MRP1_MOUSE
ID MRP1_MOUSE Reviewed; 1528 AA.
AC O35379;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000305};
DE EC=7.6.2.2 {ECO:0000269|PubMed:9281595};
DE AltName: Full=ATP-binding cassette sub-family C member 1;
DE AltName: Full=Glutathione-S-conjugate-translocating ATPase ABCC1 {ECO:0000305};
DE EC=7.6.2.3 {ECO:0000269|PubMed:9359705};
DE AltName: Full=Leukotriene C(4) transporter;
DE Short=LTC4 transporter;
GN Name=Abcc1 {ECO:0000312|MGI:MGI:102676};
GN Synonyms=Abcc1a, Abcc1b, Mdrap, Mrp;
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].
RC TISSUE=Muscle;
RX PubMed=8649356;
RA Stride B.D., Valdimarsson G., Gerlach J.H., Wilson G.M., Cole S.P.C.,
RA Deeley R.G.;
RT "Structure and expression of the messenger RNA encoding the murine
RT multidrug resistance protein, an ATP-binding cassette transporter.";
RL Mol. Pharmacol. 49:962-971(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9281595; DOI=10.1124/mol.52.3.344;
RA Stride B.D., Grant C.E., Loe D.W., Hipfner D.R., Cole S.P.C., Deeley R.G.;
RT "Pharmacological characterization of the murine and human orthologs of
RT multidrug-resistance protein in transfected human embryonic kidney cells.";
RL Mol. Pharmacol. 52:344-353(1997).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=9359705; DOI=10.1038/nm1197-1275;
RA Wijnholds J., Evers R., van Leusden M.R., Mol C.A., Zaman G.J., Mayer U.,
RA Beijnen J.H., van der Valk M., Krimpenfort P., Borst P.;
RT "Increased sensitivity to anticancer drugs and decreased inflammatory
RT response in mice lacking the multidrug resistance-associated protein.";
RL Nat. Med. 3:1275-1279(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-882, 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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-277; SER-290; SER-878 AND
RP SER-882, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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 [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-504, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (PubMed:9281595, PubMed:9359705). Hydrolyzes ATP with low efficiency.
CC Catalyzes the export of sphingosine 1-phosphate from mast cells
CC independently of their degranulation (By similarity). Participates in
CC inflammatory response by allowing export of leukotriene C4 from
CC leukotriene C4-synthezing cells (PubMed:9359705).
CC {ECO:0000250|UniProtKB:P33527, ECO:0000269|PubMed:9281595,
CC ECO:0000269|PubMed:9359705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:9359705};
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:9359705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000269|PubMed:9359705};
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:9281595, ECO:0000269|PubMed:9359705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000269|PubMed:9281595};
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:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
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 + 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:0000269|PubMed:9281595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161;
CC Evidence={ECO:0000269|PubMed:9281595};
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 -!- ACTIVITY REGULATION: MK 571 inhibits sphingosine 1-phosphate and
CC leukotriene C4 export. {ECO:0000250|UniProtKB:P33527}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 nM for leukotriene C4 {ECO:0000269|PubMed:9281595};
CC KM=3.3 nM for S-(2,4-dinitrophenyl)glutathione
CC {ECO:0000269|PubMed:9359705};
CC Vmax=350 pmol/min/mg enzyme for leukotriene C4 transport
CC {ECO:0000269|PubMed:9281595};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DISRUPTION PHENOTYPE: Homozygous ABCC1 knockout mice are healthy and
CC fertile up to at least 12 months of age. They are hypersensitive to
CC anticancer drugs resulting in an increased loss of body weight and
CC mortality and have a decreased inflammatory response.
CC {ECO:0000269|PubMed:9359705}.
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; AF022908; AAB80938.1; -; mRNA.
DR EMBL; AK029876; BAC26654.1; -; mRNA.
DR CCDS; CCDS37264.1; -.
DR RefSeq; NP_032602.1; NM_008576.3.
DR AlphaFoldDB; O35379; -.
DR SMR; O35379; -.
DR BioGRID; 201374; 7.
DR STRING; 10090.ENSMUSP00000097743; -.
DR BindingDB; O35379; -.
DR ChEMBL; CHEMBL2532; -.
DR SwissLipids; SLP:000000463; -.
DR GlyGen; O35379; 2 sites.
DR iPTMnet; O35379; -.
DR PhosphoSitePlus; O35379; -.
DR SwissPalm; O35379; -.
DR EPD; O35379; -.
DR jPOST; O35379; -.
DR MaxQB; O35379; -.
DR PaxDb; O35379; -.
DR PRIDE; O35379; -.
DR ProteomicsDB; 291409; -.
DR Antibodypedia; 4235; 578 antibodies from 50 providers.
DR DNASU; 17250; -.
DR Ensembl; ENSMUST00000100167; ENSMUSP00000097743; ENSMUSG00000023088.
DR GeneID; 17250; -.
DR KEGG; mmu:17250; -.
DR UCSC; uc007yhj.2; mouse.
DR CTD; 4363; -.
DR MGI; MGI:102676; Abcc1.
DR VEuPathDB; HostDB:ENSMUSG00000023088; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000160271; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; O35379; -.
DR OMA; IRYDFTP; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; O35379; -.
DR TreeFam; TF105199; -.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR Reactome; R-MMU-9758890; Transport of RCbl within the body.
DR BioGRID-ORCS; 17250; 9 hits in 79 CRISPR screens.
DR ChiTaRS; Abcc1; mouse.
DR PRO; PR:O35379; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O35379; protein.
DR Bgee; ENSMUSG00000023088; Expressed in stroma of bone marrow and 244 other tissues.
DR ExpressionAtlas; O35379; baseline and differential.
DR Genevisible; O35379; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IMP:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IMP:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IMP:MGI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
DR GO; GO:0042887; F:amide transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; 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:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0009235; P:cobalamin metabolic process; IMP:MGI.
DR GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0034775; P:glutathione transmembrane transport; ISO:MGI.
DR GO; GO:0071716; P:leukotriene transport; IMP:UniProtKB.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR GO; GO:0099039; P:sphingolipid translocation; ISO:MGI.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISO:MGI.
DR GO; GO:0042908; P:xenobiotic transport; IMP:ARUK-UCL.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:MGI.
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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1528
FT /note="Multidrug resistance-associated protein 1"
FT /id="PRO_0000093353"
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..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 964..984
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 985..1022
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1023..1043
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1044..1086
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1087..1107
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1109..1129
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1130..1200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1201..1221
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1222..1223
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1224..1244
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1245..1528
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 644..868
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 971..1253
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1290..1524
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 876..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 678..685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1324..1331
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:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1528 AA; 171185 MW; 68FD13667D61DBBB CRC64;
MALRSFCSAD GSDPLWDWNV TWHTSNPDFT KCFQNTVLTW VPCFYLWSCF PLYFFYLSRH
DRGYIQMTHL NKTKTALGFF LWIICWADLF YSFWERSQGV LRAPVLLVSP TLLGITMLLA
TFLIQLERRK GVQSSGIMLT FWLVALLCAL AILRSKIISA LKKDAHVDVF RDSTFYLYFT
LVLVQLVLSC FSDCSPLFSE TVHDRNPCPE SSASFLSRIT FWWITGMMVH GYRQPLESSD
LWSLNKEDTS EEVVPVLVNN WKKECDKSRK QPVRIVYAPP KDPSKPKGSS QLDVNEEVEA
LIVKSPHKDR EPSLFKVLYK TFGPYFLMSF LYKALHDLMM FAGPKILELI INFVNDREAP
DWQGYFYTAL LFVSACLQTL ALHQYFHICF VSGMRIKTAV VGAVYRKALL ITNAARKSST
VGEIVNLMSV DAQRFMDLAT YINMIWSAPL QVILALYFLW LSLGPSVLAG VAVMILMVPL
NAVMAMKTKT YQVAHMKSKD NRIKLMNEIL NGIKVLKLYA WELAFQDKVM SIRQEELKVL
KKSAYLAAVG TFTWVCTPFL VALSTFAVFV TVDERNILDA KKAFVSLALF NILRFPLNIL
PMVISSIVQA SVSLKRLRIF LSHEELEPDS IERRSIKSGE GNSITVKNAT FTWARGEPPT
LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVTLKGSVAY VPQQAWIQND
SLRENILFGH PLQENYYKAV MEACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR
AVYSNSDIYL FDDPLSAVDA HVGKHIFEKV VGPMGLLKNK TRILVTHGIS YLPQVDVIIV
MSGGKISEMG SYQELLDRDG AFAEFLRTYA NAEQDLASED DSVSGSGKES KPVENGMLVT
DTVGKHLQRH LSNSSSHSGD TSQQHSSIAE LQKAGAKEET WKLMEADKAQ TGQVQLSVYW
NYMKAIGLFI TFLSIFLFLC NHVSALASNY WLSLWTDDPP VVNGTQANRN FRLSVYGALG
ILQGAAIFGY SMAVSIGGIF ASRRLHLDLL YNVLRSPMSF FERTPSGNLV NRFSKELDTV
DSMIPQVIKM FMGSLFSVIG AVIIILLATP IAAVIIPPLG LVYFFVQRFY VASSRQLKRL
ESVSRSPVYS HFNETLLGVS VIRAFEEQER FIHQSDLKVD ENQKAYYPSI VANRWLAVRL
ECVGNCIVLF AALFAVISRH SLSAGLVGLS VSYSLQITAY LNWLVRMSSE METNIVAVER
LKEYSETEKE APWQIQETAP PSTWPHSGRV EFRDYCLRYR EDLDLVLKHI NVTIEGGEKV
GIVGRTGAGK SSLTLGLFRI NESAEGEIII DGVNIAKIGL HNLRFKITII PQDPVLFSGS
LRMNLDPFSQ YSDEEVWMAL ELAHLKGFVS ALPDKLNHEC AEGGENLSVG QRQLVCLARA
LLRKTKILVL DEATAAVDLE TDNLIQSTIR TQFEDCTVLT IAHRLNTIMD YTRVIVLDKG
EVRECGAPSE LLQQRGIFYS MAKDAGLV
