ID A0A1J1HAH2_PLARL Unreviewed; 1378 AA.
AC A0A1J1HAH2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Multidrug resistance protein 1, putative {ECO:0000313|EMBL:CRH00434.1};
GN Name=MDR1 {ECO:0000313|EMBL:CRH00434.1};
GN Synonyms=ABCB1 {ECO:0000313|EMBL:CRH00434.1};
GN ORFNames=PRELSG_1008800 {ECO:0000313|EMBL:CRH00434.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH00434.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRH00434.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRH00434.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LN835305; CRH00434.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PRELSG_1008800; -.
DR OMA; GFGQEEQ; -.
DR OrthoDB; 5487044at2759; -.
DR Proteomes; UP000220158; Chromosome 10.
DR GO; GO:0016020; C: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 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; 3.
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; LP14331P; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000220158};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..921
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..344
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 377..656
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 763..1053
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1096..1370
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 674..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 156457 MW; 4D2A40D6F87D03F5 CRC64;
MRSGLSNKKD VLSVKDEVEK ELNKKNTVQL LKKIKSQKIP FFLPFKILPP FYKRLLALAF
LCAVISGGTL PFFVSVFGII IKNINLGNNI NDILLYLVLV GIFQFIFSFI SCFCMDAVTS
KIIKTLKIKY LRSVFYQDGQ FHDNNPGSKL TSDLEFHLSQ VQAGIGTKFI TIFTYLSSFL
GLYLWSLFKN VRLTLCITCV FPVIYVFGAI CSKKIKLNKK TSLLYNNNTV SIIEEALIGI
RTVVSYCGEN LILKKFNLSE KLYSKFMLKA NFIESLHNGA INGFILSAYA LGFWYGTRIL
ISDMENQNVG GDFHGGSVIS ILLGVLISIF MLTIVLPNVA DYMKSVEATY SLFEVINRDP
LIANNSSGEK LQDIKKIEFK NVKFHYDTRK DVEIYENLSF TLEEGKTYAF VGESGCGKST
ILKLIERLYD PSDGEIIIND FYNLKDLNLK WWRSKIGVVS QDPLLFSNSI KNNIKYSLFS
INELASLENE GDVKNEDRNL RDIKNETPNE LLKMKKEYQS VDDSEIVNVS KKVLVHDFVS
SLPNKYETLI GSNASKLSGG QKQRISIARA VIRNPKILIL DEATSSLDNK SEYLVQKTIS
NLKGNESRIT IIIAHRLSTI RYANTIFVLS NKVKENGVNN NNSGSYIIEQ GTHESLMKNR
DGIYYNMIHN QKVSSSLSNG SDKDSDKKSS SYIDSITGND NEMNNLSNNG NDEHNYEKNK
EKKDERKKGA SFFKSLFNRK KKKNNNNLNF VYKEIFSYKK DIIIIILSII VAGGLYPLFA
LLYAKYVSTL FDIDNLRSNS NKYSLYILFI SIAMFISETL KNYYNNLIGE KVEKNVKYRL
FENILHQEIS FFDQDVNSPG VLISYINRDV HLLKTGLVNN MVIFTHFIVL FLVSISLSFY
FCPIVAAALT GAYFILVRVF AIKARMSENK PLQKKDDNTF AYSSDEEIFK DPGFLIQEAF
YNINAIIIYG LEDYFCSLIE NSIDFVSRGD KKKSIINSTL WGISQSSQLF INSFAYWFGS
FLIKRGIINV DNFMNSLFTF LFTGSYAGKL MSLKGDSGNA KVCFEKYYPL ITRKSNVDVR
DETGIKINKN ELKGEIDIKK VNFRYISRPN VPVYNDLSFS CQSKKTTAIV GETGSGKSTV
MNLLLRFYDL KEDHIILKKD GNKSSSTRNS DTSVDHSRDE DYIIFKNSGE ILLDGININN
YNLRDLRNTF SIVSQEPILF NMSIYENIKF GKEDATLEDV KRVCKFAAID EFIESLPDKY
DTNVGPFGRS LSGGQKQRIA IARALLKEPK ILLLDEATSS LDSNSEKLIE KTIADIKDKA
DKTIITIAHR IASIKRSDKI VVFNNPDRNG SYVQSQGTHD ELLSIEDGVY KKYVKLAK
//
