MDR4_TRIRC
ID MDR4_TRIRC Reviewed; 1366 AA.
AC P0CU83;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=ABC multidrug transporter MDR2 {ECO:0000303|PubMed:27121717};
DE AltName: Full=Multidrug resistance protein 2 {ECO:0000303|PubMed:27121717};
GN Name=MDR4 {ECO:0000303|PubMed:27121717}; ORFNames=TERG_07801;
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 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).
RN [3]
RP FUNCTION.
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: Pleiotropic ABC efflux transporter that may be involved in
CC the modulation susceptibility to a wide range of unrelated cytotoxic
CC compounds (Probable). Does not acts as an efflux pump for azoles,
CC including fluconazole, itraconazole, ketoconazole, miconazole and
CC voriconazole, nor does it modulate susceptibility to cycloheximide
CC (PubMed:31501141). {ECO:0000269|PubMed:31501141, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31501141};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon exposure to amphotericin B, the
CC allylamine terbinafine, and the azole itraconazole.
CC {ECO:0000269|PubMed:27121717}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; GG700658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CU83; -.
DR SMR; P0CU83; -.
DR STRING; 5551.XP_003231502.1; -.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1366
FT /note="ABC multidrug transporter MDR2"
FT /id="PRO_0000447182"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 56..354
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 390..669
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 768..1055
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1122..1361
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 727..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1157..1164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1366 AA; 148118 MW; 7224F816DC0F3C8A CRC64;
MTNTGILAPS SQQSEPEWWT KTQKFFSREN TITPTFGYFR LLFGTQPGKT DIALIVIGTI
AGIGAGIPFP LLGILFGELV DDLNSSTCST TQAPPGGYQA AITTKVLQVI YASILNFVCM
YIHTGCWSMV GERLVRRLRT KYFHSLLRQE IAFTDTLPSG DVTSRLVSDI EVIQAGTSEK
VGLFIGTISY FVAAYIVAFL KVATIAAMLM SVVPIYFLMA FGGGHYIKKY SSRISTHINA
ATSIVSSSLS HMSIVHAFNA NARLEALFAQ HLVSARMDAL KKAITHSIQF GMLYFVAYAS
NALAFWQGSR MIADLAEGKP SKVSVGAVYT VIFVLLDASF VLSQMAPFMH IFASAASAGD
RLMTTIKRQS AIDGTSSEGD STISLASEEI ELQDVTFNYP ARPEVPVLQG VSFKIPPNKH
TAIVGTSGSG KSTVVALLER LYDPITGCVR VGNRDLKEIN VRHLRGSIGL VQQEPNLLDR
SILENIAHGL VSSSQEKHKH LLPILLGPSL SELTEKIRQG ASEDEAVAEQ GDVVREIVNL
ARHAATLSNA IDFINALPDG LATRVGSSGA ELSGGQKQRI ALARALIRDP PVLLLDEATA
ALDSTSERLI QAALTKVSEN VTTVSIAHRL ATAKDADNII VMQKGKVMEQ GTHMDLVARD
GVYAGMVRLQ NIGKFSSSSS IMTESTQVDV NIDRSLTTDT LLNKEEKLSL EQGVLDEKEK
PAQLYMPEEA DSLPTEPEAK KEKPKQTLWA TMRGSFPLIR PNLLLISLGL ITSIMIGVSY
TGEAVIFGHT VGSLSVCRGG PSIRSSGMLF GLLFFILAVA KFAAVIVNGA AFGWAAEKTL
YRTRVLSLRS LLRQPLEWHN ADGRTPGLLV ALVTSDASAL SSLTGTTIGV LFSTVANLFA
GVILSHVIAW KIAVVLLATL PVLLASGVLR LRVMAQYQKK HQKAYAKATA ITVETVDNIK
SIAAFSLEQE AYSVFNRSLK APYKSNMKSV LHGNFWLSLA YSISTLVYAL AYWWGSQQIL
AGMYTQVQFF IVLPALLFST QSCGQMFALV PDISKARIAA SNIVDLLSIK HEGDEEYDKT
GSKASAKHTD PRFNMLEDKP RDVEAQLTTT TPSSFPTKGM GVQFRNVHFR YPSRPNQPAL
DDLSINISPG QFCALVGPSG SGKSTTFALL EKFYNPASGS IIIDGVDITK QSGAAFRDTI
ALVPQENVMF EGTVAFNIGL GARPDVEATQ EEIEEACRLA NIHDTIAALP DGYNTVCSQD
GKQFSGGQRQ RLSIARALVR KPRLLLLDES TSALDVESEK HVQDALAKVA RKTTIVAIAH
RLNTIHRADR IFMIEGGKCV DQGTHAELVE RCESYRANVI HQSLDA
