MDR1B_MOUSE
ID MDR1B_MOUSE Reviewed; 1276 AA.
AC P06795;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=ATP-dependent translocase ABCB1 {ECO:0000250|UniProtKB:P08183};
DE AltName: Full=ATP-binding cassette sub-family B member 1B;
DE AltName: Full=Multidrug resistance protein 1B;
DE EC=7.6.2.2;
DE AltName: Full=P-glycoprotein 1;
DE AltName: Full=Phospholipid transporter ABCB1 {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:P08183};
DE AltName: CD_antigen=CD243;
GN Name=Abcb1b {ECO:0000312|MGI:MGI:97568};
GN Synonyms=Abcb1, Mdr1, Mdr1b, Pgy1, Pgy1-1;
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].
RX PubMed=3768958; DOI=10.1016/0092-8674(86)90594-5;
RA Gros P., Croop J., Housman D.;
RT "Mammalian multidrug resistance gene: complete cDNA sequence indicates
RT strong homology to bacterial transport proteins.";
RL Cell 47:371-380(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2570420; DOI=10.1073/pnas.86.17.6488;
RA Raymond M., Gros P.;
RT "Mammalian multidrug-resistance gene: correlation of exon organization with
RT structural domains and duplication of an ancestral gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6488-6492(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2248681; DOI=10.1128/mcb.10.11.6036-6040.1990;
RA Raymond M., Gros P.;
RT "Cell-specific activity of cis-acting regulatory elements in the promoter
RT of the mouse multidrug resistance gene mdr1.";
RL Mol. Cell. Biol. 10:6036-6040(1990).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-641 AND SER-659, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(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. Energy-dependent efflux pump
CC responsible for decreased drug accumulation in multidrug-resistant
CC cells. {ECO:0000250|UniProtKB:P08183}.
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:0000250|UniProtKB:P08183};
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:0000250|UniProtKB:P08183};
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:0000250|UniProtKB:P08183};
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:0000250|UniProtKB:P08183};
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:0000250|UniProtKB:P08183};
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:0000250|UniProtKB:P08183}.
CC -!- PTM: Several phosphorylated serine residues are present in the linker
CC domain.
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}.
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DR EMBL; M14757; AAA79005.1; -; mRNA.
DR EMBL; M60348; AAA39513.1; -; Genomic_DNA.
DR CCDS; CCDS19085.1; -.
DR PIR; A33719; DVMS1.
DR RefSeq; NP_035205.1; NM_011075.2.
DR AlphaFoldDB; P06795; -.
DR SMR; P06795; -.
DR BioGRID; 202138; 1.
DR STRING; 10090.ENSMUSP00000009058; -.
DR BindingDB; P06795; -.
DR ChEMBL; CHEMBL3467; -.
DR GlyGen; P06795; 4 sites.
DR iPTMnet; P06795; -.
DR PhosphoSitePlus; P06795; -.
DR SwissPalm; P06795; -.
DR EPD; P06795; -.
DR jPOST; P06795; -.
DR MaxQB; P06795; -.
DR PaxDb; P06795; -.
DR PRIDE; P06795; -.
DR ProteomicsDB; 293447; -.
DR DNASU; 18669; -.
DR Ensembl; ENSMUST00000009058; ENSMUSP00000009058; ENSMUSG00000028970.
DR GeneID; 18669; -.
DR KEGG; mmu:18669; -.
DR UCSC; uc008wko.2; mouse.
DR CTD; 18669; -.
DR MGI; MGI:97568; Abcb1b.
DR VEuPathDB; HostDB:ENSMUSG00000028970; -.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000155287; -.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; P06795; -.
DR OMA; CMALCFW; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; P06795; -.
DR TreeFam; TF105193; -.
DR SABIO-RK; P06795; -.
DR BioGRID-ORCS; 18669; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Abcb1b; mouse.
DR PRO; PR:P06795; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P06795; protein.
DR Bgee; ENSMUSG00000028970; Expressed in adrenal gland and 150 other tissues.
DR ExpressionAtlas; P06795; baseline and differential.
DR Genevisible; P06795; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0098591; C:external side of apical plasma membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; 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:0005739; C:mitochondrion; HDA: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:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0099038; F:ceramide floppase activity; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0140328; F:floppase activity; ISS:UniProtKB.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:MGI.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:1905039; P:carboxylic acid transmembrane transport; ISO:MGI.
DR GO; GO:0099040; P:ceramide translocation; ISO:MGI.
DR GO; GO:0014045; P:establishment of endothelial blood-brain barrier; ISO:MGI.
DR GO; GO:0140115; P:export across plasma membrane; ISO:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
DR GO; GO:1901529; P:positive regulation of anion channel activity; ISO:MGI.
DR GO; GO:2001225; P:regulation of chloride transport; ISO:MGI.
DR GO; GO:0047484; P:regulation of response to osmotic stress; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0061843; P:Sertoli cell barrier remodeling; ISO:MGI.
DR GO; GO:0072089; P:stem cell proliferation; ISO:MGI.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISO:MGI.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:MGI.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Lipid transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1276
FT /note="ATP-dependent translocase ABCB1"
FT /id="PRO_0000093334"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 67..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 137..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 208..214
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 236..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 316..329
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..351
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 352..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 731..754
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 776..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 852
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 853..872
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 873..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 933..955
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 956..971
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 972..993
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 994..1276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 50..356
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 391..627
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 709..998
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1033..1271
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 633..659
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 633..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1068..1075
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 641
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1276 AA; 140994 MW; 1804D0F011B0FF4E CRC64;
MEFEENLKGR ADKNFSKMGK KSKKEKKEKK PAVGVFGMFR YADWLDKLCM ILGTLAAIIH
GTLLPLLMLV FGNMTDSFTK AEASILPSIT NQSGPNSTLI ISNSSLEEEM AIYAYYYTGI
GAGVLIVAYI QVSLWCLAAG RQIHKIRQKF FHAIMNQEIG WFDVHDVGEL NTRLTDDVSK
INDGIGDKIG MFFQSITTFL AGFIIGFISG WKLTLVILAV SPLIGLSSAL WAKVLTSFTN
KELQAYAKAG AVAEEVLAAI RTVIAFGGQQ KELERYNKNL EEAKNVGIKK AITASISIGI
AYLLVYASYA LAFWYGTSLV LSNEYSIGEV LTVFFSILLG TFSIGHLAPN IEAFANARGA
AFEIFKIIDN EPSIDSFSTK GYKPDSIMGN LEFKNVHFNY PSRSEVQILK GLNLKVKSGQ
TVALVGNSGC GKSTTVQLMQ RLYDPLEGVV SIDGQDIRTI NVRYLREIIG VVSQEPVLFA
TTIAENIRYG REDVTMDEIE KAVKEANAYD FIMKLPHQFD TLVGERGAQL SGGQKQRIAI
ARALVRNPKI LLLDEATSAL DTESEAVVQA ALDKAREGRT TIVIAHRLST VRNADVIAGF
DGGVIVEQGN HDELMREKGI YFKLVMTQTR GNEIEPGNNA YGSQSDTDAS ELTSEESKSP
LIRRSIYRSV HRKQDQERRL SMKEAVDEDV PLVSFWRILN LNLSEWPYLL VGVLCAVING
CIQPVFAIVF SRIVGVFSRD DDHETKRQNC NLFSLFFLVM GLISFVTYFF QGFTFGKAGE
ILTKRVRYMV FKSMLRQDIS WFDDHKNSTG SLTTRLASDA SSVKGAMGAR LAVVTQNVAN
LGTGVILSLV YGWQLTLLLV VIIPLIVLGG IIEMKLLSGQ ALKDKKQLEI SGKIATEAIE
NFRTIVSLTR EQKFETMYAQ SLQVPYRNAM KKAHVFGITF SFTQAMMYFS YAACFRFGAY
LVAQQLMTFE NVMLVFSAVV FGAMAAGNTS SFAPDYAKAK VSASHIIRII EKTPEIDSYS
TEGLKPTLLE GNVKFNGVQF NYPTRPNIPV LQGLSLEVKK GQTLALVGSS GCGKSTVVQL
LERFYDPMAG SVFLDGKEIK QLNVQWLRAH LGIVSQEPIL FDCSIAENIA YGDNSRAVSH
EEIVRAAKEA NIHQFIDSLP DKYNTRVGDK GTQLSGGQKQ RIAIARALVR QPHILLLDEA
TSALDTESEK VVQEALDKAR EGRTCIVIAH RLSTIQNADL IVVIENGKVK EHGTHQQLLA
QKGIYFSMVQ AGAKRS
