MDR4_TRIT1
ID MDR4_TRIT1 Reviewed; 1363 AA.
AC F2RPA4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=TESG_00713;
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon exposure the allylamine
CC terbinafine and the azole itraconazole. {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; GG698478; EGD93160.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RPA4; -.
DR SMR; F2RPA4; -.
DR EnsemblFungi; EGD93160; EGD93160; TESG_00713.
DR HOGENOM; CLU_000604_17_2_1; -.
DR OrthoDB; 186078at2759; -.
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 Gene3D; 1.20.1560.10; -; 3.
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; 2.
DR Pfam; PF00664; ABC_membrane; 3.
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 Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1363
FT /note="ABC multidrug transporter MDR2"
FT /id="PRO_0000447185"
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 896..916
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1016..1036
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..1052
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1119..1358
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 1154..1161
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 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1363 AA; 148024 MW; B3D4A5BD99D8AE84 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 LFAGVILSQC HRMEDSRSPS GYLTRIKHQK AYAKATAITV ESVDNIKSIA
AFSLEQEAYS VFNRSLKAPY KSNMKSVLHG NFWLSLAYSI STLVYALAYW WGSQQILAGM
YTQVQFFIVL PALLFSTQSC GQMFALVPDI SKARIAASNI VDLLSIKHEG DEEYDKTGSK
ASAKHTDPRF NMLEDKPRDV EAQLITTTPS SFPTKGMGVQ FRNVHFRYPS RPNQPALDDL
SINISPGQFC ALVGPSGSGK STTFALLEKF YNPASGSIII DGVDITKQSG AAFRDTIALV
PQENVMFEGT VAFNIGLGAR PDVEATQEEI EEACRLANIH DTIAALPDGY NTVCSQDGKQ
FSGGQRQRLS IARALVRKPR LLLLDESTSA LDVESEKHVQ DALAKVARKT TIVAIAHRLN
TIHRADRIFM IERGRCVDQG THAELVERCE SYRANVIHQS LDA
