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 27-MAR-2024, entry version 198. 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 {ECO:0000250|UniProtKB:P08183}; 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. C1orf115 regulates drug efflux CC through modulation of ABCB1 localization and activity. CC {ECO:0000250|UniProtKB:P08183}. CC -!- SUBUNIT: Interacts with PSMB5. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08183}; CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC Apical cell membrane {ECO:0000269|PubMed:8898203}. Cytoplasm CC {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced CC by C1orf115 expression levels (plasma membrane versus cytoplasm). CC {ECO:0000250|UniProtKB:P08183}. 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 PDB; 7ZK4; EM; 2.60 A; A=1-1276. DR PDB; 7ZK5; EM; 2.60 A; A=1-1276. DR PDB; 7ZK6; EM; 3.10 A; A=1-1276. DR PDB; 7ZK7; EM; 3.20 A; A=1-1276. DR PDB; 7ZK8; EM; 3.00 A; A=1-1271. DR PDB; 7ZK9; EM; 4.30 A; A=1-1260. DR PDB; 7ZKA; EM; 2.90 A; A=1-1276. DR PDB; 7ZKB; EM; 4.70 A; A=1-1276. DR PDB; 8AVY; EM; 2.90 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 PDBsum; 7ZK4; -. DR PDBsum; 7ZK5; -. DR PDBsum; 7ZK6; -. DR PDBsum; 7ZK7; -. DR PDBsum; 7ZK8; -. DR PDBsum; 7ZK9; -. DR PDBsum; 7ZKA; -. DR PDBsum; 7ZKB; -. DR PDBsum; 8AVY; -. DR AlphaFoldDB; P21447; -. DR EMDB; EMD-13059; -. DR EMDB; EMD-13060; -. DR EMDB; EMD-14758; -. DR EMDB; EMD-14759; -. DR EMDB; EMD-15687; -. DR EMDB; EMD-4391; -. 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 GlyCosmos; P21447; 3 sites, No reported glycans. DR GlyGen; P21447; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; P21447; -. DR PhosphoSitePlus; P21447; -. DR EPD; P21447; -. DR jPOST; P21447; -. DR MaxQB; P21447; -. DR PaxDb; 10090-ENSMUSP00000041204; -. DR PeptideAtlas; P21447; -. DR ProteomicsDB; 295845; -. DR ABCD; P21447; 2 sequenced antibodies. DR DNASU; 18671; -. DR Ensembl; ENSMUST00000047753.5; ENSMUSP00000041204.5; ENSMUSG00000040584.9. DR GeneID; 18671; -. DR KEGG; mmu:18671; -. DR UCSC; uc008wkl.1; mouse. DR AGR; MGI:97570; -. 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; RSDANFW; -. DR OrthoDB; 5487044at2759; -. 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 Reactome; R-MMU-9757110; Prednisone ADME. DR BioGRID-ORCS; 18671; 4 hits in 77 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 205 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL. DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI. DR GO; GO:0016020; C:membrane; 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: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; IEA:Ensembl. DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl. DR GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0050892; P:intestinal absorption; IEA:Ensembl. DR GO; GO:0007595; P:lactation; IEA:Ensembl. DR GO; GO:0035633; P:maintenance of blood-brain barrier; IEA:Ensembl. DR GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL. DR GO; GO:0001890; P:placenta development; IEA:Ensembl. DR GO; GO:1904446; P:positive regulation of establishment of Sertoli cell barrier; IEA:Ensembl. DR GO; GO:2001025; P:positive regulation of response to drug; IEA:Ensembl. DR GO; GO:1902396; P:protein localization to bicellular tight junction; IEA:Ensembl. DR GO; GO:2001225; P:regulation of chloride transport; ISO:MGI. DR GO; GO:1904478; P:regulation of intestinal absorption; IEA:Ensembl. 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: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: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 CDD; cd18558; ABC_6TM_Pgp_ABCB1; 2. DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2. DR DisProt; DP02756; -. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. 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. DR Genevisible; P21447; MM. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; KW Direct protein sequencing; Glycoprotein; Membrane; Nucleotide-binding; KW Phosphoprotein; 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 //