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   27-MAR-2024, entry version 147.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2',3'-cGAMP(in) + ATP + H2O = 2',3'-cGAMP(out) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:74887, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143093, ChEBI:CHEBI:456216;
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.ENSRNOP00000044445; -.
DR   ChEMBL; CHEMBL5680; -.
DR   SwissLipids; SLP:000000405; -.
DR   GlyCosmos; Q8CG09; 1 site, No reported glycans.
DR   GlyGen; Q8CG09; 1 site.
DR   iPTMnet; Q8CG09; -.
DR   PhosphoSitePlus; Q8CG09; -.
DR   SwissPalm; Q8CG09; -.
DR   jPOST; Q8CG09; -.
DR   PaxDb; 10116-ENSRNOP00000041695; -.
DR   Ensembl; ENSRNOT00000044108.6; ENSRNOP00000044445.6; ENSRNOG00000022305.6. [Q8CG09-1]
DR   Ensembl; ENSRNOT00055008467; ENSRNOP00055006416; ENSRNOG00055005263. [Q8CG09-1]
DR   Ensembl; ENSRNOT00060021216; ENSRNOP00060016730; ENSRNOG00060012339. [Q8CG09-1]
DR   Ensembl; ENSRNOT00065003510; ENSRNOP00065002429; ENSRNOG00065002611. [Q8CG09-1]
DR   GeneID; 24565; -.
DR   KEGG; rno:24565; -.
DR   UCSC; RGD:3112; rat. [Q8CG09-1]
DR   AGR; RGD:3112; -.
DR   CTD; 4363; -.
DR   RGD; 3112; Abcc1.
DR   eggNOG; KOG0054; Eukaryota.
DR   GeneTree; ENSGT00940000160271; -.
DR   InParanoid; Q8CG09; -.
DR   OMA; CFETGMR; -.
DR   OrthoDB; 3384185at2759; -.
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:0016328; C:lateral plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IDA:RGD.
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: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:0048708; P:astrocyte differentiation; IMP:RGD.
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:0015889; P:cobalamin transport; ISO:RGD.
DR   GO; GO:0070729; P:cyclic nucleotide transport; ISS:UniProtKB.
DR   GO; GO:0140115; P:export across plasma membrane; IDA:RGD.
DR   GO; GO:0010001; P:glial cell differentiation; IMP: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: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:2001038; P:regulation of cellular response to drug; IDA:RGD.
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   CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR   CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR005292; MRP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00957; MRP_assoc_pro; 1.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF241; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1; 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   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
//