ABCG2_RAT
ID ABCG2_RAT Reviewed; 657 AA.
AC Q80W57; Q80ST1; Q80UR3; Q80XF3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Broad substrate specificity ATP-binding cassette transporter ABCG2 {ECO:0000305};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q9UNQ0};
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=Bcrp1;
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].
RX PubMed=12819005; DOI=10.1016/s0002-9440(10)63624-3;
RA Shimano K., Satake M., Okaya A., Kitanaka J., Kitanaka N., Takemura M.,
RA Sakagami M., Terada N., Tsujimura T.;
RT "Hepatic oval cells have the side population phenotype defined by
RT expression of ATP-binding cassette transporter ABCG2/BCRP1.";
RL Am. J. Pathol. 163:3-9(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain capillary;
RX PubMed=15255930; DOI=10.1111/j.1471-4159.2004.02537.x;
RA Hori S., Ohtsuki S., Tachikawa M., Kimura N., Kondo T., Watanabe M.,
RA Nakashima E., Terasaki T.;
RT "Functional expression of rat ABCG2 on the luminal side of brain
RT capillaries and its enhancement by astrocyte-derived soluble factor(s).";
RL J. Neurochem. 90:526-536(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Yabuuchi H., Ishikawa T.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 506-657.
RC STRAIN=Sprague-Dawley; TISSUE=Brain endothelium;
RA Zhang W., Stanimirovic D.B.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18451542; DOI=10.1248/bpb.31.1032;
RA Ogura J., Kobayashi M., Itagaki S., Hirano T., Iseki K.;
RT "Post-transcriptional regulation of breast cancer resistance protein after
RT intestinal ischemia-reperfusion.";
RL Biol. Pharm. Bull. 31:1032-1035(2008).
RN [6]
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).
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 Involved in porphyrin homeostasis, mediating the export of
CC protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol
CC to extracellular space, it also functions in the cellular export of
CC heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a
CC urate exporter functioning in both renal and extrarenal urate excretion
CC (By similarity). In kidney, it also functions as a physiological
CC exporter of the uremic toxin indoxyl sulfate (By similarity). Also
CC involved in the excretion of steroids like estrone 3-sulfate/E1S,
CC 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates
CC (By similarity). Mediates the secretion of the riboflavin and biotin
CC vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin
CC catabolite of chlorophyll, reducing its bioavailability (By
CC similarity). Plays an important role in the exclusion of xenobiotics
CC from the brain. It confers to cells a resistance to multiple drugs and
CC other xenobiotics including mitoxantrone, pheophorbide, camptothecin,
CC methotrexate, azidothymidine, and the anthracyclines daunorubicin and
CC doxorubicin, through the control of their efflux (By similarity). In
CC placenta, it limits the penetration of drugs from the maternal plasma
CC into the fetus. May play a role in early stem cell self-renewal by
CC blocking differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q7TMS5, ECO:0000250|UniProtKB:Q9UNQ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q9UNQ0};
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:0000250|UniProtKB:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
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 -!- 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:0000250|UniProtKB:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
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:0000250|UniProtKB:Q7TMS5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC Evidence={ECO:0000250|UniProtKB:Q7TMS5};
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:0000269|PubMed:15255930};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:18451542}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UNQ0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain capillary, kidney and
CC small intestine. Lower expression in heart. Preferentially expressed
CC (at protein level) on the luminal membrane of brain capillaries, in
CC kidney and small intestine. {ECO:0000269|PubMed:15255930,
CC ECO:0000269|PubMed:18451542}.
CC -!- INDUCTION: Down-regulated upon ischemia-reperfusion.
CC {ECO:0000269|PubMed:18451542}.
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 in brain capillary, kidney and small intestine but
CC not in heart. {ECO:0000269|PubMed:15255930}.
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 -!- 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; AB094089; BAC75666.1; -; mRNA.
DR EMBL; AB105817; BAC76396.1; -; mRNA.
DR EMBL; AY089996; AAM09106.1; -; mRNA.
DR EMBL; AY089997; AAM09107.1; -; mRNA.
DR EMBL; AY089998; AAM09108.1; -; mRNA.
DR EMBL; AY274118; AAP23237.1; -; mRNA.
DR RefSeq; NP_852046.1; NM_181381.2.
DR RefSeq; XP_006236634.1; XM_006236572.3.
DR RefSeq; XP_006236635.1; XM_006236573.3.
DR RefSeq; XP_006236636.1; XM_006236574.3.
DR RefSeq; XP_006236638.1; XM_006236576.2.
DR RefSeq; XP_008761183.1; XM_008762961.2.
DR RefSeq; XP_017448109.1; XM_017592620.1.
DR AlphaFoldDB; Q80W57; -.
DR SMR; Q80W57; -.
DR STRING; 10116.ENSRNOP00000009546; -.
DR ChEMBL; CHEMBL3509585; -.
DR GlyGen; Q80W57; 2 sites.
DR iPTMnet; Q80W57; -.
DR PhosphoSitePlus; Q80W57; -.
DR PaxDb; Q80W57; -.
DR PRIDE; Q80W57; -.
DR Ensembl; ENSRNOT00000009546; ENSRNOP00000009546; ENSRNOG00000007041.
DR GeneID; 312382; -.
DR KEGG; rno:312382; -.
DR UCSC; RGD:631345; rat.
DR CTD; 9429; -.
DR RGD; 631345; Abcg2.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000160729; -.
DR InParanoid; Q80W57; -.
DR OMA; WCARMSS; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q80W57; -.
DR TreeFam; TF105211; -.
DR BRENDA; 7.6.2.3; 5301.
DR Reactome; R-RNO-189451; Heme biosynthesis.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:Q80W57; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007041; Expressed in duodenum and 18 other tissues.
DR Genevisible; Q80W57; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0098591; C:external side of apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:RGD.
DR GO; GO:0042887; F:amide transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0015878; P:biotin transport; ISS:UniProtKB.
DR GO; GO:1990748; P:cellular detoxification; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; IDA:RGD.
DR GO; GO:0140115; P:export across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0019389; P:glucuronoside metabolic process; IMP:RGD.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1904479; P:negative regulation of intestinal absorption; IMP:RGD.
DR GO; GO:0015711; P:organic anion transport; IDA:ARUK-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0097744; P:renal urate salt excretion; IEP:RGD.
DR GO; GO:1904612; P:response to 2,3,7,8-tetrachlorodibenzodioxine; IEP:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR GO; GO:0070633; P:transepithelial transport; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:RGD.
DR GO; GO:0046415; P:urate metabolic process; ISO:RGD.
DR GO; GO:0015747; P:urate transport; IMP:RGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:RGD.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; ISO:RGD.
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_0000093390"
FT TOPO_DOM 1..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
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 363..365
FT /note="AFR -> PFK (in Ref. 1; BAC75666)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="F -> L (in Ref. 1; BAC75666)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="I -> L (in Ref. 3; AAM09106/AAM09107/AAM09108)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="T -> L (in Ref. 1; BAC75666)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="M -> R (in Ref. 1; BAC75666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 72961 MW; C975C61A08489027 CRC64;
MSSSNDHVLV PMSQRNKNGL PGMSSRGART LAEGDVLSFH HITYRVKVKS GFLVRKTAEK
EILSDINGIM KPGLNAILGP TGGGKSSLLD VLAARKDPRG LSGDVLINGA PQPANFKCSS
GYVVQDDVVM GTLTVRENLQ FSAALRLPKA MKTHEKNERI NTIIKELGLD KVADSKVGTQ
FTRGISGGER KRTSIGMELI TDPSILFLDE PTTGLDSSTA NAVLLLLKRM SKQGRTIIFS
IHQPRYSIFK LFDSLTLLAS GKLMFHGPAQ KALEYFASAG YHCEPYNNPA DFFLDVINGD
SSAVMLNRGE QDHEANKTEE PSKREKPIIE NLAEFYINST IYGETKAELD QLPVAQKKKG
SSAFREPVYV TSFCHQLRWI ARRSFKNLLG NPQASVAQLI VTVILGLIIG ALYFGLKNDP
TGMQNRAGVF FFLTTNQCFT SVSAVELFVV EKKLFIHEYI SGYYRVSSYF FGKLVSDLLP
MRFLPSVIYT CILYFMLGLK RTVEAFFIMM FTLIMVAYTA SSMALAIAAG QSVVSVATLL
MTISFVFMML FSGLLVNLRT IGPWLSWLQY FSIPRYGFTA LQHNEFLGQE FCPGLNVTMN
STCVNSYTIC TGNDYLINQG IDLSPWGLWR NHVALACMII IFLTIAYLKL LFLKKYS
