MRP1_RAT
ID MRP1_RAT Reviewed; 1532 AA.
AC Q8CG09; Q63346; Q810E4; Q810G9; Q9JHS0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000305};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:P33527};
DE AltName: Full=ATP-binding cassette sub-family C member 1;
DE AltName: Full=Glutathione-S-conjugate-translocating ATPase ABCC1 {ECO:0000250|UniProtKB:O35379};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O35379};
DE AltName: Full=Leukotriene C(4) transporter;
DE Short=LTC4 transporter;
GN Name=Abcc1 {ECO:0000312|RGD:3112}; Synonyms=Mrp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12423064; DOI=10.1208/ps040315;
RA Yang Z., Li C.S.W., Shen D.D., Ho R.J.Y.;
RT "Cloning and characterization of the rat multidrug resistance-associated
RT protein 1.";
RL AAPS PharmSci 4:E15-E15(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF LEU-983; GLN-1090; SER-1101; VAL-1106 AND ALA-1243.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=12867490; DOI=10.1124/dmd.31.8.1016;
RA Nunoya K., Grant C.E., Zhang D.-W., Cole S.P.C., Deeley R.G.;
RT "Molecular cloning and pharmacological characterization of rat multidrug
RT resistance protein 1 (mrp1).";
RL Drug Metab. Dispos. 31:1016-1026(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA Yabuuchi H., Takayanagi S., Ishikawa T.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Spleen;
RA Takayanagi S., Ishikawa T.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 711-1532 (ISOFORM 1).
RX PubMed=11208926; DOI=10.1046/j.1471-4159.2001.00101.x;
RA Hirrlinger J., Koenig J., Keppler D., Lindenau J., Schulz J.B., Dringen R.;
RT "The multidrug resistance protein MRP1 mediates the release of glutathione
RT disulfide from rat astrocytes during oxidative stress.";
RL J. Neurochem. 76:627-636(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1426-1532 (ISOFORMS 1/2).
RX PubMed=8662992; DOI=10.1074/jbc.271.25.15091;
RA Buechler M., Koenig J., Brom M., Kartenbeck J., Spring H., Horie T.,
RA Keppler D.;
RT "cDNA cloning of the hepatocyte canalicular isoform of the multidrug
RT resistance protein, cMrp, reveals a novel conjugate export pump deficient
RT in hyperbilirubinemic mutant rats.";
RL J. Biol. Chem. 271:15091-15098(1996).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15129170; DOI=10.1097/00001756-200405190-00020;
RA Dallas S., Ronaldson P.T., Bendayan M., Bendayan R.;
RT "Multidrug resistance protein 1-mediated transport of saquinavir by
RT microglia.";
RL NeuroReport 15:1183-1186(2004).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=17050692; DOI=10.1073/pnas.0603734103;
RA Mitra P., Oskeritzian C.A., Payne S.G., Beaven M.A., Milstien S.,
RA Spiegel S.;
RT "Role of ABCC1 in export of sphingosine-1-phosphate from mast cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16394-16399(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-879, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Mediates export of organic anions and drugs from the
CC cytoplasm. Mediates ATP-dependent transport of glutathione and
CC glutathione conjugates, leukotriene C4, estradiol-17-beta-o-
CC glucuronide, methotrexate, antiviral drugs and other xenobiotics.
CC Confers resistance to anticancer drugs by decreasing accumulation of
CC drug in cells, and by mediating ATP- and GSH-dependent drug export.
CC Hydrolyzes ATP with low efficiency (PubMed:15129170). Catalyzes the
CC export of sphingosine 1-phosphate from mast cells independently of
CC their degranulation (PubMed:17050692). Participates in inflammatory
CC response by allowing export of leukotriene C4 from leukotriene C4-
CC synthezing cells (By similarity). {ECO:0000250|UniProtKB:O35379,
CC ECO:0000269|PubMed:15129170, ECO:0000269|PubMed:17050692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:O35379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O35379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) +
CC phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17050692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000269|PubMed:17050692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64677, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + vincristine(in) = ADP + H(+) + phosphate +
CC vincristine(out); Xref=Rhea:RHEA:60160, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:143658, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- ACTIVITY REGULATION: MK 571 inhibits sphingosine 1-phosphate and
CC leukotriene C4 export. {ECO:0000250|UniProtKB:P33527,
CC ECO:0000269|PubMed:17050692}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15129170};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:15129170}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CG09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CG09-2; Sequence=VSP_017015;
CC -!- TISSUE SPECIFICITY: Skeletal muscle, brain, heart, spleen, lung and
CC kidney. {ECO:0000269|PubMed:12867490}.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AY170916; AAN86532.1; -; mRNA.
DR EMBL; AF487549; AAO85437.1; -; mRNA.
DR EMBL; AY174892; AAO44983.1; -; mRNA.
DR EMBL; AJ277881; CAB97204.1; -; mRNA.
DR EMBL; X96394; CAA65258.1; -; mRNA.
DR RefSeq; NP_071617.2; NM_022281.2. [Q8CG09-1]
DR AlphaFoldDB; Q8CG09; -.
DR SMR; Q8CG09; -.
DR STRING; 10116.ENSRNOP00000041695; -.
DR ChEMBL; CHEMBL5680; -.
DR SwissLipids; SLP:000000405; -.
DR GlyGen; Q8CG09; 1 site.
DR iPTMnet; Q8CG09; -.
DR PhosphoSitePlus; Q8CG09; -.
DR jPOST; Q8CG09; -.
DR PaxDb; Q8CG09; -.
DR PRIDE; Q8CG09; -.
DR Ensembl; ENSRNOT00000044108; ENSRNOP00000044445; ENSRNOG00000022305. [Q8CG09-1]
DR GeneID; 24565; -.
DR KEGG; rno:24565; -.
DR UCSC; RGD:3112; rat. [Q8CG09-1]
DR CTD; 4363; -.
DR RGD; 3112; Abcc1.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000160271; -.
DR InParanoid; Q8CG09; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q8CG09; -.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR Reactome; R-RNO-9758890; Transport of RCbl within the body.
DR PRO; PR:Q8CG09; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; ISO:RGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:RGD.
DR GO; GO:0042887; F:amide transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:RGD.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IMP:RGD.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:1905039; P:carboxylic acid transmembrane transport; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0009235; P:cobalamin metabolic process; ISO:RGD.
DR GO; GO:0140115; P:export across plasma membrane; IDA:RGD.
DR GO; GO:0034775; P:glutathione transmembrane transport; IMP:RGD.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IDA:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0033700; P:phospholipid efflux; IMP:RGD.
DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0099039; P:sphingolipid translocation; ISO:RGD.
DR GO; GO:0070633; P:transepithelial transport; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IDA:RGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:RGD.
DR GO; GO:0042908; P:xenobiotic transport; IMP:RGD.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:RGD.
DR Gene3D; 1.20.1560.10; -; 2.
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; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR005292; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
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 TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Hydrolase;
KW Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1532
FT /note="Multidrug resistance-associated protein 1"
FT /id="PRO_0000093354"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 96..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..172
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 194..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 318..338
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 339..364
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 365..385
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 386..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..462
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 463..465
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 466..486
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 487..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 549..569
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 570..591
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 592..612
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 613..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 968..988
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 989..1026
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1027..1047
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1048..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1091..1111
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1112
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1113..1133
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1134..1204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1205..1225
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1226..1227
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1228..1248
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1249..1532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 326..609
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 645..869
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 975..1257
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1294..1528
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 679..686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1328..1335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 277
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 504
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 912..920
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_017015"
FT MUTAGEN 983
FT /note="L->M: No effect on estradiol glucuronide transport."
FT /evidence="ECO:0000269|PubMed:12867490"
FT MUTAGEN 1090
FT /note="Q->E: 7.6-fold increase of the estradiol glucuronide
FT transport; when associated with T-1243. Increases
FT doxorubicin inhibition."
FT /evidence="ECO:0000269|PubMed:12867490"
FT MUTAGEN 1101
FT /note="S->N: 50% increase of estradiol glucuronide
FT transport."
FT /evidence="ECO:0000269|PubMed:12867490"
FT MUTAGEN 1106
FT /note="V->C: No effect on estradiol glucuronide transport."
FT /evidence="ECO:0000269|PubMed:12867490"
FT MUTAGEN 1243
FT /note="A->T: 7.6-fold increase of the estradiol glucuronide
FT transport; when associated with E-1090."
FT /evidence="ECO:0000269|PubMed:12867490"
FT CONFLICT 4
FT /note="S -> R (in Ref. 1; AAN86532 and 4; AAO44983)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="F -> S (in Ref. 4; AAO44983)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="N -> S (in Ref. 5; CAB97204)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="R -> P (in Ref. 5; CAB97204)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="S -> G (in Ref. 5; CAB97204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="P -> T (in Ref. 5; CAB97204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="S -> P (in Ref. 1; AAN86532)"
FT /evidence="ECO:0000305"
FT CONFLICT 1473
FT /note="I -> V (in Ref. 1; AAN86532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1532 AA; 171493 MW; 2E6939F63F5A3F68 CRC64;
MALSSFCSSD GSDPLWDWNV TWHTSNPDFT KCFQNTVLTW VPCFYLWSCF PLYFLYLSRH
DRGYIQMTHL NKAKTALGFF LWIICWADLF YSFWERSQGM LLAPVLLVSP TLLGITMLLA
TFLIQFERRK GVQSSGIMLT FWLVALLCAL AILRSKIISA LKKDAQVDMF RDSAFYLYFT
LVFIQLVLSC FSDSSPLFSE TVRDPNPCPE SSASFLSRIT FWWITGMMVQ GYRQPLKSSD
LWSLNKEDTS EEVVPVLVNN WKKECVKSRK QPVRIVYAPP KDPTKPKGSS QLDVNEEVEA
LIVKSSHKDR DPSLFKVLYK TFGPYFLMSF LYKALHDLMM FAGPEILELI INFVNDREAP
DWQGYLYTAL LFVSACLQTL ALHQYFHICF VTGMRIKTAV VGAVYRKALV ITNSARKSST
VGEIVNLMSV DAQRFMDLAT YINMIWSAPL QVTLALYFLW LNLGPSVLAG VAVMILMVPF
NAVMAMKTKT YQVAHMKSKD NRIKLMNEIL NGIKVLKLYA WELAFQDKVM NIRQEELKVL
KKSAYLAAVG TFTWVCTPFL VALSTFAVFV TVDEKNILDA KKAFVSLALF NILRFPLNIL
PMVISSIVQA SVSLKRLRIF LSHEELEPDS IERWSIKDGG GMNSITVKNA TFTWARDEPP
TLNGITFAIP DGALVAVVGQ VGCGKSSLLS ALLAEMDKVE GHVTLKGSVA YVPQQAWIQN
DSLRENILFG RPLQEHCYKA VMEACALLPD LEILPSGDLT EIGEKGVNLS GGQKQRVSLA
RAVYCNSDIY LLDDPLSAVD AHVGKHIFEK VVGPMGLLKN KTRILVTHGI SYLPQVDVII
VMSGGKISEM GSYQELLDRD GAFAEFVRTY ANTEQDLASE DDSKNGVSGL GKESKPVENG
ILVTDAVGKP LQRHLSNSSS HSVVTNQQHS STAELQKSGV KEETWKLMEA DKAQTGQVKL
SVYWNYMKAI GLCISFLSIF LFLCNHVSAL ASNYWLSLWT DDRPAVNGTQ ENRNFRLSVY
GALGILQGVA VFGYSMAVSI GGIFASRRLH LDLLQNVLRS PMSFFERTPS GNLVNRFSKE
LDTVDSMIPQ VIKMFMGSLF SVIGAVIIIL LATPIAAVII PPLGLVYFFV QRFYVASSRQ
LKRLESVSRS PVYSHFNETL LGVSVIRAFE EQERFIRQSD LKVDENQKAY YPSIVANRWL
AVRLECVGNC IVLFAALFAV ISRHSLSAGL VGLSVSYSLQ ITAYLNWLVR MSSEMETNIV
AVERLKEYSE TEKEASWQIQ ETAPPSTWPH SGRVEFRDYC LRYREDLDLV LKHINVTIEG
GEKVGIVGRT GAGKSSLTLG LFRINESAEG EIIIDGINIA KIGLHNLRFK ITIIPQDPVL
FSGSLRMNLD PFSQYSDEEV WMALELAHLK GFVSALPDKL NHECAEGGEN LSVGQRQLVC
LARALLRKTK ILVLDEATAA VDLETDDLIQ STIRTQFEDS TVLTIAHRLN TIMDYTRVIV
LDKGEIRECG APSELLQQRG VFYSMAKDAG LV
