ID   Q672M3_PLAVI            Unreviewed;      1464 AA.
AC   Q672M3;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   22-FEB-2023, entry version 111.
DE   SubName: Full=Mdr1 {ECO:0000313|EMBL:AAU04972.1};
GN   Name=mdr1 {ECO:0000313|EMBL:AAU04972.1};
OS   Plasmodium vivax (malaria parasite P. vivax).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5855 {ECO:0000313|EMBL:AAU04972.1};
RN   [1] {ECO:0000313|EMBL:AAU04972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL004 {ECO:0000313|EMBL:AAU04970.1}, and CL014
RC   {ECO:0000313|EMBL:AAU04972.1};
RA   Martha-Sa J., Nomura T., Wellems T.E., del Portillo H.A.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAU04972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL004 {ECO:0000313|EMBL:AAU04970.1}, and CL014
RC   {ECO:0000313|EMBL:AAU04972.1};
RX   PubMed=15755424; DOI=10.1016/j.exppara.2004.12.005;
RA   Sa J.M., Nomura T., Neves J., Baird J.K., Wellems T.E., del Portillo H.A.;
RT   "Plasmodium vivax: allele variants of the mdr1 gene do not associate with
RT   chloroquine resistance among isolates from Brazil, Papua, and monkey-
RT   adapted strains.";
RL   Exp. Parasitol. 109:256-259(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AY571976; AAU04970.1; -; Genomic_DNA.
DR   EMBL; AY571978; AAU04972.1; -; Genomic_DNA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR   CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF503; GH19726P; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 3.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        825..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        866..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        940..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        967..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1065..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..350
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          383..679
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          826..1120
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1164..1461
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          661..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1464 AA;  165402 MW;  BA8EF4A50778BA7C CRC64;
     MKKDQRQPRD NSNSSNNLSI KDEVEKELNK KGTFELYKKI KTQKIPFFLP FKCLPSSHRK
     LLGVSFVCAT ISGGTLPFFV SVFGVIMKNM NLGENVNDII FSLVLIGIFQ FILSFISSFC
     MDVVTTKILK TLKIEFLKSV FYQDGQFHDN NPGSKLTSDL DFYLEQVNAG IGTKFITIFT
     YASAFLGLYI WSLFKNARLT LCITCVFPLI YICGVICNKK VKINKKTSLL YNNNTMSIIE
     EALVGIRTVV SYCGENTILK KFNLSEKLYS KYTLKANLME SLHIGMINGF ILASYAFGFW
     YGTRIIISDL SNQQPNNDFH GGSVISILLG VLISMFMLTI ILPNITEYMK SLEATNNLYE
     IINRKPLVEN NQDGKKLKDI KKIQFKNVRF HYDTRKDVEI YKDLNFTLTE GKTYAFVGES
     GCGKSTILKL IERLYDPTEG DVIINDSHNL KDVNLKWWRS KIGVVSQDPL LFSNSIKNNI
     KYSLYSLKDL EALSEESNED GFSSQSDSNS HNSCRAKCAG DLNDMIQTTD STELIQVRKN
     YETIEDSEVV SVSKKVLIHD FVSALPDKYE TLVGSNASKL SGGQKQRISI ARAIIRNPKI
     LILDEATSSL DNKSEYLVQK TINNLKGNEN RITIIIAHRL STIRYANTIF VLSNRENGST
     VDVDVLGEDP TKDSNEKNEK HDKQEKGGKN SSANQKISNA GSYIIEQGTH DALMKNKNGI
     YYTMINNQKV SSKSSSNNDN DKDSDMKSSI YKDSERGYDP DEANGNAKNE SASAKKSEKM
     SDAKASNTNA GGRLAFLRNL FKRKPKAPNN LRVVYREIFS YKEDIAIIAL SIMVAGGLYP
     LFALLYAKYV GTLFDFANLE ANSNKYSLYI LVIAIAMFIS ETLKNYYNNV IGEKVEKTMK
     LRLFENILYQ EISFFDQDSH APGLLSAHIN RDVHLLKTGL VNNIVIFTHF IVLFLVSMVM
     SFYFCPIVAA VLTGTFFIFM RVFAIRARIA ANKDVEKKRV NQPGTAFVYN SDDEIFKDPS
     FLIQEAFYNM NTVIIYGLED YFCTLIEKAI DYSNKGQKRK TLINSMLWGF SQSAQLFINS
     FAYWFGSFLI RRGTIQVDDF MKSFFTFLFT GSYAGKLMSL KGDSENAKLS FERYYPLITR
     KSLIDVRDNG GIKIKNSNDI KGKIEIMDVN FRYLSRPNVP IYKDLTFSCE SKKTTAIVGE
     TGSGKSTVMS LLMRFYDLKN DHHIVFKNEQ TGESSKEQMQ QGDEEQNVGM KNANEFSSSK
     EGADGQSSTL FKNSGKILLD GVDICDYNLK DLRNLFSIVS QEPMLFNMSI YENIKFGKEN
     ATREDVKRAC KFAAIDEFIE SLPNQYDTNV GPYGKSLSGG QKQRIAIARA LLREPKILLL
     DEATSSLDSN SEKLIEKTIV DIKDKADKTI ITIAHRIASI KRSDKIVVFN NPDRTGSFVQ
     AQGTHEELLS VQDGVYKKYV KLAK
//