ID   G3SL88_LOXAF            Unreviewed;       659 AA.
AC   G3SL88;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   02-SEP-2026, entry version 84.
DE   RecName: Full=Broad substrate specificity ATP-binding cassette transporter ABCG2 {ECO:0000256|ARBA:ARBA00019542};
DE            EC=7.6.2.2 {ECO:0000256|ARBA:ARBA00012191};
DE   AltName: Full=ATP-binding cassette sub-family G member 2 {ECO:0000256|ARBA:ARBA00031839};
DE   AltName: Full=Urate exporter {ECO:0000256|ARBA:ARBA00031848};
GN   Name=ABCG2 {ECO:0000313|Ensembl:ENSLAFP00000000153.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000153.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000000153.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000153.2};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000000153.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000153.2};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
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 + phosphate +
CC         H(+); Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00047576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC         Evidence={ECO:0000256|ARBA:ARBA00047576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4-
CC         methylumbelliferone beta-D-glucuronate(out) + ADP + phosphate + H(+);
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:0000256|ARBA:ARBA00047877};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373;
CC         Evidence={ECO:0000256|ARBA:ARBA00047877};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4-
CC         methylumbelliferone sulfate(out) + ADP + phosphate + H(+);
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:0000256|ARBA:ARBA00049018};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369;
CC         Evidence={ECO:0000256|ARBA:ARBA00049018};
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 + phosphate + H(+); 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:0000256|ARBA:ARBA00049490};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385;
CC         Evidence={ECO:0000256|ARBA:ARBA00049490};
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 + phosphate + H(+); 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:0000256|ARBA:ARBA00047542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377;
CC         Evidence={ECO:0000256|ARBA:ARBA00047542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00034018};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dehydroepiandrosterone 3-sulfate(in) + ATP + H2O =
CC         dehydroepiandrosterone 3-sulfate(out) + ADP + phosphate + H(+);
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:0000256|ARBA:ARBA00047279};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC         Evidence={ECO:0000256|ARBA:ARBA00047279};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(in) + ATP + H2O = estrone 3-sulfate(out) +
CC         ADP + phosphate + H(+); Xref=Rhea:RHEA:61348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60050, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00047516};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349;
CC         Evidence={ECO:0000256|ARBA:ARBA00047516};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=indoxyl sulfate(in) + ATP + H2O = indoxyl sulfate(out) + ADP +
CC         phosphate + H(+); 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:0000256|ARBA:ARBA00049205};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333;
CC         Evidence={ECO:0000256|ARBA:ARBA00049205};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=itaconate(in) + ATP + H2O = itaconate(out) + ADP + phosphate +
CC         H(+); Xref=Rhea:RHEA:82291, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17240, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00052001};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82292;
CC         Evidence={ECO:0000256|ARBA:ARBA00052001};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lumichrome(in) + ATP + H2O = lumichrome(out) + ADP + phosphate
CC         + H(+); Xref=Rhea:RHEA:86403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17781, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00094047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86404;
CC         Evidence={ECO:0000256|ARBA:ARBA00094047};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=methotrexate(in) + ATP + H2O = methotrexate(out) + ADP +
CC         phosphate + H(+); 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:0000256|ARBA:ARBA00048296};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357;
CC         Evidence={ECO:0000256|ARBA:ARBA00048296};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pheophorbide a(in) + ATP + H2O = pheophorbide a(out) + ADP +
CC         phosphate + H(+); 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:0000256|ARBA:ARBA00048455};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361;
CC         Evidence={ECO:0000256|ARBA:ARBA00048455};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=riboflavin(in) + ATP + H2O = riboflavin(out) + ADP + phosphate
CC         + H(+); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57986,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00048280};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353;
CC         Evidence={ECO:0000256|ARBA:ARBA00048280};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphing-4-enine 1-phosphate(in) + ATP + H2O = sphing-4-enine 1-
CC         phosphate(out) + ADP + phosphate + H(+); 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:0000256|ARBA:ARBA00047354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC         Evidence={ECO:0000256|ARBA:ARBA00047354};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urate(in) + ATP + H2O = urate(out) + ADP + phosphate + H(+);
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:0000256|ARBA:ARBA00048665};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462;
CC         Evidence={ECO:0000256|ARBA:ARBA00048665};
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:0000256|ARBA:ARBA00046614}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Mitochondrion membrane
CC       {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004225}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC       {ECO:0000256|ARBA:ARBA00005814}.
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DR   RefSeq; XP_003414134.1; XM_003414086.4.
DR   RefSeq; XP_023409032.1; XM_023553264.2.
DR   RefSeq; XP_023409033.1; XM_023553265.2.
DR   RefSeq; XP_023409034.1; XM_023553266.2.
DR   AlphaFoldDB; G3SL88; -.
DR   FunCoup; G3SL88; 17.
DR   STRING; 9785.ENSLAFP00000000153; -.
DR   Ensembl; ENSLAFT00000000189.2; ENSLAFP00000000153.2; ENSLAFG00000000187.2.
DR   GeneID; 100669676; -.
DR   KEGG; lav:100669676; -.
DR   CTD; 9429; -.
DR   eggNOG; KOG0061; Eukaryota.
DR   GeneTree; ENSGT00940000160729; -.
DR   HOGENOM; CLU_000604_57_8_1; -.
DR   InParanoid; G3SL88; -.
DR   OMA; MCVNGFM; -.
DR   OrthoDB; 66620at2759; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:TreeGrafter.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IEA:TreeGrafter.
DR   GO; GO:0098754; P:detoxification; IEA:UniProtKB-ARBA.
DR   GO; GO:0097744; P:renal urate salt excretion; IEA:UniProtKB-ARBA.
DR   CDD; cd03213; ABCG_EPDR; 1.
DR   FunFam; 3.40.50.300:FF:000622; ATP-binding cassette sub-family G member 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR050352; ABCG_transporters.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF92; BROAD SUBSTRATE SPECIFICITY ATP-BINDING CASSETTE TRANSPORTER ABCG2; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00434}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00434}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        506..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        537..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        635..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..286
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   BINDING         80..87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   659 AA;  73178 MW;  32FCE58A3C7D83F7 CRC64;
     MSSDNIQVFI PMSENTNGLP GTMTSNDLKP CTEGAVLSFH NICYRVKVKS GFILCRKTAE
     KEILKDINGI MRPGLNAILG PTGGGKSSLL DVLAERKDPH GLSGDVLING APRPANFKCN
     SGYVVQDDVV MGTLTVRENL QFSAALRLPT TMKNHEKNER VNMIIQELGL EKVADSKVGT
     QFIRGVSGGE RKRTSIGMEL ITDPSILFLD EPTTGLDAST ANAVLLLLKR MSKRGRTIIF
     SIHQPRYSIF KLFDSLTLLA SGRLIFHGPA QEALGYFASA GYNCEPYNNP ADFFLDIING
     DSSAVVLNRE EEDRKARGAK ELSQNDQTII EKLAEFYANS TFSRETKTEL DGLSGVQKKK
     KSTAFKEITY TTSFCHQLRW VTKRSFKNLL GNPQASIAQL IVTAVLGLII GAIFYGLQND
     QTGIQNRAGV LFFLTTNQCF SSVSAVELFV IEKKLFIHEY ISGYYRVSSY FFGKLLSDLL
     PMRMLPSIIF TCIIYFLLGL KPTAEAFFIM MFSLMMVAYT ASSMGLAVAA GQSVVSIATL
     LMTICFVFMM LFSGLLVNLK TIVPWLSWLQ YFSIPRYGYT ALLHNEFSGQ HFCPDLNVTT
     NNTCDYEAYA VCTGEEFLTS QGIDLSPWGL WKNHLALACM IVIFLTIAYL KLLFLKKYS
//