ABCG5_MOUSE
ID ABCG5_MOUSE Reviewed; 652 AA.
AC Q99PE8; Q540E8;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=ATP-binding cassette sub-family G member 5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000269|PubMed:16867993};
DE AltName: Full=Sterolin-1 {ECO:0000303|PubMed:11907139, ECO:0000303|PubMed:15040800};
GN Name=Abcg5 {ECO:0000312|MGI:MGI:1351659};
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11138003; DOI=10.1038/83799;
RA Lee M.-H., Lu K., Hazard S., Yu H., Shulenin S., Hidaka H., Kojima H.,
RA Allikmets R., Sakuma N., Pegoraro R., Srivastava A.K., Salen G., Dean M.,
RA Patel S.B.;
RT "Identification of a gene, ABCG5, important in the regulation of dietary
RT cholesterol absorption.";
RL Nat. Genet. 27:79-83(2001).
RN [2] {ECO:0000312|EMBL:AAL82586.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAL82586.1};
RX PubMed=11907139;
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] {ECO:0000312|EMBL:AAO45094.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=PERA/Ei {ECO:0000312|EMBL:AAO45094.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAO45094.1};
RX PubMed=12949731; DOI=10.1016/s0016-5085(03)01053-9;
RA Wittenburg H., Lyons M.A., Li R., Churchill G.A., Carey M.C., Paigen B.;
RT "FXR and ABCG5/ABCG8 as determinants of cholesterol gallstone formation
RT from quantitative trait locus mapping in mice.";
RL Gastroenterology 125:868-881(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28965.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAE28965.1};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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 [11]
RP DOWN-REGULATION BY ENDOTOXIN, AND INDUCTION.
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 [12]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, 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 [13]
RP SUBUNIT, GLYCOSYLATION AT ASN-585 AND ASN-592, AND MUTAGENESIS OF ASN-585
RP AND ASN-592.
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 [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION VIA THE OXYSTEROLS RECEPTOR
RP LXR PATHWAY.
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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, COFACTOR, DOMAIN, AND MUTAGENESIS
RP OF LYS-93; ILE-194; SER-196; GLY-197 AND GLU-219.
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 [16]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF
RP LYS-93, 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 [17]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION,
RP PALMITOYLATION AT CYS-61, AND MUTAGENESIS OF CYS-61.
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 [18]
RP DISEASE, FUNCTION, VARIANT TRAC 492-TRP--ARG-652 DEL, AND CHARACTERIZATION
RP OF VARIANT TRAC 492-TRP--ARG-652 DEL.
RX PubMed=19846887; DOI=10.1182/blood-2009-05-219808;
RA Chase T.H., Lyons B.L., Bronson R.T., Foreman O., Donahue L.R.,
RA Burzenski L.M., Gott B., Lane P., Harris B., Ceglarek U., Thiery J.,
RA Wittenburg H., Thon J.N., Italiano J.E. Jr., Johnson K.R., Shultz L.D.;
RT "The mouse mutation 'thrombocytopenia and cardiomyopathy' (trac) disrupts
RT Abcg5: a spontaneous single gene model for human hereditary
RT phytosterolemia/sitosterolemia.";
RL Blood 115:1267-1276(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [20]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
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 dietary plant sterols and
CC cholesterol in and out of the enterocytes and in the selective sterol
CC excretion by the liver into bile (PubMed:12444248, PubMed:14504269,
CC PubMed:14657202, PubMed:19846887, PubMed:25378657). Required for normal
CC sterol homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer
CC with ABCG8 has 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:19846887, ECO:0000269|PubMed:25378657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; 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=ATP + H2O + sitosterol(in) = ADP + H(+) + phosphate +
CC sitosterol(out); Xref=Rhea:RHEA:39103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27693, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC 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:16352607, 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 ABCG8. {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:15040800, ECO:0000269|PubMed:16867993,
CC ECO:0000269|PubMed:18402465}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in liver and jejunum (PubMed:12444248,
CC PubMed:15040800, PubMed:18402465, PubMed:25378657). Detected on
CC enterocyte villi (at protein level) (PubMed:15040800). Expressed in
CC jejunum, ileum and, at lower level, in the liver (PubMed:11138003,
CC PubMed:11907139, PubMed:11099417, PubMed:12444248, PubMed:25378657).
CC {ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11138003,
CC ECO:0000269|PubMed:11907139, ECO:0000269|PubMed:12444248,
CC ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:18402465,
CC ECO:0000269|PubMed:25378657}.
CC -!- INDUCTION: Up-regulated in liver and small intestine by cholesterol
CC feeding (PubMed:11099417). Up-regulated via the oxysterols receptor
CC LXR/retinoic X receptor (LXR/RXR) pathway (PubMed:14657202). Endotoxin
CC (LPS) significantly decreased mRNA levels in the liver but not in the
CC small intestine (PubMed:12777468). {ECO:0000269|PubMed:11099417,
CC ECO:0000269|PubMed:12777468, ECO:0000269|PubMed:14657202}.
CC -!- DOMAIN: The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is
CC expected to bind ATP. Within this motif, the conserved Lys is essential
CC for transport activity mediated by the heterodimer with ABCG8.
CC {ECO:0000269|PubMed:16352607}.
CC -!- PTM: N-glycosylated (PubMed:12208867, PubMed:12444248, PubMed:16867993,
CC PubMed:15040800, PubMed:15054092, PubMed:18402465, PubMed:25378657). N-
CC glycosylation is important for efficient export out of the endoplasmic
CC reticulum (PubMed:15054092). {ECO:0000269|PubMed:12208867,
CC ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800,
CC ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993,
CC ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}.
CC -!- DISEASE: Note=A spontaneous mutation gives raise to thrombocytopenia
CC and cardiomyopathy (trac), with recessive inheritance and fully
CC penetrant phenotype. Mice are small, infertile, and have shortened
CC lifespan. {ECO:0000269|PubMed:19846887}.
CC -!- DISRUPTION PHENOTYPE: Mice deficient for both Abcg5 and Abcg8 appear
CC healthy and are fertile, but display strongly increased levels of the
CC food-derived plant sterols sitosterol and campesterol in liver and
CC blood plasma (PubMed:12444248, PubMed:14657202, PubMed:25378657). When
CC mice are fed chow containing 0.02% cholesterol, cholesterol levels in
CC blood plasma and in liver are considerably lower than in wild-type
CC (PubMed:12444248, PubMed:14657202). In spite of the increased plasma
CC and liver levels of plant sterols, and the decreased cholesterol
CC levels, the total sterol levels in plasma and liver are closely similar
CC in wild-type and mutant mice (PubMed:14657202). When mice are fed chow
CC containing 2% cholesterol, plasma cholesterol levels remain stable in
CC wild-type, but increase 2.4-fold in mutant mice. In the liver of mice
CC kept on chow containing 2% cholesterol, cholesterol levels increase 3-
CC fold for wild-type mice and 18-fold for mutant mice, resulting in much
CC higher cholesterol levels than in wild-type livers (PubMed:12444248).
CC Dietary 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:25378657}.
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; AF312713; AAG53097.1; -; mRNA.
DR EMBL; AH011511; AAL82586.1; -; Genomic_DNA.
DR EMBL; AF351786; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351787; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351789; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351790; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351791; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351792; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351793; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351794; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351795; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351796; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AF351797; AAL82586.1; JOINED; Genomic_DNA.
DR EMBL; AY195873; AAO45094.1; -; mRNA.
DR EMBL; AK149569; BAE28965.1; -; mRNA.
DR EMBL; CH466537; EDL38580.1; -; Genomic_DNA.
DR EMBL; BC106766; AAI06767.1; -; mRNA.
DR CCDS; CCDS29001.1; -.
DR RefSeq; NP_114090.1; NM_031884.2.
DR AlphaFoldDB; Q99PE8; -.
DR SMR; Q99PE8; -.
DR BioGRID; 205215; 1.
DR CORUM; Q99PE8; -.
DR STRING; 10090.ENSMUSP00000069495; -.
DR GlyGen; Q99PE8; 3 sites.
DR iPTMnet; Q99PE8; -.
DR PhosphoSitePlus; Q99PE8; -.
DR SwissPalm; Q99PE8; -.
DR jPOST; Q99PE8; -.
DR MaxQB; Q99PE8; -.
DR PaxDb; Q99PE8; -.
DR PRIDE; Q99PE8; -.
DR ProteomicsDB; 285820; -.
DR Antibodypedia; 14899; 235 antibodies from 31 providers.
DR DNASU; 27409; -.
DR Ensembl; ENSMUST00000066175; ENSMUSP00000069495; ENSMUSG00000040505.
DR GeneID; 27409; -.
DR KEGG; mmu:27409; -.
DR UCSC; uc008dsz.1; mouse.
DR CTD; 64240; -.
DR MGI; MGI:1351659; Abcg5.
DR VEuPathDB; HostDB:ENSMUSG00000040505; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000157985; -.
DR HOGENOM; CLU_000604_57_9_1; -.
DR InParanoid; Q99PE8; -.
DR OMA; RVRPWWD; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q99PE8; -.
DR TreeFam; TF105212; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR BioGRID-ORCS; 27409; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Abcg5; mouse.
DR PRO; PR:Q99PE8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99PE8; protein.
DR Bgee; ENSMUSG00000040505; Expressed in small intestine Peyer's patch and 57 other tissues.
DR ExpressionAtlas; Q99PE8; baseline and differential.
DR Genevisible; Q99PE8; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
DR GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; ISO:MGI.
DR GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; ISO:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0015918; P:sterol transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disease variant; Glycoprotein; Lipid transport;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Palmitate; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..652
FT /note="ATP-binding cassette sub-family G member 5"
FT /id="PRO_0000093394"
FT TOPO_DOM 1..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 385..405
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 406..422
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 423..443
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 444..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 469..490
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 491..501
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 502..522
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 523..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 530..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 551..624
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TRANSMEM 625..645
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT TOPO_DOM 646..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H222"
FT DOMAIN 39..294
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 389..646
FT /note="ABC transmembrane type-2"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT LIPID 61
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:18402465"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15054092"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15054092"
FT VARIANT 462..652
FT /note="Missing (in trac; strongly increased levels of
FT sitosterol, brassicasterol and campesterol in blood
FT plasma)"
FT /evidence="ECO:0000269|PubMed:19846887"
FT MUTAGEN 61
FT /note="C->A: Abolishes palmitoylation. No effect on
FT function and subcellular location."
FT /evidence="ECO:0000269|PubMed:18402465"
FT MUTAGEN 93
FT /note="K->M: Disrupts sterol transport activity. Decreases
FT expression of both ABCG5 and ABCG8."
FT /evidence="ECO:0000269|PubMed:16352607,
FT ECO:0000269|PubMed:16867993"
FT MUTAGEN 93
FT /note="K->R: Strongly reduces cholesterol transport
FT activity, but has little effect on biliary secretion of
FT campesterol and sitosterol. No effect on ATP-binding and on
FT expression of ABCG5 and ABCG8."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 194
FT /note="I->V: No effect on cholesterol and sitosterol
FT transport activity; when associated with G-196."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 196
FT /note="S->G: No effect on cholesterol and sitosterol
FT transport activity; when associated with V-194."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 197
FT /note="G->D: No effect on cholesterol and sitosterol
FT transport activity. Mildly reduced expression of ABCG5 and
FT ABCG8."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 219
FT /note="E->D: Decreases expression of both ABCG5 and ABCG8.
FT Disrupts sterol transport activity."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 219
FT /note="E->Q: Strongly decreases expression of both ABCG5
FT and ABCG8. Disrupts sterol transport activity."
FT /evidence="ECO:0000269|PubMed:16352607"
FT MUTAGEN 585
FT /note="N->Q: Loss of one N-glycosylation site. Abolishes N-
FT glycosylation; when associated with Q-592."
FT /evidence="ECO:0000269|PubMed:15054092"
FT MUTAGEN 592
FT /note="N->Q: Loss of one N-glycosylation site. Abolishes N-
FT glycosylation; when associated with Q-585."
FT /evidence="ECO:0000269|PubMed:15054092"
SQ SEQUENCE 652 AA; 73244 MW; 80CE37ADCC19771E CRC64;
MGELPFLSPE GARGPHINRG SLSSLEQGSV TGTEARHSLG VLHVSYSVSN RVGPWWNIKS
CQQKWDRQIL KDVSLYIESG QIMCILGSSG SGKTTLLDAI SGRLRRTGTL EGEVFVNGCE
LRRDQFQDCF SYVLQSDVFL SSLTVRETLR YTAMLALCRS SADFYNKKVE AVMTELSLSH
VADQMIGSYN FGGISSGERR RVSIAAQLLQ DPKVMMLDEP TTGLDCMTAN QIVLLLAELA
RRDRIVIVTI HQPRSELFQH FDKIAILTYG ELVFCGTPEE MLGFFNNCGY PCPEHSNPFD
FYMDLTSVDT QSREREIETY KRVQMLECAF KESDIYHKIL ENIERARYLK TLPTVPFKTK
DPPGMFGKLG VLLRRVTRNL MRNKQAVIMR LVQNLIMGLF LIFYLLRVQN NTLKGAVQDR
VGLLYQLVGA TPYTGMLNAV NLFPMLRAVS DQESQDGLYH KWQMLLAYVL HVLPFSVIAT
VIFSSVCYWT LGLYPEVARF GYFSAALLAP HLIGEFLTLV LLGIVQNPNI VNSIVALLSI
SGLLIGSGFI RNIQEMPIPL KILGYFTFQK YCCEILVVNE FYGLNFTCGG SNTSMLNHPM
CAITQGVQFI EKTCPGATSR FTANFLILYG FIPALVILGI VIFKVRDYLI SR
