MDR2_TRIT1
ID MDR2_TRIT1 Reviewed; 1331 AA.
AC F2RP52;
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=MDR2 {ECO:0000303|PubMed:27121717}; ORFNames=TESG_00664;
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:A0A059JJ46}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + itraconazole(in) = ADP + H(+) + itraconazole(out)
CC + phosphate; Xref=Rhea:RHEA:33503, ChEBI:CHEBI:6076,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:F2T1C4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33504;
CC Evidence={ECO:0000250|UniProtKB:F2T1C4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced upon exposure to amphotericin B,
CC griseofulvin, the 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; GG698478; EGD93108.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RP52; -.
DR SMR; F2RP52; -.
DR EnsemblFungi; EGD93108; EGD93108; TESG_00664.
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; -; 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 Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1331
FT /note="ABC multidrug transporter MDR2"
FT /id="PRO_0000447180"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 910..930
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 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 97..387
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 422..667
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 764..1051
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1086..1324
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1121..1128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1331 AA; 145322 MW; F2850E14C0199916 CRC64;
MVEVSEKPNT QDDGVSKQEN RNPASSSSST SDKEKVAKKG NSDATKSSTP EDLDAQLAHL
PEHEREILKQ QLFIPDVKAT YGTLFRYATR NDMIFLAIVS LASIAAGAAL PLFTVLFGSL
AGTFRDIALH RITYDEFNSI LTRNSLYFVY LGIAQFILLY VSTVGFIYVG EHITQKIRAK
YLHAILRQNI GFFDKLGAGE VTTRITADTN LIQDGISEKV GLTLTALSTF FSAFIIGYVR
YWKLALICSS TIVAMILVMG GISRFVVKSG RMTLVSYGEG GTVAEEVISS IRNATAFGTQ
EKLARQYEVH LKEARKWGRR LQMMLGIMFG SMMAIMYSNY GLGFWMGSRF LVGGETDLSA
IVNILLAIVI GSFSIGNVAP NTQAFASAIS AGAKIFSTID RVSAIDPGSD EGDTIENVEG
TIEFRGIKHI YPSRPEVVVM EDINLVVPKG KTTALVGPSG SGKSTVVGLL ERFYNPVSGS
VLLDGRDIKT LNLRWLRQQI SLVSQEPTLF GTTIFENIRL GLIGSPMENE SEEQIKERIV
SAAKEANAHD FIMGLPDGYA TDVGQRGFLL SGGQKQRIAI ARAIVSDPKI LLLDEATSAL
DTKSEGVVQA ALDAASRGRT TIVIAHRLST IKSADNIVVI VGGRIAEQGT HDELVDKKGT
YLQLVEAQKI NEERGEESED EAVLEKEKEI SRQISVPAKS VNSGKYPDED VEANLGRIDT
KKSLSSVILS QKRSQENETE YSLGTLIRFI AGFNKPERLI MLCGFFFAVL SGAGQPVQSV
FFAKGITTLS LPPSLYGKLR EDANFWSLMF LMLGLVQLVT QSAQGVIFAI CSESLIYRAR
SKSFRAMLRQ DIAFFDLPEN STGALTSFLS TETKHLSGVS GATLGTILMV STTLIVALTV
ALAFGWKLAL VCISTVPVLL LCGFYRFWIL AQFQTRAKKA YESSASYACE ATSSIRTVAS
LTREQGVMEI YEGQLNDQAK KSLRSVAKSS LLYAASQSFS FFCLALGFWY GGGLLGKGEY
NAFQFFLCIS CVIFGSQSAG IVFSFSPDMG KAKSAAADFK RLFDRVPTID IESPDGEKLE
TVEGTIEFRD VHFRYPTRPE QPVLRGLNLT VKPGQYIALV GPSGCGKSTT IALVERFYDT
LSGGVYIDGK DISRLNVNSY RSHLALVSQE PTLYQGTIRD NVLLGVDRDE LPDEQVFAAC
KAANIYDFIM SLPDGFGTVV GSKGSMLSGG QKQRIAIARA LIRDPKVLLL DEATSALDSE
SEKVVQAALD AAAKGRTTIA VAHRLSTIQK ADIIYVFDQG RIVESGTHHE LLQNKGRYYE
LVHMQSLEKT Q
