MDR_ORYSJ
ID MDR_ORYSJ Reviewed; 1245 AA.
AC Q6YUU5; A0A0N7KEU5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Putative multidrug resistance protein;
DE AltName: Full=P-glycoprotein;
GN OrderedLocusNames=Os02g0190300, LOC_Os02g09720; ORFNames=OSJNBb0031B09.19;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
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; AP005849; BAD16475.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77393.1; -; Genomic_DNA.
DR RefSeq; XP_015625016.1; XM_015769530.1.
DR AlphaFoldDB; Q6YUU5; -.
DR SMR; Q6YUU5; -.
DR STRING; 4530.OS02T0190300-01; -.
DR PaxDb; Q6YUU5; -.
DR PRIDE; Q6YUU5; -.
DR EnsemblPlants; Os02t0190300-01; Os02t0190300-01; Os02g0190300.
DR GeneID; 4328570; -.
DR Gramene; Os02t0190300-01; Os02t0190300-01; Os02g0190300.
DR KEGG; osa:4328570; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q6YUU5; -.
DR OMA; CMALCFW; -.
DR OrthoDB; 186078at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1245
FT /note="Putative multidrug resistance protein"
FT /id="PRO_0000247627"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 35..324
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 359..595
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 674..962
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 999..1233
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 610..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1032..1039
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1245 AA; 135053 MW; F1EDE693F68665C6 CRC64;
MGGGDGGAGK AKARPVFSSF MTVFMHADAA DVALMVLGLL GAMGDGISTP VMLLITSRIF
NDLGSGADIV KEFSSKVNVN ARNLVFLAAA SWVMAFLEGY CWARTAERQA SRMRARYLRA
VLRQDVEYFD LKKGSTAEVI TSVSNDSLVV QDVLSEKVPN FVMNAAMFAG SYAVGFALLW
RLTLVALPSV VLLIIPGFMY GRILVGLARR IREQYTRPGA IAEQAVSSAR TVYSFVAERT
TMAQFSAALE ESARLGLKQG LAKGIAVGSN GITFAIWAFN VWYGSRLVMY HGYQGGTVFA
VSAAIVVGGL ALGSGLSNVK YFSEASSAAE RILEVIRRVP KIDSESDTGE ELANVTGEVE
FRNVEFCYPS RPESPIFVSF NLRVPAGRTV ALVGGSGSGK STVIALLERF YDPSAGEVMV
DGVDIRRLRL KWLRAQMGLV SQEPALFATS IRENILFGKE EATAEEVVAA AKAANAHNFI
SQLPQGYDTQ VGERGVQMSG GQKQRIAIAR AILKSPKILL LDEATSALDT ESERVVQEAL
DLASMGRTTI VIAHRLSTIR NADIIAVMQS GEVKELGPHD ELIANDNGLY SSLVRLQQTR
DSNEIDEIGV TGSTSAVGQS SSHSMSRRFS AASRSSSARS LGDARDDDNT EKPKLPVPSF
RRLLMLNAPE WKQALMGSFS AVVFGGIQPA YAYAMGSMIS VYFLTDHAEI KDKTRTYALI
FVGLAVLSFL INIGQHYNFG AMGEYLTKRI REQMLAKILT FEIGWFDRDE NSSGAICSQL
AKDANVVRSL VGDRMALVIQ TISAVLIACT MGLVIAWRLA LVMIAVQPLI IVCFYARRVL
LKSMSKKSIH AQAESSKLAA EAVSNLRTIT AFSSQERILR LFEQSQDGPR KESIRQSWFA
GLGLGTSMSL MTCTWALDFW YGGRLMAEHH ISAKELFQTF MILVSTGRVI ADAGSMTTDL
AKGADAVASV FAVLDRETEI DPDNPQGYKP EKLKGEVDIR GVDFAYPSRP DVIIFKGFTL
SIQPGKSTAL VGQSGSGKST IIGLIERFYD PIRGSVKIDG RDIKAYNLRA LRRHIGLVSQ
EPTLFAGTIR ENIVYGTETA SEAEIEDAAR SANAHDFISN LKDGYDTWCG ERGVQLSGGQ
KQRIAIARAI LKNPAILLLD EATSALDSQS EKVVQEALDR VMIGRTSVVV AHRLSTIQNC
DLITVLEKGT VVEKGTHASL MAKGLSGTYF SLVNLQQGGN QQVQH
