MDR4_TRIIM
ID MDR4_TRIIM Reviewed; 1379 AA.
AC A0A059JK44;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=H109_00425;
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816;
RX PubMed=29467168; DOI=10.1534/genetics.117.300573;
RA Persinoti G.F., Martinez D.A., Li W., Doegen A., Billmyre R.B.,
RA Averette A., Goldberg J.M., Shea T., Young S., Zeng Q., Oliver B.G.,
RA Barton R., Metin B., Hilmioglu-Polat S., Ilkit M., Graeser Y.,
RA Martinez-Rossi N.M., White T.C., Heitman J., Cuomo C.A.;
RT "Whole-genome analysis illustrates global clonal population structure of
RT the ubiquitous dermatophyte pathogen Trichophyton rubrum.";
RL Genetics 208:1657-1669(2018).
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon exposure to amphotericin B and
CC the allylamine terbinafine. This induction requires the presence of
CC MDR2. {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; AOKY01000033; KDB27857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059JK44; -.
DR SMR; A0A059JK44; -.
DR EnsemblFungi; KDB27857; KDB27857; H109_00425.
DR HOGENOM; CLU_000604_17_2_1; -.
DR OMA; HRLNTIH; -.
DR Proteomes; UP000024533; 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..1379
FT /note="ABC multidrug transporter MDR2"
FT /id="PRO_0000447183"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 920..942
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1032..1052
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 69..367
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 403..682
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 781..1068
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1135..1374
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 738..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 438..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1170..1177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1379 AA; 149560 MW; DB3954CC1FD48B52 CRC64;
MAVEEKNSPT GAAMTNTGIL VPSSQQSLPE WWTKTQKFFS RENTITPTFG YFRLLFGTQP
GKTDIALIVI GTIAGIGAGI PFPLLGILFG ELVDDLNSST CSTTQAPPGG YQAAITTKVL
QVIYVSILNF VCMYIHTGCW SMVGERLVRR LRTKYFHSLL RQEIAFTDTL PSGDVTSRLV
SDIEVIQAGT SEKVGLFIGT ISYFVAAYIV AFLKVATIAA MLMSVVPIYF LMAFGGGHYI
KKYSGRISTH INAATSIVSS SLSHMSIVHA FNANARLEAL FAQHLVSARM DALKKAITHS
IQFGMLYFVA YASNALAFWQ GSRMIADLAE GKPSKVSVGA VYTVIFVLLD ASFVLSQMAP
FMHIFASAAS AGDRLMTTIK RQSAIDGTSS EGDSTISLAS EEIELQDVTF NYPARPEVPV
LQGVSFKIPP NKHTAIVGTS GSGKSTVVAL LERLYDPITG CVRVGNRDLK EINVRHLRGS
IGLVQQEPNL LDRSILENIA HGLVSSSQEK HKHLLPTLLG PSLSELTEKI RQGASEDEAV
TEQGDVVREI VNLTRHAATL SNAIDFINAL PDGLATRVGS SGAELSGGQK QRIALARALI
RDPPVLLLDE ATAALDSTSE RLIQAALNKV SENVTTVSIA HRLATAKDAD NIIVMQKGRV
MEQGTHMDLV ARDGVYAGMV RLQNIGKFSS SSSIMTESTQ VDANIDRSLT TDTLLNKEEK
LSLEQGVLDE KEKPAQLYMP EEADSLPTEP ENEKEKPKQT LWATMKGSFP LIRPNILLIS
LGLITSIMIG VSYTGEAVIF GHTVGSLSVC RGGPSIRSSG MLFGLLFFIL AIVKFAAVIV
NGAAFGWAAE KTLYRTRVLS LRSLLRQPLE WHNADGRTPG LLVALVTSDA SALSSLTGTT
IGVLFSTVAN LFAGVILSHV IAWKIAVVLL ATLPVLLASG VLRLRVMAQY QKKHQKAYAK
ATAITVESVD NIKSIAAFSL EQEAYSVFNR SLKAPYKSNM KSVLHGNFWL SLAYSISTLV
YALAYWWGSQ QILAGMYTQV QFFIVLPALL FSTQSCGQMF ALVPDISKAR IAASNIVDLL
SIKHEGDEEY DKTGSKASAK HTDPRFNMLE DKPRDVEAQL ITTTPSSFPT KGMGVQFRNV
HFRYPSRPNQ PALDDLSINI SPGQFCALVG PSGSGKSTTF ALLEKFYNPA SGSIIIDGVD
ITKQSGAAFR DTIALVPQEN VMFEGTVAFN IGLGARPDVE ATQEEIEEAC RLANIHDTIA
ALPDGYNTVC SQDGKQFSGG QRQRLSIARA LVRKPRLLLL DESTSALDVE SEKHVQDALA
KVARKTTIVA IAHRLNTIHR ADRIFMIEGG RCVDQGTHAE LVERCESYRA NVIHQSLDA
