MRP3_MOUSE
ID MRP3_MOUSE Reviewed; 1523 AA.
AC B2RX12; J3QML2; Q3U1W8; Q56PH0; Q59DK9; Q59DL0; Q5SUF4; Q80ZK8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP-binding cassette sub-family C member 3;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O15438};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:O15438};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O15438};
DE AltName: Full=Canalicular multispecific organic anion transporter 2;
DE AltName: Full=Multidrug resistance-associated protein 3;
GN Name=Abcc3; Synonyms=Cmoat2, Mrp3;
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] (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15814571; DOI=10.1124/mol.104.010587;
RA Belinsky M.G., Dawson P.A., Shchaveleva I., Bain L.J., Wang R., Ling V.,
RA Chen Z.-S., Grinberg A., Westphal H., Klein-Szanto A., Lerro A., Kruh G.D.;
RT "Analysis of the in vivo functions of Mrp3.";
RL Mol. Pharmacol. 68:160-168(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Shimizu H., Ishikawa T., Yabuuchi H.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4-1523 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Brain, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Spleen;
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 [8]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16225954; DOI=10.1016/j.jhep.2005.07.022;
RA Zelcer N., van de Wetering K., de Waart R., Scheffer G.L., Marschall H.U.,
RA Wielinga P.R., Kuil A., Kunne C., Smith A., van der Valk M., Wijnholds J.,
RA Elferink R.O., Borst P.;
RT "Mice lacking Mrp3 (Abcc3) have normal bile salt transport, but altered
RT hepatic transport of endogenous glucuronides.";
RL J. Hepatol. 44:768-775(2006).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that bind and hydrolyze ATP to enable active transport of
CC various substrates including many drugs, toxicants and endogenous
CC compound across cell membranes. Transports glucuronide conjugates such
CC as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH
CC conjugates such as leukotriene C4 (LTC4) (By similarity). Transports
CC also various bile salts (taurocholate, glycocholate,
CC taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By
CC similarity). Does not contribute substantially to bile salt physiology
CC but provides an alternative route for the export of bile acids and
CC glucuronides from cholestatic hepatocytes (PubMed:15814571,
CC PubMed:16225954). {ECO:0000250|UniProtKB:O15438,
CC ECO:0000269|PubMed:15814571, ECO:0000269|PubMed:16225954}.
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:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:O15438};
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:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP +
CC dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC Evidence={ECO:0000250|UniProtKB:O15438};
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:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O88563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000250|UniProtKB:O88563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O88563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC Evidence={ECO:0000250|UniProtKB:O88563};
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:0000250|UniProtKB:O88563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H(+)
CC + phosphate + taurochenodeoxycholate 3-sulfate(out);
CC Xref=Rhea:RHEA:66176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:166912,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66177;
CC Evidence={ECO:0000250|UniProtKB:O88563};
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:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181;
CC Evidence={ECO:0000250|UniProtKB:O15438};
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:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66193;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:16225954}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B2RX12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2RX12-2; Sequence=VSP_036012;
CC Name=3;
CC IsoId=B2RX12-3; Sequence=VSP_036011;
CC -!- TISSUE SPECIFICITY: Detected throughout the gastrointestinal tract,
CC liver, lung, pancreas, bladder, gall bladder and at low levels in the
CC adrenal gland. {ECO:0000269|PubMed:16225954}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice do not exhibit any overt phenotype
CC under normal conditions. However when challenged with cholestasis
CC induced by bile duct ligation, increased levels of hepatic bile salts
CC and lower serum levels of bilirubin glucuronide are observed,
CC suggesting that Abcc3 provides an alternative route for removal from
CC the liver of these substrates under cholestatic conditions.
CC {ECO:0000269|PubMed:15814571, ECO:0000269|PubMed:16225954}.
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; AY841885; AAX39010.1; -; mRNA.
DR EMBL; AY795569; AAX33774.1; -; mRNA.
DR EMBL; AF534127; AAQ10530.1; -; mRNA.
DR EMBL; AF534128; AAQ10531.1; -; mRNA.
DR EMBL; AK149551; BAE28953.1; -; mRNA.
DR EMBL; AK155664; BAE33375.1; -; mRNA.
DR EMBL; AL645965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048825; AAH48825.1; -; mRNA.
DR EMBL; BC150788; AAI50789.1; -; mRNA.
DR CCDS; CCDS25254.1; -. [B2RX12-2]
DR CCDS; CCDS88225.1; -. [B2RX12-1]
DR RefSeq; NP_083876.3; NM_029600.3. [B2RX12-2]
DR RefSeq; XP_006534491.1; XM_006534428.3.
DR AlphaFoldDB; B2RX12; -.
DR SMR; B2RX12; -.
DR STRING; 10090.ENSMUSP00000021231; -.
DR ChEMBL; CHEMBL2073683; -.
DR GlyGen; B2RX12; 2 sites.
DR iPTMnet; B2RX12; -.
DR PhosphoSitePlus; B2RX12; -.
DR SwissPalm; B2RX12; -.
DR jPOST; B2RX12; -.
DR MaxQB; B2RX12; -.
DR PaxDb; B2RX12; -.
DR PeptideAtlas; B2RX12; -.
DR PRIDE; B2RX12; -.
DR ProteomicsDB; 295655; -. [B2RX12-1]
DR ProteomicsDB; 295656; -. [B2RX12-2]
DR ProteomicsDB; 295657; -. [B2RX12-3]
DR ProteomicsDB; 373304; -.
DR Antibodypedia; 18128; 324 antibodies from 37 providers.
DR DNASU; 76408; -.
DR Ensembl; ENSMUST00000021231; ENSMUSP00000021231; ENSMUSG00000020865. [B2RX12-2]
DR Ensembl; ENSMUST00000178136; ENSMUSP00000136343; ENSMUSG00000020865. [B2RX12-1]
DR GeneID; 76408; -.
DR KEGG; mmu:76408; -.
DR UCSC; uc007kym.1; mouse. [B2RX12-2]
DR UCSC; uc011ycu.1; mouse. [B2RX12-3]
DR CTD; 8714; -.
DR MGI; MGI:1923658; Abcc3.
DR VEuPathDB; HostDB:ENSMUSG00000020865; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000161624; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; B2RX12; -.
DR OMA; MDLMTFL; -.
DR OrthoDB; 138195at2759; -.
DR TreeFam; TF105199; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 76408; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Abcc3; mouse.
DR PRO; PR:B2RX12; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; B2RX12; protein.
DR Bgee; ENSMUSG00000020865; Expressed in urinary bladder urothelium and 124 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; ISS:UniProtKB.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015164; F:glucuronoside transmembrane transporter activity; ISO:MGI.
DR GO; GO:0071714; F:icosanoid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0098656; P:anion transmembrane transport; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; ISO:MGI.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:MGI.
DR GO; GO:0042908; P:xenobiotic transport; 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1523
FT /note="ATP-binding cassette sub-family C member 3"
FT /id="PRO_0000356238"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 57..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 97..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 124..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 151..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 192..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 325..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 367..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 463..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 557..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 589..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 968..988
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 989..1013
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1034
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1035..1071
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1072..1092
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1093..1096
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1097..1117
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1118..1191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1192..1212
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1213..1219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1241..1523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 310..593
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 626..850
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 967..1248
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1287..1519
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 903..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 660..667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1319..1326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15438"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15438"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 803..827
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036011"
FT VAR_SEQ 862
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036012"
FT CONFLICT 81
FT /note="W -> R (in Ref. 2; AAQ10530/AAQ10531)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="D -> N (in Ref. 3; BAE33375)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="R -> G (in Ref. 1; AAX39010/AAX33774, 2; AAQ10530/
FT AAQ10531, 3; BAE33375 and 5; AAH48825/AAI50789)"
FT CONFLICT 742
FT /note="E -> G (in Ref. 3; BAE33375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1523 AA; 169223 MW; F25A63BDE6123AC1 CRC64;
MDRLCGSGEL GSKFWDSNLS IYTNTPDLTP CFQNSLLAWV PCIYLWAALP CYLFYLRHHQ
LGYIVLSWLS RLKTALGVLL WCVSWVDLFY SFHGLIHGSS PAPVFFVTPL VVGITMLLAT
LLIQYERLRG VQSSGVLIIF WLLCVICAII PFRSKILSAL AEGKILDPFR FTTFYIYFAL
VFCALILSCF KEKPPLFSPE NLDTNPCPEA SAGFFSRLSF WWFTRLAILG YRRPLEDRDL
WSLSEEDCSH KVVQRLLEAW QKQQNQASRS QTATAEPKIP GEDAVLLKPR PKSKQPSFLR
ALVRTFTSSL LMSACFNLIQ NLLGFVNPQL LSILIRFISD PTAPTWWGFL LAGLMFLSST
MQTLILHQYY HCIFVMALRL RTAIIGVIYR KALVITNSVK RESTVGEMVN LMSVDAQRFM
DVSPFINLLW SAPLQVILAI YFLWQILGPS ALAGVAVIVL LIPLNGAVSM KMKTYQVKQM
KFKDSRIKLM SEILNGIKVL KLYAWEPSFL EQVKGIRQSE LQLLRKGAYL QAISTFIWIC
TPFLVTLITL GVYVYVDESN VLDAEKAFVS LSLFNILKIP LNMLPQLISG LTQASVSLKR
IQDFLNQNEL DPQCVERKTI SPGYAITIHN GTFTWAQDLP PTLHSLNIQI PKGALVAVVG
PVGCGKSSLV SALLGEMEKL EGVVSVKGSV AYVPQQAWIQ NCTLQENVLF GQPMNPKRYQ
QALETCALLA DLDVLPGGDQ TEIGEKGINL SGGQRQRVSL ARAVYSDANI FLLDDPLSAV
DSHVAKHIFD QVIGPEGVLA GKTRVLVTHG ISFLPQTDFI IVLAGGQVSE MGHYSALLQH
DGSFANFLRN YAPDEDQEDH EAALQNANEE VLLLEDTLST HTDLTDNEPA IYEVRKQFMR
EMSSLSSEGE VQNRTMPKKH TNSLEKEALV TKTKETGALI KEEIAETGNV KLSVYWDYAK
SMGLCTTLSI CLLYGGQSAA AIGANVWLSA WSNDAEEHGQ QNKTSVRLGV YAALGILQGL
LVMLSAFTMV VGAIQAARLL HEALLHNKIR SPQSFFDTTP SGRILNRFSK DIYVIDEVLA
PTILMLLNSF FTSISTIMVI VASTPLFMVV VLPLAVLYGF VQRFYVATSR QLKRLESISR
SPIFSHFSET VTGTSVIRAY GRIQDFKVLS DTKVDNNQKS SYPYIASNRW LGVHVEFVGN
CVVLFAALFA VIGRNSLNPG LVGLSVSYAL QVTMALNWMI RMISDLESNI IAVERVKEYS
KTKTEAPWVV ESNRAPEGWP TRGMVEFRNY SVRYRPGLEL VLKNVTVHVQ GGEKVGIVGR
TGAGKSSMTL CLFRILEAAE GEIVIDGLNV AHIGLHDLRS QLTIIPQDPI LFSGTLRMNL
DPFGRYSEED IWRALELSHL NTFVSSQPAG LDFQCAEGGD NLSVGQRQLV CLARALLRKS
RVLVLDEATA AIDLETDDLI QGTIRTQFED CTVLTIAHRL NTIMDYNRVL VLDKGVVAEF
DSPVNLIAAG GIFYGMAKDA GLA
