MDR_PLAFF
ID MDR_PLAFF Reviewed; 1419 AA.
AC P13568;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Multidrug resistance protein;
DE EC=7.6.2.2;
DE AltName: Full=Chloroquine resistance protein;
GN Name=MDR1;
OS Plasmodium falciparum (isolate FC27 / Papua New Guinea).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5837;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2701941; DOI=10.1016/0092-8674(89)90330-9;
RA Foote S.J., Thompson J.K., Cowman A.F., Kemp D.J.;
RT "Amplification of the multidrug resistance gene in some chloroquine-
RT resistant isolates of P. falciparum.";
RL Cell 57:921-930(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1922044; DOI=10.1128/mcb.11.10.5244-5250.1991;
RA Triglia T., Foote S.J., Kemp D.J., Cowman A.F.;
RT "Amplification of the multidrug resistance gene pfmdr1 in Plasmodium
RT falciparum has arisen as multiple independent events.";
RL Mol. Cell. Biol. 11:5244-5250(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8426608; DOI=10.1016/0166-6851(93)90252-s;
RA Wilson C.M., Volkman S.K., Thaithong S., Martin R.K., Kyle D.E.,
RA Milhous W.K., Wirth D.F.;
RT "Amplification of pfmdr 1 associated with mefloquine and halofantrine
RT resistance in Plasmodium falciparum from Thailand.";
RL Mol. Biochem. Parasitol. 57:151-160(1993).
CC -!- FUNCTION: Energy-dependent efflux pump responsible for decreased drug
CC accumulation in multidrug-resistant cells.
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 -!- MISCELLANEOUS: P.falciparum resistant to the drug chloroquine have
CC multiple copies of the gene coding for MDR.
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; M29154; AAA29646.1; -; Genomic_DNA.
DR EMBL; X56851; CAA40180.1; -; Genomic_DNA.
DR EMBL; S53996; AAD13870.1; -; Genomic_DNA.
DR PIR; S18204; DVZQF.
DR AlphaFoldDB; P13568; -.
DR SMR; P13568; -.
DR DrugBank; DB11638; Artenimol.
DR TCDB; 3.A.1.201.4; the atp-binding cassette (abc) superfamily.
DR BRENDA; 7.6.2.2; 4889.
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 Gene3D; 1.20.1560.10; -; 2.
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; 3.
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 ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1419
FT /note="Multidrug resistance protein"
FT /id="PRO_0000093344"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..82
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 91..116
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 160..188
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 314..338
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 339..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1063..1083
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1084..1419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..345
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 378..662
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 789..1089
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1126..1416
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 639..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1161..1168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1419 AA; 162252 MW; 0F96C7C1850B33D0 CRC64;
MGKEQKEKKD GNLSIKEEVE KELNKKSTAE LFRKIKNEKI SFFLPFKCLP AQHRKLLFIS
FVCAVLSGGT LPFFISVFGV ILKNMNLGDD INPIILSLVS IGLVQFILSM ISSYCMDVIT
SKILKTLKLE YLRSVFYQDG QFHDNNPGSK LRSDLDFYLE QVSSGIGTKF ITIFTYASSF
LGLYIWSLIK NARLTLCITC VFPLIYVCGV ICNKKVKLNK KTSLLYNNNT MSIIEEALMG
IRTVASYCGE KTILNKFNLS ETFYSKYILK ANFVEALHIG LINGLILVSY AFGFWYGTRI
IINSATNQYP NNDFNGASVI SILLGVLISM FMLTIILPNI TEYMKALEAT NSLYEIINRK
PLVENNDDGE TLPNIKKIEF KNVRFHYDTR KDVEIYKDLS FTLKEGKTYA FVGESGCGKS
TILKLIERLY DPTEGDIIVN DSHNLKDINL KWWRSKIGVV SQDPLLFSNS IKNNIKYSLY
SLKDLEAMEN YYEENTNDTY ENKNFSLISN SMTSNELLEM KKEYQTIKDS DVVDVSKKVL
IHDFVSSLPD KYDTLVGSNA SKLSGGQKQR ISIARAIMRN PKILILDEAT SSLDNKSEYL
VQKTINNLKG NENRITIIIA HRLSTIRYAN TIFVLSNRER SDNNNNNNND DNNNNNNNNN
NKINNEGSYI IEQGTHDSLM KNKNGIYHLM INNQKISSNK SSNNGNDNGS DNKSSAYKDS
DTGNDADNMN SLSIHENENI SNNRNCKNTA ENEKEEKVPF FKRMFRRKKK APNNLRIIYK
EIFSYKKDVT IIFFSILVAG GLYPVFALLY ARYVSTLFDF ANLEYNSNKY SIYILLIAIA
MFISETLKNY YNNKIGEKVE KTMKRRLFEN ILYQEMSFFD QDKNTPGVLS AHINRDVHLL
KTGLVNNIVI FSHFIMLFLV SMVMSFYFCP IVAAVLTFIY FINMRVFAVR ARLTKSKEIE
KKENMSSGVF AFSSDDEMFK DPSFLIQEAF YNMHTVINYG LEDYFCNLIE KAIDYKNKGQ
KRRIIVNAAL WGFSQSAQLF INSFAYWFGS FLIKRGTILV DDFMKSLFTF IFTGSYAGKL
MSLKGDSENA KLSFEKYYPL MIRKSNIDVR DDGGIRINKN LIKGKVDIKD VNFRYISRPN
VPIYKNLSFT CDSKKTTAIV GETGSGKSTF MNLLLRFYDL KNDHIILKND MTNFQDYQNN
NNNSLVLKNV NEFSNQSGSA EDYTVFNNNG EILLDDINIC DYNLRDLRNL FSIVSQEPML
FNMSIYENIK FGREDATLED VKRVSKFAAI DEFIESLPNK YDTNVGPYGK SLSGGQKQRI
AIARALLREP KILLLDEATS SLDSNSEKLI EKTIVDIKDK ADKTIITIAH RIASIKRSDK
IVVFNNPDRN GTFVQSHGTH DELLSAQDGI YKKYVKLAK
