MRP2_RAT
ID MRP2_RAT Reviewed; 1541 AA.
AC Q63120; Q63145;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=ATP-binding cassette sub-family C member 2;
DE EC=7.6.2.- {ECO:0000269|PubMed:10421658, ECO:0000269|PubMed:11248200};
DE EC=7.6.2.2 {ECO:0000269|PubMed:10220572};
DE EC=7.6.2.3 {ECO:0000269|PubMed:10220572, ECO:0000269|PubMed:8662992};
DE AltName: Full=Canalicular multidrug resistance protein;
DE AltName: Full=Canalicular multispecific organic anion transporter 1 {ECO:0000305};
DE AltName: Full=Multidrug resistance-associated protein 2 {ECO:0000250|UniProtKB:Q92887};
GN Name=Abcc2 {ECO:0000312|RGD:2366};
GN Synonyms=Cmoat, Cmrp {ECO:0000303|PubMed:8662992}, Mrp2;
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].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8599091; DOI=10.1126/science.271.5252.1126;
RA Paulusma C.C., Bosma P.J., Zaman G.J.R., Bakker C.T.M., Otter M.,
RA Scheffer G.L., Scheper R.J., Borst P., Oude Elferink R.P.J.;
RT "Congenital jaundice in rats with a mutation in a multidrug resistance-
RT associated protein gene.";
RL Science 271:1126-1128(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN EHBR, FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN EHBR.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Ito K., Suzuki H., Hirohashi T., Kume K., Shimizu T., Sugiyama Y.;
RT "Expression of the putative ATP-binding cassette region, homologous to that
RT in multidrug resistance associated protein (MRP), is hereditarily defective
RT in Eisai hyperbilirubinemic rats (EHBR).";
RL Int. Hepatol. Commun. 292:292-299(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-281 AND SER-874, AND
RP IDENTIFICATION BY 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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10421658; DOI=10.1002/hep.510300220;
RA Kamisako T., Leier I., Cui Y., Koenig J., Buchholz U.,
RA Hummel-Eisenbeiss J., Keppler D.;
RT "Transport of monoglucuronosyl and bisglucuronosyl bilirubin by recombinant
RT human and rat multidrug resistance protein 2.";
RL Hepatology 30:485-490(1999).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10220572;
RA Cui Y., Koenig J., Buchholz J.K., Spring H., Leier I., Keppler D.;
RT "Drug resistance and ATP-dependent conjugate transport mediated by the
RT apical multidrug resistance protein, MRP2, permanently expressed in human
RT and canine cells.";
RL Mol. Pharmacol. 55:929-937(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11248200; DOI=10.1016/s0005-2736(00)00355-2;
RA Akita H., Suzuki H., Ito K., Kinoshita S., Sato N., Takikawa H.,
RA Sugiyama Y.;
RT "Characterization of bile acid transport mediated by multidrug resistance
RT associated protein 2 and bile salt export pump.";
RL Biochim. Biophys. Acta 1511:7-16(2001).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that binds and hydrolyzes ATP to enable active transport of
CC various substrates including many drugs, toxicants and endogenous
CC compound across cell membranes. Transports a wide variety of conjugated
CC organic anions such as sulfate-, glucuronide- and glutathione (GSH)-
CC conjugates of endo- and xenobiotics substrates (PubMed:8662992,
CC PubMed:10421658, PubMed:10220572, PubMed:11248200). Mediates
CC hepatobiliary excretion of mono- and bis-glucuronidated bilirubin
CC molecules and therefore play an important role in bilirubin
CC detoxification (PubMed:10421658). Mediates also hepatobiliary excretion
CC of others glucuronide conjugates such as 17beta-estradiol 17-
CC glucosiduronic acid and leukotriene C4 (PubMed:10220572,
CC PubMed:8662992). Transports sulfated bile salt such as
CC taurolithocholate sulfate (PubMed:11248200). Transport various
CC anticancer drugs, such as anthracycline, vinca alkaloid and
CC methotrexate and HIV-drugs such as protease inhibitors (By similarity).
CC {ECO:0000250|UniProtKB:Q92887, ECO:0000269|PubMed:10220572,
CC ECO:0000269|PubMed:10421658, ECO:0000269|PubMed:11248200,
CC ECO:0000269|PubMed:8662992}.
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:0000269|PubMed:10220572, ECO:0000269|PubMed:8662992};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000305|PubMed:10220572, ECO:0000305|PubMed:8662992};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) +
CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:11248200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085;
CC Evidence={ECO:0000269|PubMed:11248200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000269|PubMed:10220572};
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:0000269|PubMed:10220572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000269|PubMed:10220572};
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:0000269|PubMed:10220572, ECO:0000269|PubMed:8662992};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000305|PubMed:10220572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-glucuronoside(in) + H2O = ADP + bilirubin-
CC glucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57767, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10421658};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181;
CC Evidence={ECO:0000305|PubMed:10421658};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-bisglucuronoside(in) + H2O = ADP + bilirubin-
CC bisglucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58471, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:10421658};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for taurolithocholate 3-sulfate
CC {ECO:0000269|PubMed:11248200};
CC KM=6.9 uM for 17beta-estradiol 17-O-(beta-D-glucuronate)
CC {ECO:0000269|PubMed:10220572};
CC KM=1.1 uM for leukotriene C4 {ECO:0000269|PubMed:10220572};
CC KM=0.8 uM for bilirubin-glucuronoside {ECO:0000269|PubMed:10421658};
CC KM=0.5 uM for bilirubin-bisglucuronoside
CC {ECO:0000269|PubMed:10421658};
CC Vmax=1486 pmol/min/mg enzyme for taurolithocholate 3-sulfate
CC {ECO:0000269|PubMed:11248200};
CC Vmax=152 pmol/min/mg enzyme for bilirubin-glucuronoside transport
CC {ECO:0000269|PubMed:10421658};
CC Vmax=264 pmol/min/mg enzyme bilirubin-bisglucuronoside transport
CC {ECO:0000269|PubMed:10421658};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10220572, ECO:0000269|PubMed:8662992}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localized to the canalicular
CC membrane of hepatocytes. {ECO:0000269|PubMed:8662992}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the liver.
CC {ECO:0000269|PubMed:8662992}.
CC -!- DISEASE: Note=Defects in Abcc2 are a cause of hereditary conjugated
CC hyperbilirubinemia (EHBR). {ECO:0000269|PubMed:8599091,
CC ECO:0000269|Ref.3}.
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; L49379; AAC42087.1; -; mRNA.
DR EMBL; X96393; CAA65257.1; -; mRNA.
DR EMBL; D86086; BAA13016.1; -; mRNA.
DR PIR; S71839; S71839.
DR RefSeq; NP_036965.1; NM_012833.2.
DR AlphaFoldDB; Q63120; -.
DR SMR; Q63120; -.
DR BioGRID; 247342; 1.
DR IntAct; Q63120; 2.
DR MINT; Q63120; -.
DR STRING; 10116.ENSRNOP00000064799; -.
DR BindingDB; Q63120; -.
DR ChEMBL; CHEMBL2073676; -.
DR CarbonylDB; Q63120; -.
DR GlyGen; Q63120; 4 sites.
DR iPTMnet; Q63120; -.
DR PhosphoSitePlus; Q63120; -.
DR PaxDb; Q63120; -.
DR PRIDE; Q63120; -.
DR Ensembl; ENSRNOT00000070861; ENSRNOP00000064799; ENSRNOG00000046727.
DR GeneID; 25303; -.
DR KEGG; rno:25303; -.
DR CTD; 1244; -.
DR RGD; 2366; Abcc2.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161741; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; Q63120; -.
DR OMA; ICMATPV; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; Q63120; -.
DR BRENDA; 7.6.2.3; 5301.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR Reactome; R-RNO-9754706; Atorvastatin ADME.
DR SABIO-RK; Q63120; -.
DR PRO; PR:Q63120; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000046727; Expressed in liver and 10 other tissues.
DR Genevisible; Q63120; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
DR GO; GO:0046691; C:intracellular canaliculus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IMP:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015127; F:bilirubin transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:RGD.
DR GO; GO:0016999; P:antibiotic metabolic process; IMP:RGD.
DR GO; GO:1901086; P:benzylpenicillin metabolic process; IMP:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEP:RGD.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0015723; P:bilirubin transport; IMP:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; IMP:RGD.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IDA:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071354; P:cellular response to interleukin-6; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050787; P:detoxification of mercury ion; IMP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0071716; P:leukotriene transport; IMP:UniProtKB.
DR GO; GO:0015694; P:mercury ion transport; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0015711; P:organic anion transport; IMP:RGD.
DR GO; GO:0015732; P:prostaglandin transport; IMP:RGD.
DR GO; GO:0120188; P:regulation of bile acid secretion; IEP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IEP:RGD.
DR GO; GO:1904486; P:response to 17alpha-ethynylestradiol; IEP:RGD.
DR GO; GO:0097327; P:response to antineoplastic agent; IEP:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0033762; P:response to glucagon; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0070327; P:thyroid hormone transport; IMP:RGD.
DR GO; GO:0070633; P:transepithelial transport; IMP:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042178; P:xenobiotic catabolic process; IMP:RGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:RGD.
DR GO; GO:0046618; P:xenobiotic export from cell; ISO:RGD.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; IMP:UniProtKB.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IMP:ARUK-UCL.
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; IPR030247; ABCC2.
DR InterPro; IPR005292; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF176; PTHR24223:SF176; 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 TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
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..1541
FT /note="ATP-binding cassette sub-family C member 2"
FT /id="PRO_0000093359"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 48..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 89..92
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 114..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 126..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 147..164
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 165..185
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 186..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 310..330
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 331..356
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 357..377
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 378..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 434..454
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 455..457
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 458..478
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 479..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 541..561
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 562..583
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 584..604
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 605..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..1029
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1030..1050
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1051..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1094..1114
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1116..1136
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1137..1207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1208..1228
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1229..1230
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1231..1251
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1252..1541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 318..601
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 633..857
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 975..1260
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1296..1530
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 862..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 667..674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1330..1337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT MOD_RES 1434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92887"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 420
FT /note="M -> V (in Ref. 3; BAA13016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1541 AA; 173384 MW; D5FB55571BFDDB39 CRC64;
MDKFCNSTFW DLSLLESPEA DLPLCFEQTV LVWIPLGFLW LLAPWQLYSV YRSRTKRSSI
TKFYLAKQVF VVFLLILAAI DLSLALTEDT GQATVPPVRY TNPILYLCTW LLVLAVQHSR
QWCVRKNSWF LSLFWILSVL CGVFQFQTLI RALLKDSKSN MAYSYLFFVS YGFQIVLLIL
TAFSGPSDST QTPSVTASFL SSITFSWYDR TVLKGYKHPL TLEDVWDIDE GFKTRSVTSK
FEAAMTKDLQ KARQAFQRRL QKSQRKPEAT LHGLNKKQSQ SQDVLVLEEA KKKSEKTTKD
YPKSWLIKSL FKTFHVVILK SFILKLIHDL LVFLNPQLLK LLIGFVKSSN SYVWFGYICA
ILMFAVTLIQ SFCLQSYFQH CFVLGMCVRT TVMSSIYKKA LTLSNLARKQ YTIGETVNLM
SVDSQKLMDA TNYMQLVWSS VIQITLSIFF LWRELGPSIL AGVGVMVLLI PVNGVLATKI
RNIQVQNMKN KDKRLKIMNE ILSGIKILKY FAWEPSFQEQ VQGIRKKELK NLLRFGQLQS
LLIFILQITP ILVSVVTFSV YVLVDSANVL NAEKAFTSIT LFNILRFPLS MLPMVTSSIL
QASVSVDRLE RYLGGDDLDT SAIRRVSNFD KAVKFSEASF TWDPDLEATI QDVNLDIKPG
QLVAVVGTVG SGKSSLVSAM LGEMENVHGH ITIQGSTAYV PQQSWIQNGT IKDNILFGSE
YNEKKYQQVL KACALLPDLE ILPGGDMAEI GEKGINLSGG QKQRVSLARA AYQDADIYIL
DDPLSAVDAH VGKHIFNKVV GPNGLLAGKT RIFVTHGIHF LPQVDEIVVL GKGTILEKGS
YRDLLDKKGV FARNWKTFMK HSGPEGEATV NNDSEAEDDD DGLIPTMEEI PEDAASLAMR
RENSLRRTLS RSSRSSSRRG KSLKNSLKIK NVNVLKEKEK EVEGQKLIKK EFVETGKVKF
SIYLKYLQAV GWWSILFIIL FYGLNNVAFI GSNLWLSAWT SDSDNLNGTN NSSSHRDMRI
GVFGALGLAQ GICLLISTLW SIYACRNASK ALHGQLLTNI LRAPMRFFDT TPTGRIVNRF
SGDISTVDDL LPQTLRSWMM CFFGIAGTLV MICMATPVFA IIIIPLSILY ISVQVFYVAT
SRQLRRLDSV TKSPIYSHFS ETVTGLPIIR AFEHQQRFLA WNEKQIDINQ KCVFSWITSN
RWLAIRLELV GNLVVFCSAL LLVIYRKTLT GDVVGFVLSN ALNITQTLNW LVRMTSEAET
NIVAVERISE YINVENEAPW VTDKRPPADW PRHGEIQFNN YQVRYRPELD LVLKGITCNI
KSGEKVGVVG RTGAGKSSLT NCLFRILESA GGQIIIDGID VASIGLHDLR ERLTIIPQDP
ILFSGSLRMN LDPFNKYSDE EVWRALELAH LRSFVSGLQL GLLSEVTEGG DNLSIGQRQL
LCLGRAVLRK SKILVLDEAT AAVDLETDSL IQTTIRKEFS QCTVITIAHR LHTIMDSDKI
MVLDNGKIVE YGSPEELLSN RGSFYLMAKE AGIENVNHTE L
