ABCG2_MOUSE
ID ABCG2_MOUSE Reviewed; 657 AA.
AC Q7TMS5; Q9R004; Q9Z1T0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Broad substrate specificity ATP-binding cassette transporter ABCG2 {ECO:0000305};
DE EC=7.6.2.2 {ECO:0000269|PubMed:10485464, ECO:0000269|PubMed:12477054};
DE AltName: Full=ATP-binding cassette sub-family G member 2;
DE AltName: Full=Breast cancer resistance protein 1 homolog;
DE AltName: Full=Urate exporter;
DE AltName: CD_antigen=CD338;
GN Name=Abcg2; Synonyms=Abcp, Bcrp1;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=FVB/NJ; TISSUE=Liver;
RX PubMed=10485464;
RA Allen J.D., Brinkhuis R.F., Wijnholds J., Schinkel A.H.;
RT "The mouse Bcrp1/Mxr/Abcp gene: amplification and overexpression in cell
RT lines selected for resistance to topotecan, mitoxantrone, or doxorubicin.";
RL Cancer Res. 59:4237-4241(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 511-657.
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=9850061;
RA Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., Dean M.;
RT "A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome
RT 4q22 that is involved in multidrug resistance.";
RL Cancer Res. 58:5337-5339(1998).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11036110; DOI=10.1093/jnci/92.20.1651;
RA Jonker J.W., Smit J.W., Brinkhuis R.F., Maliepaard M., Beijnen J.H.,
RA Schellens J.H., Schinkel A.H.;
RT "Role of breast cancer resistance protein in the bioavailability and fetal
RT penetration of topotecan.";
RL J. Natl. Cancer Inst. 92:1651-1656(2000).
RN [5]
RP FUNCTION.
RX PubMed=11533706; DOI=10.1038/nm0901-1028;
RA Zhou S., Schuetz J.D., Bunting K.D., Colapietro A.M., Sampath J.,
RA Morris J.J., Lagutina I., Grosveld G.C., Osawa M., Nakauchi H.,
RA Sorrentino B.P.;
RT "The ABC transporter Bcrp1/ABCG2 is expressed in a wide variety of stem
RT cells and is a molecular determinant of the side-population phenotype.";
RL Nat. Med. 7:1028-1034(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12477054;
RA Allen J.D., van Loevezijn A., Lakhai J.M., van der Valk M.,
RA van Tellingen O., Reid G., Schellens J.H., Koomen G.J., Schinkel A.H.;
RT "Potent and specific inhibition of the breast cancer resistance protein
RT multidrug transporter in vitro and in mouse intestine by a novel analogue
RT of fumitremorgin C.";
RL Mol. Cancer Ther. 1:417-425(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12429862; DOI=10.1073/pnas.202607599;
RA Jonker J.W., Buitelaar M., Wagenaar E., Van Der Valk M.A., Scheffer G.L.,
RA Scheper R.J., Plosch T., Kuipers F., Elferink R.P., Rosing H.,
RA Beijnen J.H., Schinkel A.H.;
RT "The breast cancer resistance protein protects against a major chlorophyll-
RT derived dietary phototoxin and protoporphyria.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15649-15654(2002).
RN [8]
RP FUNCTION, AND INDUCTION BY HYPOXIA.
RX PubMed=15044468; DOI=10.1074/jbc.m313599200;
RA Krishnamurthy P., Ross D.D., Nakanishi T., Bailey-Dell K., Zhou S.,
RA Mercer K.E., Sarkadi B., Sorrentino B.P., Schuetz J.D.;
RT "The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through
RT interactions with heme.";
RL J. Biol. Chem. 279:24218-24225(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17145775; DOI=10.1128/mcb.01621-06;
RA van Herwaarden A.E., Wagenaar E., Merino G., Jonker J.W., Rosing H.,
RA Beijnen J.H., Schinkel A.H.;
RT "Multidrug transporter ABCG2/breast cancer resistance protein secretes
RT riboflavin (vitamin B2) into milk.";
RL Mol. Cell. Biol. 27:1247-1253(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30042379; DOI=10.1038/s41598-018-29208-w;
RA Takada T., Yamamoto T., Matsuo H., Tan J.K., Ooyama K., Sakiyama M.,
RA Miyata H., Yamanashi Y., Toyoda Y., Higashino T., Nakayama A.,
RA Nakashima A., Shinomiya N., Ichida K., Ooyama H., Fujimori S., Suzuki H.;
RT "Identification of ABCG2 as an exporter of uremic toxin indoxyl sulfate in
RT mice and as a crucial factor influencing CKD progression.";
RL Sci. Rep. 8:11147-11147(2018).
CC -!- FUNCTION: Broad substrate specificity ATP-dependent transporter of the
CC ATP-binding cassette (ABC) family that actively extrudes a wide variety
CC of physiological compounds, dietary toxins and xenobiotics from cells
CC (PubMed:10485464, PubMed:12477054, PubMed:12429862, PubMed:17145775,
CC PubMed:30042379). Involved in porphyrin homeostasis, mediating the
CC export of protoporphyrin IX (PPIX) from both mitochondria to cytosol
CC and cytosol to extracellular space, it also functions in the cellular
CC export of heme (PubMed:12429862, PubMed:15044468). Also mediates the
CC efflux of sphingosine-1-P from cells (By similarity). Acts as a urate
CC exporter functioning in both renal and extrarenal urate excretion (By
CC similarity). In kidney, it also functions as a physiological exporter
CC of the uremic toxin indoxyl sulfate (PubMed:30042379). Also involved in
CC the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-
CC androst-5-en-17-one/DHEAS, and other sulfate conjugates (By
CC similarity). Mediates the secretion of the riboflavin and biotin
CC vitamins into milk (PubMed:17145775). Extrudes pheophorbide a, a
CC phototoxic porphyrin catabolite of chlorophyll, reducing its
CC bioavailability (PubMed:12429862). Plays an important role in the
CC exclusion of xenobiotics from the brain (PubMed:10485464). It confers
CC to cells a resistance to multiple drugs and other xenobiotics including
CC mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine,
CC and the anthracyclines daunorubicin and doxorubicin, through the
CC control of their efflux (PubMed:12477054). In placenta, it limits the
CC penetration of drugs from the maternal plasma into the fetus
CC (PubMed:12429862). May play a role in early stem cell self-renewal by
CC blocking differentiation (Probable). {ECO:0000250|UniProtKB:Q9UNQ0,
CC ECO:0000269|PubMed:10485464, ECO:0000269|PubMed:12429862,
CC ECO:0000269|PubMed:12477054, ECO:0000269|PubMed:15044468,
CC ECO:0000269|PubMed:17145775, ECO:0000269|PubMed:30042379,
CC ECO:0000305|PubMed:11533706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:10485464,
CC ECO:0000269|PubMed:12477054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate +
CC riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57986, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17145775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353;
CC Evidence={ECO:0000269|PubMed:17145775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide
CC a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58687, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:17145775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000269|PubMed:17145775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out);
CC Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl
CC sulfate(out) + phosphate; Xref=Rhea:RHEA:61332, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:144643, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30042379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333;
CC Evidence={ECO:0000269|PubMed:30042379};
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:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3-
CC sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
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:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4-
CC methylumbelliferone sulfate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:61368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144581,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-
CC benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl-
CC 2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D-
CC glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61384,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:144584, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-
CC methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:61372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144582,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3-
CC benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2-
CC methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:61376, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:144583, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
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:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out)
CC + phosphate; Xref=Rhea:RHEA:61356, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50681, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
CC -!- ACTIVITY REGULATION: Specifically inhibited by the fungal toxin
CC fumitremorgin C and Ko143. {ECO:0000269|PubMed:12477054}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.3 mM for indoxyl sulfate {ECO:0000269|PubMed:30042379};
CC Vmax=5.27 nmol/min/mg enzyme for indoxyl sulfate transport
CC {ECO:0000269|PubMed:30042379};
CC -!- SUBUNIT: Homodimer; disulfide-linked. The minimal functional unit is a
CC homodimer, but the major oligomeric form in plasma membrane is a
CC homotetramer with possibility of higher order oligomerization up to
CC homododecamers. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UNQ0};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:12429862}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UNQ0};
CC Multi-pass membrane protein {ECO:0000255}. Note=Enriched in membrane
CC lipid rafts. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Lower expression in
CC liver, colon, heart, spleen, and placenta (PubMed:11036110). Expressed
CC in mammary gland (PubMed:17145775). Expressed in intestinal villi and
CC renal proximal tubules, hepatic bile canalicular membranes, and
CC placental labyrinth cells (at protein level) (PubMed:12429862).
CC {ECO:0000269|PubMed:11036110, ECO:0000269|PubMed:12429862,
CC ECO:0000269|PubMed:17145775}.
CC -!- INDUCTION: Up-regulated upon hypoxia. {ECO:0000269|PubMed:15044468}.
CC -!- DOMAIN: The extracellular loop 3 (ECL3) is involved in binding
CC porphyrins and transfer them to other carriers, probably albumin.
CC {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- PTM: N-glycosylated. Glycosylation-deficient ABCG2 is normally
CC expressed and functional. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- PTM: Phosphorylated. Phosphorylation may regulate the localization to
CC the plasma membrane, the homooligomerization and therefore, the
CC activity of the transporter. {ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Abcg2 are born at the expected
CC Mendelian ratio and do not display overt phenotype (PubMed:12429862).
CC However, under specific housing conditions, they show phototoxic skin
CC lesions induced by pheophorbide a, a porphyrin catabolite of
CC chlorophyll found in their diet, that accumulates in mice plasma
CC (PubMed:12429862). They also accumulate a red substance in their bile
CC and display protoporphyria with an accumulation of protoporphyrin IX
CC (PPIX) in erythrocytes (PubMed:12429862). Mice lacking Abcg2 present
CC decreased elimination of some uremic toxins like indoxyl sulfate
CC leading to their accumulation in plasma (PubMed:30042379). They also
CC show reduced survival rate upon adenine-induced chronic kidney disease
CC (PubMed:30042379). {ECO:0000269|PubMed:12429862,
CC ECO:0000269|PubMed:30042379}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; AF140218; AAD54216.1; -; mRNA.
DR EMBL; BC053730; AAH53730.1; -; mRNA.
DR EMBL; AF103875; AAD09189.1; -; mRNA.
DR CCDS; CCDS20195.1; -.
DR RefSeq; NP_036050.1; NM_011920.3.
DR RefSeq; XP_006506211.1; XM_006506148.3.
DR RefSeq; XP_006506212.1; XM_006506149.3.
DR RefSeq; XP_006506213.1; XM_006506150.3.
DR RefSeq; XP_006506214.1; XM_006506151.3.
DR RefSeq; XP_011239664.1; XM_011241362.1.
DR AlphaFoldDB; Q7TMS5; -.
DR SMR; Q7TMS5; -.
DR CORUM; Q7TMS5; -.
DR IntAct; Q7TMS5; 1.
DR STRING; 10090.ENSMUSP00000031822; -.
DR ChEMBL; CHEMBL2073705; -.
DR GlyGen; Q7TMS5; 2 sites.
DR iPTMnet; Q7TMS5; -.
DR PhosphoSitePlus; Q7TMS5; -.
DR SwissPalm; Q7TMS5; -.
DR EPD; Q7TMS5; -.
DR jPOST; Q7TMS5; -.
DR MaxQB; Q7TMS5; -.
DR PaxDb; Q7TMS5; -.
DR PeptideAtlas; Q7TMS5; -.
DR PRIDE; Q7TMS5; -.
DR ProteomicsDB; 285819; -.
DR DNASU; 26357; -.
DR GeneID; 26357; -.
DR KEGG; mmu:26357; -.
DR CTD; 9429; -.
DR MGI; MGI:1347061; Abcg2.
DR eggNOG; KOG0061; Eukaryota.
DR InParanoid; Q7TMS5; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q7TMS5; -.
DR TreeFam; TF105211; -.
DR BRENDA; 7.6.2.3; 3474.
DR Reactome; R-MMU-189451; Heme biosynthesis.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 26357; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Abcg2; mouse.
DR PRO; PR:Q7TMS5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TMS5; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0098591; C:external side of apical plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO: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:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015878; P:biotin transport; IMP:UniProtKB.
DR GO; GO:1990748; P:cellular detoxification; ISO:MGI.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; ISO:MGI.
DR GO; GO:0140115; P:export across plasma membrane; ISO:MGI.
DR GO; GO:0019389; P:glucuronoside metabolic process; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1904479; P:negative regulation of intestinal absorption; ISO:MGI.
DR GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0097744; P:renal urate salt excretion; ISS:UniProtKB.
DR GO; GO:0032218; P:riboflavin transport; IMP:UniProtKB.
DR GO; GO:0070633; P:transepithelial transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046415; P:urate metabolic process; ISO:MGI.
DR GO; GO:0015747; P:urate transport; ISO:MGI.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; ISO:MGI.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR030256; ABCG2.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48041:SF92; PTHR48041:SF92; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Lipid transport;
KW Membrane; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..657
FT /note="Broad substrate specificity ATP-binding cassette
FT transporter ABCG2"
FT /id="PRO_0000093388"
FT TOPO_DOM 1..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..632
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..285
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 389..653
FT /note="ABC transmembrane type-2"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 183..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT BINDING 242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 592..610
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT DISULFID 603
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9UNQ0"
FT CONFLICT 23
FT /note="T -> M (in Ref. 1; AAD54216)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="V -> I (in Ref. 1; AAD54216)"
FT /evidence="ECO:0000305"
FT CONFLICT 512..516
FT /note="TLIMV -> GLGAE (in Ref. 3; AAD09189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 72978 MW; DCD70C5D9FA2BA5F CRC64;
MSSSNDHVLV PMSQRNNNGL PRTNSRAVRT LAEGDVLSFH HITYRVKVKS GFLVRKTVEK
EILSDINGIM KPGLNAILGP TGGGKSSLLD VLAARKDPKG LSGDVLINGA PQPAHFKCCS
GYVVQDDVVM GTLTVRENLQ FSAALRLPTT MKNHEKNERI NTIIKELGLE KVADSKVGTQ
FIRGISGGER KRTSIGMELI TDPSILFLDE PTTGLDSSTA NAVLLLLKRM SKQGRTIIFS
IHQPRYSIFK LFDSLTLLAS GKLVFHGPAQ KALEYFASAG YHCEPYNNPA DFFLDVINGD
SSAVMLNREE QDNEANKTEE PSKGEKPVIE NLSEFYINSA IYGETKAELD QLPGAQEKKG
TSAFKEPVYV TSFCHQLRWI ARRSFKNLLG NPQASVAQLI VTVILGLIIG AIYFDLKYDA
AGMQNRAGVL FFLTTNQCFS SVSAVELFVV EKKLFIHEYI SGYYRVSSYF FGKVMSDLLP
MRFLPSVIFT CVLYFMLGLK KTVDAFFIMM FTLIMVAYTA SSMALAIATG QSVVSVATLL
MTIAFVFMML FSGLLVNLRT IGPWLSWLQY FSIPRYGFTA LQYNEFLGQE FCPGFNVTDN
STCVNSYAIC TGNEYLINQG IELSPWGLWK NHVALACMII IFLTIAYLKL LFLKKYS
