MDR1_TRIT1
ID MDR1_TRIT1 Reviewed; 1567 AA.
AC F2RSQ6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=ABC multidrug transporter MDR1 {ECO:0000303|PubMed:27121717};
DE AltName: Full=Multidrug resistance protein 1 {ECO:0000303|PubMed:27121717};
GN Name=MDR1 {ECO:0000303|PubMed:27121717}; ORFNames=TESG_01875;
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818;
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 INDUCTION.
RX PubMed=27121717; DOI=10.1099/jmm.0.000268;
RA Martins M.P., Franceschini A.C.C., Jacob T.R., Rossi A.,
RA Martinez-Rossi N.M.;
RT "Compensatory expression of multidrug-resistance genes encoding ABC
RT transporters in dermatophytes.";
RL J. Med. Microbiol. 65:605-610(2016).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter that may be involved in
CC the modulation susceptibility to a wide range of unrelated cytotoxic
CC compounds. {ECO:0000250|UniProtKB:A0A059J0G5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + voriconazole(in) = ADP + H(+) + phosphate +
CC voriconazole(out); Xref=Rhea:RHEA:61912, ChEBI:CHEBI:10023,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61913;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46081, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61917;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-miconazole(in) + ATP + H2O = (R)-miconazole(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:61928, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82894, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61929;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-miconazole(in) + ATP + H2O = (S)-miconazole(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:61932, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82897, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61933;
CC Evidence={ECO:0000250|UniProtKB:F2SHL1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon exposure to griseofulvin and
CC itraconazole. {ECO:0000269|PubMed:27121717}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; GG698483; EGD94355.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RSQ6; -.
DR SMR; F2RSQ6; -.
DR EnsemblFungi; EGD94355; EGD94355; TESG_01875.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OrthoDB; 56980at2759; -.
DR Proteomes; UP000009172; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1567
FT /note="ABC multidrug transporter MDR1"
FT /id="PRO_0000447177"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1345..1365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1372..1392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1498..1518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 167..432
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 891..1134
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 927..934
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1567 AA; 174782 MW; EB6D7ADFFC3F0536 CRC64;
MASQPPQPPS GQPDTQYEEY QSEVITETTN RPTPAADVYE ITPTNDVMDD RYEHEHDDYE
SGAMYETVRT WSPQSRPELV RIASVFSRID SHPDVAPTTE DGGQLNRRDT LAGVKIGDPV
LDPTKPEFDF YKWARMFTHV MEKEGIKRNR TGVMFRNLTV LGSGSAVQYQ DTFLSPFAAP
FRPGELCGKG RNPEKVILHD FNGAIREGEL LMVLGRPGSG CSTFLKAICG ELHGLQKKKE
SIIHYNGVSQ HTFKKELRGE AVYSAEDEHH FPHLTVGQTL EFAAAARTPS KRVLGLSRKD
FSTHLARVMM SVFGLSHTYN TKVGDDYVRG VSGGERKRVS IAEIALSGAP ICCWDNSTRG
LDSATALEFT KALKIGSQVG GITQCLAIYQ ASQAIYDIFD KVIVLYEGRQ IFFGPTRIAK
QYFEEMGWYC PPRQTTADFL TSVTNPKERI AKEGYENRVP RTAVEFERYW KQSQNNKLLL
ADMDRFEAEY PLEEGHLEKL RETHGQAQAK HTASKSPYRI SVPMQVKLCT VRAYQRLWGD
KSSTIATNIS QIMMALIIGS LFFDTPQTTD GFFAKGSVIF FAILLNGLMS ITEINGLCKA
TDPIVPNAQR PIVVKHVNFA FYHAYSEALA GIVADIPIKF LLALVFNIII YFLGGLERSA
AKFFIFFLFT FITILTMSAI FRTLAAATKT IPQALALAGV MILALVIYTG FTLQPSYMHP
WFKWILYINP IAYAYEALLV NEVHGNRYRC ATPIPPYGSG TNFACAVAGA VPGEMSVSGD
AWVESSYDYS YAHIWRNLGI LLGFLAFFYF VYLVVSELNL SSASSAEFLV FRRGHLPKNF
QGSKDEEAAA GGVMHPNDPA RLPPTNTNGA AGETAPGGST VAVIPPQKDI FTWRNVTYDI
TIKGEPRRLL DNISGWVRPG TLTALMGVSG AGKTTLLDAL AQRTTMGVIT GDMLVNGRPL
DSSFQRKTGY VQQQDLHLET TTVREALRFS ADLRQPKSVS RKEKYEYVED VIKMLSMEDF
SEAVVGNPGE GLNVEQRKLL TIGVELAAKP QLLLFLDEPT SGLDSQSSWS IVTFLRKLAD
NGQAVLSTIH QPSGILFEQF DRLLFLAKGG RTVYFGDIGK NSETLLNYFE THGAEPCGPS
ENPAEYMLNI VGAGPSGKSK IDWPAVWKES EESRHVQQEL DRIQSETSKR NEGHGQSAEK
EPGEFAMPFT SQLYCVTTRV FQQYWRTPSY IWGKLLLGLT SALFIGFSFF LQNSSMAGLQ
NSLFSIFMLT TIFSSLVQQI MPRFVTQRDL FEVRERPSRA YSWKVFLLAN IIVEIPYQIL
LGIIAWASLF YPTFGAHLSS ERQGILLLYC VQFFIFASTF AQMIIAGLPD AETAGGIATT
MFGLMVTFNG VLQKPNALPG FWRFMWRVSP ITYTVGGLAA TSLHSREVKC AQNELAIFDP
PSGATCAQYL QKLVEAGAPG KLYNPMSTSQ CQYCPLSSGD QFLGGSEIHW SDRWRNFGIG
WAYIVFNIFA TVALYYLIRV RKSSGRPNRI ISVITYHLSQ FGTYCRAFIT GRKEKCPRKR
EQIGKIY
