ID ABCG8_MOUSE Reviewed; 673 AA. AC Q9DBM0; Q8R543; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 185. DE RecName: Full=ATP-binding cassette sub-family G member 8 {ECO:0000305}; DE EC=7.6.2.- {ECO:0000269|PubMed:16867993}; DE AltName: Full=Sterolin-2 {ECO:0000303|PubMed:11452359, ECO:0000303|PubMed:11907139}; GN Name=Abcg8 {ECO:0000312|MGI:MGI:1914720}; 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] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=11452359; DOI=10.1086/321294; RA Lu K., Lee M.-H., Hazard S., Brooks-Wilson A., Hidaka H., Kojima H., RA Ose L., Stalenhoef A.F.H., Mietinnen T., Bjorkhem I., Bruckert E., RA Pandya A., Brewer H.B. Jr., Salen G., Dean M., Srivastava A.K., Patel S.B.; RT "Two genes that map to the STSL locus cause sitosterolemia: genomic RT structure and spectrum of mutations involving sterolin-1 and sterolin-2, RT encoded by ABCG5 and ABCG8, respectively."; RL Am. J. Hum. Genet. 69:278-290(2001). RN [2] {ECO:0000312|EMBL:AAL82898.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, RP AND TISSUE SPECIFICITY. RC STRAIN=129/Sv {ECO:0000312|EMBL:AAL82898.1}; RX PubMed=11907139; DOI=10.1016/s0022-2275(20)31486-3; RA Lu K., Lee M.H., Yu H., Zhou Y., Sandell S.A., Salen G., Patel S.B.; RT "Molecular cloning, genomic organization, genetic variations, and RT characterization of murine sterolin genes Abcg5 and Abcg8."; RL J. Lipid Res. 43:565-578(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11099417; DOI=10.1126/science.290.5497.1771; RA Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J., RA Kwiterovich P., Shan B., Barnes R., Hobbs H.H.; RT "Accumulation of dietary cholesterol in sitosterolemia caused by mutations RT in adjacent ABC transporters."; RL Science 290:1771-1775(2000). RN [5] RP SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=12208867; DOI=10.1172/jci16000; RA Graf G.A., Li W.P., Gerard R.D., Gelissen I., White A., Cohen J.C., RA Hobbs H.H.; RT "Coexpression of ATP-binding cassette proteins ABCG5 and ABCG8 permits RT their transport to the apical surface."; RL J. Clin. Invest. 110:659-669(2002). RN [6] RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND GLYCOSYLATION. RX PubMed=12444248; DOI=10.1073/pnas.252582399; RA Yu L., Hammer R.E., Li-Hawkins J., Von Bergmann K., Lutjohann D., RA Cohen J.C., Hobbs H.H.; RT "Disruption of Abcg5 and Abcg8 in mice reveals their crucial role in RT biliary cholesterol secretion."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16237-16242(2002). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=14504269; DOI=10.1074/jbc.m310223200; RA Graf G.A., Yu L., Li W.P., Gerard R., Tuma P.L., Cohen J.C., Hobbs H.H.; RT "ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and RT biliary cholesterol excretion."; RL J. Biol. Chem. 278:48275-48282(2003). RN [8] RP DOWN-REGULATION BY ENDOTOXIN. RX PubMed=12777468; DOI=10.1194/jlr.m300100-jlr200; RA Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.; RT "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and RT ABCG1 in J774 murine macrophages: differential role of LXR."; RL J. Lipid Res. 44:1728-1736(2003). RN [9] RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=15040800; DOI=10.1186/1741-7015-2-5; RA Klett E.L., Lu K., Kosters A., Vink E., Lee M.H., Altenburg M., Shefer S., RA Batta A.K., Yu H., Chen J., Klein R., Looije N., Oude-Elferink R., RA Groen A.K., Maeda N., Salen G., Patel S.B.; RT "A mouse model of sitosterolemia: absence of Abcg8/sterolin-2 results in RT failure to secrete biliary cholesterol."; RL BMC Med. 2:5-5(2004). RN [10] RP SUBUNIT, GLYCOSYLATION AT ASN-619, AND MUTAGENESIS OF ASN-619. RX PubMed=15054092; DOI=10.1074/jbc.m402634200; RA Graf G.A., Cohen J.C., Hobbs H.H.; RT "Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and RT trafficking."; RL J. Biol. Chem. 279:24881-24888(2004). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=14657202; DOI=10.1194/jlr.m300377-jlr200; RA Yu L., von Bergmann K., Lutjohann D., Hobbs H.H., Cohen J.C.; RT "Selective sterol accumulation in ABCG5/ABCG8-deficient mice."; RL J. Lipid Res. 45:301-307(2004). RN [12] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-112; VAL-214; RP GLY-216; GLY-217 AND GLU-239, AND DOMAIN. RX PubMed=16352607; DOI=10.1074/jbc.m512277200; RA Zhang D.W., Graf G.A., Gerard R.D., Cohen J.C., Hobbs H.H.; RT "Functional asymmetry of nucleotide-binding domains in ABCG5 and ABCG8."; RL J. Biol. Chem. 281:4507-4516(2006). RN [13] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF RP ARG-112 AND GLY-217, ACTIVITY REGULATION, COFACTOR, AND CATALYTIC ACTIVITY. RX PubMed=16867993; DOI=10.1074/jbc.m605603200; RA Wang J., Sun F., Zhang D.W., Ma Y., Xu F., Belani J.D., Cohen J.C., RA Hobbs H.H., Xie X.S.; RT "Sterol transfer by ABCG5 and ABCG8: in vitro assay and reconstitution."; RL J. Biol. Chem. 281:27894-27904(2006). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION, RP AND MUTAGENESIS OF 664-LEU--TRP-673. RX PubMed=18402465; DOI=10.1021/bi800292v; RA Wang J., Zhang D.W., Lei Y., Xu F., Cohen J.C., Hobbs H.H., Xie X.S.; RT "Purification and reconstitution of sterol transfer by native mouse ABCG5 RT and ABCG8."; RL Biochemistry 47:5194-5204(2008). RN [15] RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=25378657; DOI=10.1194/jlr.m054544; RA Wang J., Mitsche M.A., Luetjohann D., Cohen J.C., Xie X.S., Hobbs H.H.; RT "Relative roles of ABCG5/ABCG8 in liver and intestine."; RL J. Lipid Res. 56:319-330(2015). CC -!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates CC Mg(2+)- and ATP-dependent sterol transport across the cell membrane CC (PubMed:16352607, PubMed:16867993, PubMed:18402465). Plays an essential CC role in the selective transport of the dietary cholesterol in and out CC of the enterocytes and in the selective sterol excretion by the liver CC into bile (PubMed:12444248, PubMed:14504269, PubMed:14657202, CC PubMed:25378657). Plays an important role in preventing the CC accumulation of dietary plant sterols in the body (PubMed:12444248, CC PubMed:14657202). Required for normal sterol homeostasis CC (PubMed:12444248, PubMed:14657202). The heterodimer with ABCG5 has CC ATPase activity (PubMed:16352607, PubMed:16867993). CC {ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14504269, CC ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:16352607, CC ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465, CC ECO:0000269|PubMed:25378657}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol(in) + ATP + H2O = cholesterol(out) + ADP + CC phosphate + H(+); Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:16867993}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; CC Evidence={ECO:0000269|PubMed:16867993}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sitosterol(in) + ATP + H2O = sitosterol(out) + ADP + phosphate CC + H(+); Xref=Rhea:RHEA:39103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:27693, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16867993}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39104; CC Evidence={ECO:0000269|PubMed:16867993}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16867993}; CC -!- ACTIVITY REGULATION: Cholesterol transport is inhibited by vanadate and CC by beryllium fluoride. {ECO:0000269|PubMed:16867993}. CC -!- SUBUNIT: Heterodimer with ABCG5. {ECO:0000269|PubMed:12208867, CC ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15054092, CC ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993, CC ECO:0000269|PubMed:18402465}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12208867, CC ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass CC membrane protein {ECO:0000305}. Apical cell membrane CC {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, CC ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9DBM0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DBM0-2; Sequence=VSP_000053; CC -!- TISSUE SPECIFICITY: Detected in liver and jejunum (at protein level) CC (PubMed:12444248, PubMed:18402465, PubMed:25378657). Expressed in CC jejunum and ileum and, at lower level, in the liver (PubMed:11099417, CC PubMed:11907139, PubMed:12444248, PubMed:15040800, PubMed:25378657). CC {ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11907139, CC ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800, CC ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}. CC -!- INDUCTION: Up-regulated in liver and small intestine by cholesterol CC feeding (PubMed:11099417). Possibly mediated by the liver X CC receptor/retinoic X receptor (LXR/RXR) pathway. Endotoxin (LPS) CC significantly decreased mRNA levels in the liver but not in the small CC intestine (PubMed:12777468). {ECO:0000269|PubMed:11099417, CC ECO:0000269|PubMed:12777468}. CC -!- DOMAIN: A functional Walker motif (consensus sequence G-X-X-G-X-G-K- CC [ST]-T) is expected to bind ATP. The essential Lys in this region is CC not conserved in ABCG8 (G-S-S-G-C-R-A-S) and is not required for CC transport activity mediated by the heterodimer with ABCG5. CC {ECO:0000269|PubMed:16352607}. CC -!- PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:15054092, CC PubMed:16867993, PubMed:18402465). N-glycosylation is important for CC efficient export out of the endoplasmic reticulum (PubMed:15054092). CC {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:12444248, CC ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993, CC ECO:0000269|PubMed:18402465}. CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate. CC They display decreased cholesterol levels, but strongly increased CC levels of the food-derived plant sterols campesterol and beta- CC sitosterol in blood plasma, liver and spleen (PubMed:25378657). CC Besides, mutant mice may have slightly increased total plasma CC triglyceride levels. Expression of Abcg5 is not affected. Mutant mice CC display decreased biliary sterol secretion (PubMed:15040800). Mice CC deficient for both Abcg5 and Abcg8 appear healthy and are fertile, but CC display strongly increased levels of the food-derived plant sterols CC sitosterol and campesterol in liver and blood plasma (PubMed:12444248, CC PubMed:14657202, PubMed:25378657). When mice are fed chow containing CC 0.02% cholesterol, cholesterol levels in blood plasma and in liver are CC considerably lower than in wild-type (PubMed:12444248, CC PubMed:14657202). In spite of the increased plasma and liver levels of CC plant sterols, and the decreased cholesterol levels, the total sterol CC levels in plasma and liver are closely similar in wild-type and mutant CC mice (PubMed:14657202). When mice are fed chow containing 2% CC cholesterol, plasma cholesterol levels remain stable in wild-type, but CC increase 2.4-fold in mutant mice. In the liver of mice kept on chow CC containing 2% cholesterol, cholesterol levels increase 3-fold for wild- CC type mice and 18-fold for mutant mice, resulting in much higher CC cholesterol levels than in wild-type livers (PubMed:12444248). Dietary CC cholesterol absorption appears normal in mutant mice, but the CC absorption of dietary cholestanol, campesterol and sitosterol is CC increased (PubMed:12444248). At the same time, mutant mice have very CC low cholesterol levels in bile, suggesting that the increased hepatic CC cholesterol levels are due to impaired cholesterol secretion into bile CC (PubMed:12444248). Likewise, the levels of the food-derived plant CC sterols stigmasterol, sitosterol, campesterol and brassicasterol are CC strongly decreased in bile from mutant mice (PubMed:14657202). In CC contrast, biliary phospholipid and bile acid levels appear unchanged CC relative to wild-type (PubMed:12444248). The blood plasma of mice with CC liver-specific or intestine-specific disruption of Abcg5 and Abcg8 has CC nearly normal levels of cholesterol, and mildly increased levels of CC sitosterol and campesterol (PubMed:25378657). Mice with intestine- CC specific disruption of Abcg5 and Abcg8 have strongly increased levels CC of sitosterol and campesterol in enterocytes, similar to that observed CC for mice with complete gene disruption (PubMed:25378657). In addition, CC they display strongly increased levels of sitosterol and campesterol in CC bile (PubMed:25378657). Mice with liver-specific disruption of Abcg5 CC and Abcg8 have slightly increased levels of campesterol and sitosterol CC in the liver, and normal, low levels of sitosterol and campesterol in CC bile (PubMed:25378657). Enterocytes and liver from mice with liver- CC specific or intestine-specific disruption of Abcg5 and Abcg8 have CC normal cholesterol levels (PubMed:25378657). CC {ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14657202, CC ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:25378657}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}. CC -!- CAUTION: Seems to have a defective ATP-binding region. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AH011518; AAL82898.1; -; Genomic_DNA. DR EMBL; AF351799; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351800; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351801; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351802; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351803; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351804; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351807; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351808; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351809; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF351810; AAL82898.1; JOINED; Genomic_DNA. DR EMBL; AF324495; AAK84079.1; -; mRNA. DR EMBL; AK004871; BAB23630.1; -; mRNA. DR CCDS; CCDS29002.1; -. [Q9DBM0-1] DR RefSeq; NP_001272934.1; NM_001286005.1. DR RefSeq; NP_001334347.1; NM_001347418.1. DR RefSeq; NP_080456.1; NM_026180.3. [Q9DBM0-1] DR AlphaFoldDB; Q9DBM0; -. DR SMR; Q9DBM0; -. DR CORUM; Q9DBM0; -. DR FunCoup; Q9DBM0; 90. DR STRING; 10090.ENSMUSP00000035246; -. DR GlyCosmos; Q9DBM0; 1 site, No reported glycans. DR GlyGen; Q9DBM0; 1 site. DR iPTMnet; Q9DBM0; -. DR PhosphoSitePlus; Q9DBM0; -. DR SwissPalm; Q9DBM0; -. DR jPOST; Q9DBM0; -. DR PaxDb; 10090-ENSMUSP00000035246; -. DR ProteomicsDB; 285821; -. [Q9DBM0-1] DR ProteomicsDB; 285822; -. [Q9DBM0-2] DR Antibodypedia; 14910; 312 antibodies from 27 providers. DR DNASU; 67470; -. DR Ensembl; ENSMUST00000045714.15; ENSMUSP00000035246.9; ENSMUSG00000024254.16. [Q9DBM0-1] DR GeneID; 67470; -. DR KEGG; mmu:67470; -. DR UCSC; uc008dta.2; mouse. [Q9DBM0-1] DR AGR; MGI:1914720; -. DR CTD; 64241; -. DR MGI; MGI:1914720; Abcg8. DR VEuPathDB; HostDB:ENSMUSG00000024254; -. DR eggNOG; KOG0061; Eukaryota. DR GeneTree; ENSGT00940000159739; -. DR InParanoid; Q9DBM0; -. DR OMA; WLAWEDY; -. DR OrthoDB; 66620at2759; -. DR PhylomeDB; Q9DBM0; -. DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis. DR BioGRID-ORCS; 67470; 3 hits in 77 CRISPR screens. DR PRO; PR:Q9DBM0; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q9DBM0; protein. DR Bgee; ENSMUSG00000024254; Expressed in small intestine Peyer's patch and 22 other cell types or tissues. DR ExpressionAtlas; Q9DBM0; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0043235; C:signaling receptor complex; IDA:BHF-UCL. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI. DR GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL. DR GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; ISO:GO_Central. DR GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; ISO:GO_Central. DR GO; GO:0015914; P:phospholipid transport; IMP:MGI. DR GO; GO:0055092; P:sterol homeostasis; IMP:MGI. DR GO; GO:0015918; P:sterol transport; IDA:UniProtKB. DR CDD; cd03234; ABCG_White; 1. DR FunFam; 3.40.50.300:FF:000831; ATP-binding cassette sub-family G member 8; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR013525; ABC2_TM. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. 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:SF71; ATP-BINDING CASSETTE SUB-FAMILY G MEMBER 8; 1. DR Pfam; PF01061; ABC2_membrane; 1. DR Pfam; PF19055; ABC2_membrane_7; 1. DR Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Glycoprotein; Lipid transport; KW Magnesium; Membrane; Metal-binding; Reference proteome; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..673 FT /note="ATP-binding cassette sub-family G member 8" FT /id="PRO_0000093397" FT TOPO_DOM 1..416 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 417..437 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 438..447 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 448..468 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 469..497 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 498..518 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 519..527 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 528..548 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 549..555 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 556..576 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 577..639 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TRANSMEM 640..660 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT TOPO_DOM 661..673 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9H221" FT DOMAIN 48..314 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 411..665 FT /note="ABC transmembrane type-2" FT CARBOHYD 619 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15054092" FT VAR_SEQ 377 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11452359, FT ECO:0000303|PubMed:11907139" FT /id="VSP_000053" FT MUTAGEN 112 FT /note="R->K,M: No effect on ATP-binding and on expression FT of both ABCG5 and ABCG8. No effect on sterol transport." FT /evidence="ECO:0000269|PubMed:16352607" FT MUTAGEN 214 FT /note="V->I: No effect on sterol transport; when associated FT with S-216." FT /evidence="ECO:0000269|PubMed:16352607" FT MUTAGEN 216 FT /note="G->S: No effect on sterol transport; when associated FT with I-214." FT /evidence="ECO:0000269|PubMed:16352607" FT MUTAGEN 217 FT /note="G->D: Abolishes cholesterol transport activity, and FT nearly abolishes plant sterol transport." FT /evidence="ECO:0000269|PubMed:16352607, FT ECO:0000269|PubMed:16867993" FT MUTAGEN 239 FT /note="E->D: No effect on sterol transport." FT /evidence="ECO:0000269|PubMed:16352607" FT MUTAGEN 239 FT /note="E->Q: Mildly decreases cholesterol transport. No FT effect on plant sterol transport." FT /evidence="ECO:0000269|PubMed:16352607" FT MUTAGEN 619 FT /note="N->A,Q: Abolishes N-glycosylation." FT /evidence="ECO:0000269|PubMed:15054092" FT MUTAGEN 664..673 FT /note="Missing: Abolishes expression at the apical cell FT membrane. Strongly decreases cholesterol secretion into FT bile." FT /evidence="ECO:0000269|PubMed:18402465" FT CONFLICT 544 FT /note="T -> N (in Ref. 2; AAL82898)" FT /evidence="ECO:0000305" SQ SEQUENCE 673 AA; 75996 MW; 78012611A5DF2589 CRC64; MAEKTKEETQ LWNGTVLQDA SQGLQDSLFS SESDNSLYFT YSGQSNTLEV RDLTYQVDIA SQVPWFEQLA QFKIPWRSHS SQDSCELGIR NLSFKVRSGQ MLAIIGSSGC GRASLLDVIT GRGHGGKMKS GQIWINGQPS TPQLVRKCVA HVRQHDQLLP NLTVRETLAF IAQMRLPRTF SQAQRDKRVE DVIAELRLRQ CANTRVGNTY VRGVSGGERR RVSIGVQLLW NPGILILDEP TSGLDSFTAH NLVTTLSRLA KGNRLVLISL HQPRSDIFRL FDLVLLMTSG TPIYLGAAQQ MVQYFTSIGH PCPRYSNPAD FYVDLTSIDR RSKEREVATV EKAQSLAALF LEKVQGFDDF LWKAEAKELN TSTHTVSLTL TQDTDCGTAV ELPGMIEQFS TLIRRQISND FRDLPTLLIH GSEACLMSLI IGFLYYGHGA KQLSFMDTAA LLFMIGALIP FNVILDVVSK CHSERSMLYY ELEDGLYTAG PYFFAKILGE LPEHCAYVII YAMPIYWLTN LRPVPELFLL HFLLVWLVVF CCRTMALAAS AMLPTFHMSS FFCNALYNSF YLTAGFMINL DNLWIVPAWI SKLSFLRWCF SGLMQIQFNG HLYTTQIGNF TFSILGDTMI SAMDLNSHPL YAIYLIVIGI SYGFLFLYYL SLKLIKQKSI QDW //