MDR1_LEIEN
ID MDR1_LEIEN Reviewed; 1280 AA.
AC Q06034;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Multidrug resistance protein 1;
DE EC=7.6.2.2;
DE AltName: Full=P-glycoprotein 1;
GN Name=MDR1;
OS Leishmania enriettii.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5663;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8232412; DOI=10.1016/0166-6851(93)90131-g;
RA Chow L.M.C., Wong A.K.C., Ullman B., Wirth D.F.;
RT "Cloning and functional analysis of an extrachromosomally amplified
RT multidrug resistance-like gene in Leishmania enriettii.";
RL Mol. Biochem. Parasitol. 60:195-208(1993).
CC -!- FUNCTION: Energy-dependent efflux pump responsible for decreased drug
CC accumulation in multi-drug-resistant cells. Confers vinblastine
CC resistance.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; L08091; AAA16255.1; -; Unassigned_DNA.
DR AlphaFoldDB; Q06034; -.
DR SMR; Q06034; -.
DR VEuPathDB; TriTrypDB:CUR178_01425; -.
DR VEuPathDB; TriTrypDB:LENLEM3045_340014500; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; 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; 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 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Glycoprotein; Membrane;
KW Nucleotide-binding; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1280
FT /note="Multidrug resistance protein 1"
FT /id="PRO_0000093345"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 346..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 762..781
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 72..357
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 391..634
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 713..1002
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1036..1274
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 426..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1071..1078
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 1113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 286
FT /note="G -> D"
SQ SEQUENCE 1280 AA; 139729 MW; 76B65C82CE5E4043 CRC64;
MSRAHAAYAN EGWSAPEGGI AGKDGSTRDC SGYGSQGPLF SAEEEVKGTV VRETVGPIEI
FRYADATDRV LMIAGTAFAV ACGAGMPVFS FIFGRIAMDL MSGVGSAEEK AAKTSLIMVY
VGIAMLIACA GHVMCWTVAA CRQVARIRLL FFRAVLRQDI GWHDEHSPGA LTARMTGDTR
VIQNGINDKL SQGIMNGSMG VIGYIAGFVF SWELTLMMIG MMPFIIVMAA IIGSIVSKIT
ESSRKYFAKA GSLATEVMEN IRTVQAFGRE DYELERFTKA VLYAQGRGIR KELASNLSAA
VIMALMYVSY TVAFFFGSYL VEWGRRDMAD IISTFLAVLM GSFGLGFVAP SRTAFTESRA
AAYEIFKAID RVPPVDIDAG GVPVPGFKES IEFRNVRFAY PTRPGMILFR DLSLKIKCGQ
KVAFSGASGC GKSSVIGLIQ RFYDPIGGAV LVDGVRMREL CLREWRDQIG IVSQEPNLFA
GTMMENVRMG KPNATDEEVV EACRQANIHD TIMALPDRYD TPVGPVGSLL SGGQKQRIAI
ARALVKRPPI LLLDEATSAL DRKSEMEVQA ALDQLIQRGG TTVVVIAHRL ATIRDMDRIY
YVKHDGAEGS RITESGTFDE LLELDGEFAA VAKMQGVLAG DAKSGASVRD AKKASGHLGV
ILDEADLAQL DEDVPRTARQ NVPIDELAKW EVKHAKVGFL RLMRMNKDKA WAVALGILSS
VVIGSARPAS SIVMGHMLRV LGEYSATKDV EALRSGTNLY APLFIVFAVA NFSGWILHGF
YGYAGEHLTT KIRVLLFRQI MRQDINFFDI PGRDAGTLAG MLSGDCEAVH QLWGPSIGLK
VQTMCIIASG LVVGFIYQWK LALVALACMP LMIGCSLTRR LMINGYTKSR EGDTDDTIVT
EALSNVRTVT SLNMKEDCVE AFQAALREEA PRSVRKGIIA GGIYGITQFI FYGVYALCFW
YGSKLIDKGE AEFKDVMIAS MSILFGAQNA GEAGAFATKL ADAEASAKRV FSVIDRVPDV
DIEQAGNKDL GEGCDIEYRN VQFIYSARPK QVVLASVNMR FGDATSNGLI GQTGCGKSTV
IQMLARFYER RSGLISVNGR DLSSLDIAEW RRNISIVLQE PNLFSGTVRE NIRYAREGAT
DEEVEEAARL AHIHHEIIKW TDGYDTEVGY KGRALSGGQK QRIAIARGLL RRPRLLLLDE
ATSALDSVTE AKVQEGIEAF QAKYKVTTVS IAHRLTTIRH CDQIILLDSG CIIEQGSHEE
LMALGGEYKT RYDLYMSALS
