW; D39312C312BB18E8 CRC64;
MHYRFLRDSF VGRVTYHLSK HKYFAHPEEA KNYIIPEKYL ADYKPTLADD TSINFEKEEI
DNQGEPNSSQ SSSSNNTIVD NNNNNNNDVD GDKIVVTWDG DDDPENPQNW PTLQKAFFIF
QISFLTTSVY MGSAVYTPGI EELMHDFGIG RVVATLPLTL FVIGYGVGPL VFSPMSENAI
FGRTSIYIIT LFLFVILQIP TALVNNIAGL CILRFLGGFF ASPCLATGGA SVADVVKFWN
LPVGLAAWSL GAVCGPSFGP FFGSILTVKA SWRWTFWFMC IISGFSFVML CFTLPETFGK
TLLYRKAKRL RAITGNDRIT SEGEIENSKM TSHELIIDTL WRPLEITVME PVVLLINIYI
AMVYSILYLF FEVFPIYFVG VKHFTLVELG TTYMSIVIGI VIAAFIYIPV IRQKFTKPIL
RQEQVFPEVF IPIAIVGGIL LTSGLFIFGW SANRTTHWVG PLFGAATTAS GAFLIFQTLF
NFMGASFKPH YIASVFASND LFRSVIASVF PLFGAPLFDN LATPEYPVAW GSSVLGFITL
VMIAIPVLFY LNGPKLRARS KYAN
