MDR1A_MOUSE
ID MDR1A_MOUSE Reviewed; 1276 AA.
AC P21447; Q5I1Y5;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ATP-dependent translocase ABCB1 {ECO:0000250|UniProtKB:P08183};
DE AltName: Full=ATP-binding cassette sub-family B member 1A {ECO:0000305};
DE AltName: Full=MDR1A;
DE AltName: Full=Multidrug resistance protein 1A;
DE EC=7.6.2.2;
DE AltName: Full=Multidrug resistance protein 3;
DE AltName: Full=P-glycoprotein 3;
DE AltName: Full=Phospholipid transporter ABCB1 {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P08183};
GN Name=Abcb1a {ECO:0000312|MGI:MGI:97570};
GN Synonyms=Abcb4, Mdr1a, Mdr3, Pgy-3, Pgy3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1969610; DOI=10.1128/mcb.10.4.1652-1663.1990;
RA Devault A., Gros P.;
RT "Two members of the mouse mdr gene family confer multidrug resistance with
RT overlapping but distinct drug specificities.";
RL Mol. Cell. Biol. 10:1652-1663(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1972547; DOI=10.1128/mcb.10.7.3596-3606.1990;
RA Hsu S.I.H., Cohen D., Kirschner L.S., Lothstein L., Hartstein M.,
RA Horwitz S.B.;
RT "Structural analysis of the mouse mdr1a (P-glycoprotein) promoter reveals
RT the basis for differential transcript heterogeneity in multidrug-resistant
RT J774.2 cells.";
RL Mol. Cell. Biol. 10:3596-3606(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Pimprale S.S., Xiao G., Patten C., Crespi C.;
RT "Heterologus expression of mouse mdr1a (Abcb1a), (P-glycoprotein), using
RT the insect cell baculovirus expression system.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 173-1276.
RC STRAIN=BALB/cJ;
RX PubMed=2473069; DOI=10.1016/s0021-9258(18)80173-9;
RA Hsu S.I.H., Lothstein L., Horwitz S.B.;
RT "Differential overexpression of three mdr gene family members in multidrug-
RT resistant J774.2 mouse cells. Evidence that distinct P-glycoprotein
RT precursors are encoded by unique mdr genes.";
RL J. Biol. Chem. 264:12053-12062(1989).
RN [6]
RP PROTEIN SEQUENCE OF 273-282, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=8898203; DOI=10.1016/s0092-8674(00)81370-7;
RA van Helvoort A., Smith A.J., Sprong H., Fritzsche I., Schinkel A.H.,
RA Borst P., van Meer G.;
RT "MDR1 P-glycoprotein is a lipid translocase of broad specificity, while
RT MDR3 P-glycoprotein specifically translocates phosphatidylcholine.";
RL Cell 87:507-517(1996).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEXES WITH INHIBITORS, AND
RP TOPOLOGY.
RX PubMed=19325113; DOI=10.1126/science.1168750;
RA Aller S.G., Yu J., Ward A., Weng Y., Chittaboina S., Zhuo R., Harrell P.M.,
RA Trinh Y.T., Zhang Q., Urbatsch I.L., Chang G.;
RT "Structure of P-glycoprotein reveals a molecular basis for poly-specific
RT drug binding.";
RL Science 323:1718-1722(2009).
CC -!- FUNCTION: Translocates drugs and phospholipids across the membrane.
CC Catalyzes the flop of phospholipids from the cytoplasmic to the
CC exoplasmic leaflet of the apical membrane. Participates mainly to the
CC flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-
CC glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent
CC efflux pump responsible for decreased drug accumulation in multidrug-
CC resistant cells (By similarity). {ECO:0000250|UniProtKB:P08183,
CC ECO:0000269|PubMed:8898203}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:P08183};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:8898203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:36439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:8898203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:8898203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ATP +
CC H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:38943, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:8898203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:8898203};
CC -!- ACTIVITY REGULATION: Translocase activity is inhibited by verapamil and
CC is sensitive to energy depletion. {ECO:0000250|UniProtKB:P08183}.
CC -!- SUBUNIT: Interacts with PSMB5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane
CC {ECO:0000269|PubMed:8898203}.
CC -!- MISCELLANEOUS: In mouse the MDR gene family includes three or more
CC related but distinct cellular genes.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M30697; AAA39517.1; -; mRNA.
DR EMBL; M33581; AAA39514.1; -; mRNA.
DR EMBL; M33580; AAA39518.1; -; Genomic_DNA.
DR EMBL; AY864315; AAW56448.1; -; mRNA.
DR EMBL; CH466600; EDL14677.1; -; Genomic_DNA.
DR EMBL; M24417; AAA03243.1; -; mRNA.
DR CCDS; CCDS19084.1; -.
DR PIR; A34175; DVMS1A.
DR PIR; A34786; A34786.
DR RefSeq; NP_035206.2; NM_011076.2.
DR RefSeq; XP_006503618.1; XM_006503555.3.
DR RefSeq; XP_006503619.1; XM_006503556.3.
DR PDB; 3G5U; X-ray; 3.80 A; A/B=1-1276.
DR PDB; 3G60; X-ray; 4.40 A; A/B=1-1276.
DR PDB; 3G61; X-ray; 4.35 A; A/B=1-1276.
DR PDB; 4KSB; X-ray; 3.80 A; A=1-1276.
DR PDB; 4KSC; X-ray; 4.00 A; A=1-1276.
DR PDB; 4KSD; X-ray; 4.10 A; A=1-1276.
DR PDB; 4LSG; X-ray; 3.80 A; A/B=1-1276.
DR PDB; 4M1M; X-ray; 3.80 A; A/B=1-1276.
DR PDB; 4M2S; X-ray; 4.40 A; A/B=1-1276.
DR PDB; 4M2T; X-ray; 4.35 A; A/B=1-1276.
DR PDB; 4Q9H; X-ray; 3.40 A; A=1-1276.
DR PDB; 4Q9I; X-ray; 3.78 A; A=1-1276.
DR PDB; 4Q9J; X-ray; 3.60 A; A=1-1276.
DR PDB; 4Q9K; X-ray; 3.80 A; A=1-1276.
DR PDB; 4Q9L; X-ray; 3.80 A; A=1-1276.
DR PDB; 4XWK; X-ray; 3.50 A; A=1-1276.
DR PDB; 5KO2; X-ray; 3.30 A; A/B=1-1276.
DR PDB; 5KOY; X-ray; 3.85 A; A/B=1-1276.
DR PDB; 5KPD; X-ray; 3.35 A; A/B=1-1276.
DR PDB; 5KPI; X-ray; 4.01 A; A/B=1-1276.
DR PDB; 5KPJ; X-ray; 3.50 A; A=1-1276.
DR PDB; 6GDI; EM; 7.90 A; A=1-1276.
DR PDB; 6Q81; EM; 7.90 A; A=1-1276.
DR PDB; 6UJN; X-ray; 3.98 A; A=1-1276.
DR PDB; 6UJP; X-ray; 3.98 A; A=1-1276.
DR PDB; 6UJR; X-ray; 4.10 A; A=1-1276.
DR PDB; 6UJS; X-ray; 4.17 A; A=1-1276.
DR PDB; 6UJT; X-ray; 4.17 A; A=1-1276.
DR PDB; 6UJW; X-ray; 4.15 A; A=1-1276.
DR PDB; 7OTG; EM; 5.40 A; A=1-1276.
DR PDB; 7OTI; EM; 4.20 A; A=1-1276.
DR PDBsum; 3G5U; -.
DR PDBsum; 3G60; -.
DR PDBsum; 3G61; -.
DR PDBsum; 4KSB; -.
DR PDBsum; 4KSC; -.
DR PDBsum; 4KSD; -.
DR PDBsum; 4LSG; -.
DR PDBsum; 4M1M; -.
DR PDBsum; 4M2S; -.
DR PDBsum; 4M2T; -.
DR PDBsum; 4Q9H; -.
DR PDBsum; 4Q9I; -.
DR PDBsum; 4Q9J; -.
DR PDBsum; 4Q9K; -.
DR PDBsum; 4Q9L; -.
DR PDBsum; 4XWK; -.
DR PDBsum; 5KO2; -.
DR PDBsum; 5KOY; -.
DR PDBsum; 5KPD; -.
DR PDBsum; 5KPI; -.
DR PDBsum; 5KPJ; -.
DR PDBsum; 6GDI; -.
DR PDBsum; 6Q81; -.
DR PDBsum; 6UJN; -.
DR PDBsum; 6UJP; -.
DR PDBsum; 6UJR; -.
DR PDBsum; 6UJS; -.
DR PDBsum; 6UJT; -.
DR PDBsum; 6UJW; -.
DR PDBsum; 7OTG; -.
DR PDBsum; 7OTI; -.
DR AlphaFoldDB; P21447; -.
DR SMR; P21447; -.
DR BioGRID; 202140; 1.
DR STRING; 10090.ENSMUSP00000041204; -.
DR BindingDB; P21447; -.
DR ChEMBL; CHEMBL2573; -.
DR DrugCentral; P21447; -.
DR GuidetoPHARMACOLOGY; 768; -.
DR SwissLipids; SLP:000000383; -.
DR GlyGen; P21447; 3 sites.
DR iPTMnet; P21447; -.
DR PhosphoSitePlus; P21447; -.
DR EPD; P21447; -.
DR jPOST; P21447; -.
DR MaxQB; P21447; -.
DR PaxDb; P21447; -.
DR PeptideAtlas; P21447; -.
DR PRIDE; P21447; -.
DR ProteomicsDB; 295845; -.
DR ABCD; P21447; 2 sequenced antibodies.
DR DNASU; 18671; -.
DR Ensembl; ENSMUST00000047753; ENSMUSP00000041204; ENSMUSG00000040584.
DR GeneID; 18671; -.
DR KEGG; mmu:18671; -.
DR UCSC; uc008wkl.1; mouse.
DR CTD; 18671; -.
DR MGI; MGI:97570; Abcb1a.
DR VEuPathDB; HostDB:ENSMUSG00000040584; -.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000155287; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; P21447; -.
DR OMA; FSTEFFC; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; P21447; -.
DR TreeFam; TF105193; -.
DR BRENDA; 7.6.2.2; 3474.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 18671; 4 hits in 72 CRISPR screens.
DR EvolutionaryTrace; P21447; -.
DR PRO; PR:P21447; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P21447; protein.
DR Bgee; ENSMUSG00000040584; Expressed in right colon and 203 other tissues.
DR Genevisible; P21447; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0099038; F:ceramide floppase activity; IDA:BHF-UCL.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0140328; F:floppase activity; IMP:UniProtKB.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IDA:BHF-UCL.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IDA:BHF-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1905039; P:carboxylic acid transmembrane transport; ISO:MGI.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
DR GO; GO:1905231; P:cellular response to borneol; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071217; P:cellular response to external biotic stimulus; IEA:Ensembl.
DR GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0036146; P:cellular response to mycotoxin; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0099040; P:ceramide translocation; IDA:BHF-UCL.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0043215; P:daunorubicin transport; ISO:MGI.
DR GO; GO:0060856; P:establishment of blood-brain barrier; ISO:MGI.
DR GO; GO:1990963; P:establishment of blood-retinal barrier; ISO:MGI.
DR GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0009914; P:hormone transport; ISO:MGI.
DR GO; GO:0050892; P:intestinal absorption; ISO:MGI.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:1901529; P:positive regulation of anion channel activity; ISO:MGI.
DR GO; GO:1904446; P:positive regulation of establishment of Sertoli cell barrier; ISO:MGI.
DR GO; GO:2001025; P:positive regulation of response to drug; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:2001225; P:regulation of chloride transport; ISO:MGI.
DR GO; GO:1904478; P:regulation of intestinal absorption; ISO:MGI.
DR GO; GO:0047484; P:regulation of response to osmotic stress; ISO:MGI.
DR GO; GO:0097327; P:response to antineoplastic agent; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:1905233; P:response to codeine; IEA:Ensembl.
DR GO; GO:1905237; P:response to cyclosporin A; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:1905235; P:response to quercetin; IEA:Ensembl.
DR GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; ISO:MGI.
DR GO; GO:0046865; P:terpenoid transport; IMP:ARUK-UCL.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:MGI.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IMP:ARUK-UCL.
DR DisProt; DP02756; -.
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; IPR030258; MDR1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF251; PTHR24221:SF251; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1276
FT /note="ATP-dependent translocase ABCB1"
FT /id="PRO_0000093336"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 44..66
FT /note="Helical"
FT TOPO_DOM 67..112
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..133
FT /note="Helical"
FT TOPO_DOM 134..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 183..204
FT /note="Helical"
FT TOPO_DOM 205..211
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 212..232
FT /note="Helical"
FT TOPO_DOM 233..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 291..312
FT /note="Helical"
FT TOPO_DOM 313..326
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 327..348
FT /note="Helical"
FT TOPO_DOM 349..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 708..728
FT /note="Helical"
FT TOPO_DOM 729..752
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 753..773
FT /note="Helical"
FT TOPO_DOM 774..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 829..849
FT /note="Helical"
FT TOPO_DOM 850
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 851..870
FT /note="Helical"
FT TOPO_DOM 871..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 931..953
FT /note="Helical"
FT TOPO_DOM 954..969
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 970..991
FT /note="Helical"
FT TOPO_DOM 992..1276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 50..353
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 388..624
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 707..996
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1031..1269
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1066..1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06795"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 526..527
FT /note="QL -> HV (in Ref. 2; AAA39514 and 5; AAA03243)"
FT /evidence="ECO:0000305"
FT CONFLICT 939
FT /note="S -> F (in Ref. 1; AAA39517)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="V -> F (in Ref. 1; AAA39517)"
FT /evidence="ECO:0000305"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 44..82
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 96..153
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 184..206
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 208..232
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 234..255
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 279..318
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 324..366
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5KPD"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 418..427
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 480..485
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 513..516
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 529..543
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 592..598
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 608..614
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 617..625
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 699..703
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 704..737
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 744..794
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 797..800
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 802..805
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 807..815
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 816..819
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 820..824
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 826..849
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 851..885
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 887..898
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 900..906
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 909..961
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:4Q9H"
FT HELIX 967..988
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 994..1009
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1031..1038
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1049..1056
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1061..1067
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1072..1079
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1086..1092
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1097..1099
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1102..1107
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1109..1112
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1120..1122
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1123..1128
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1138..1147
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1151..1155
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1157..1159
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 1160..1162
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1164..1170
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1174..1188
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1191..1197
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1204..1217
FT /evidence="ECO:0007829|PDB:5KO2"
FT TURN 1218..1220
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1221..1226
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1230..1233
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1237..1243
FT /evidence="ECO:0007829|PDB:5KO2"
FT STRAND 1246..1251
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1253..1259
FT /evidence="ECO:0007829|PDB:5KO2"
FT HELIX 1262..1269
FT /evidence="ECO:0007829|PDB:5KO2"
SQ SEQUENCE 1276 AA; 140647 MW; 542E101DF18DDC52 CRC64;
MELEEDLKGR ADKNFSKMGK KSKKEKKEKK PAVSVLTMFR YAGWLDRLYM LVGTLAAIIH
GVALPLMMLI FGDMTDSFAS VGNVSKNSTN MSEADKRAMF AKLEEEMTTY AYYYTGIGAG
VLIVAYIQVS FWCLAAGRQI HKIRQKFFHA IMNQEIGWFD VHDVGELNTR LTDDVSKINE
GIGDKIGMFF QAMATFFGGF IIGFTRGWKL TLVILAISPV LGLSAGIWAK ILSSFTDKEL
HAYAKAGAVA EEVLAAIRTV IAFGGQKKEL ERYNNNLEEA KRLGIKKAIT ANISMGAAFL
LIYASYALAF WYGTSLVISK EYSIGQVLTV FFSVLIGAFS VGQASPNIEA FANARGAAYE
VFKIIDNKPS IDSFSKSGHK PDNIQGNLEF KNIHFSYPSR KEVQILKGLN LKVKSGQTVA
LVGNSGCGKS TTVQLMQRLY DPLDGMVSID GQDIRTINVR YLREIIGVVS QEPVLFATTI
AENIRYGRED VTMDEIEKAV KEANAYDFIM KLPHQFDTLV GERGAQLSGG QKQRIAIARA
LVRNPKILLL DEATSALDTE SEAVVQAALD KAREGRTTIV IAHRLSTVRN ADVIAGFDGG
VIVEQGNHDE LMREKGIYFK LVMTQTAGNE IELGNEACKS KDEIDNLDMS SKDSGSSLIR
RRSTRKSICG PHDQDRKLST KEALDEDVPP ASFWRILKLN STEWPYFVVG IFCAIINGGL
QPAFSVIFSK VVGVFTNGGP PETQRQNSNL FSLLFLILGI ISFITFFLQG FTFGKAGEIL
TKRLRYMVFK SMLRQDVSWF DDPKNTTGAL TTRLANDAAQ VKGATGSRLA VIFQNIANLG
TGIIISLIYG WQLTLLLLAI VPIIAIAGVV EMKMLSGQAL KDKKELEGSG KIATEAIENF
RTVVSLTREQ KFETMYAQSL QIPYRNAMKK AHVFGITFSF TQAMMYFSYA ACFRFGAYLV
TQQLMTFENV LLVFSAIVFG AMAVGQVSSF APDYAKATVS ASHIIRIIEK TPEIDSYSTQ
GLKPNMLEGN VQFSGVVFNY PTRPSIPVLQ GLSLEVKKGQ TLALVGSSGC GKSTVVQLLE
RFYDPMAGSV FLDGKEIKQL NVQWLRAQLG IVSQEPILFD CSIAENIAYG DNSRVVSYEE
IVRAAKEANI HQFIDSLPDK YNTRVGDKGT QLSGGQKQRI AIARALVRQP HILLLDEATS
ALDTESEKVV QEALDKAREG RTCIVIAHRL STIQNADLIV VIQNGKVKEH GTHQQLLAQK
GIYFSMVSVQ AGAKRS
