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ATP-binding cassette sub-family G member 5 (Sterolin-1)

 ABCG5_MOUSE             Reviewed;         652 AA.
Q99PE8; Q540E8;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 146.
RecName: Full=ATP-binding cassette sub-family G member 5;
AltName: Full=Sterolin-1 {ECO:0000303|PubMed:11907139, ECO:0000303|PubMed:15040800};
Name=Abcg5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=11138003; DOI=10.1038/83799;
Lee M.-H., Lu K., Hazard S., Yu H., Shulenin S., Hidaka H., Kojima H.,
Allikmets R., Sakuma N., Pegoraro R., Srivastava A.K., Salen G.,
Dean M., Patel S.B.;
"Identification of a gene, ABCG5, important in the regulation of
dietary cholesterol absorption.";
Nat. Genet. 27:79-83(2001).
[2] {ECO:0000312|EMBL:AAL82586.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv {ECO:0000312|EMBL:AAL82586.1};
PubMed=11907139;
Lu K., Lee M.H., Yu H., Zhou Y., Sandell S.A., Salen G., Patel S.B.;
"Molecular cloning, genomic organization, genetic variations, and
characterization of murine sterolin genes Abcg5 and Abcg8.";
J. Lipid Res. 43:565-578(2002).
[3] {ECO:0000312|EMBL:AAO45094.1}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=PERA/Ei {ECO:0000312|EMBL:AAO45094.1};
TISSUE=Liver {ECO:0000312|EMBL:AAO45094.1};
PubMed=12949731; DOI=10.1016/S0016-5085(03)01053-9;
Wittenburg H., Lyons M.A., Li R., Churchill G.A., Carey M.C.,
Paigen B.;
"FXR and ABCG5/ABCG8 as determinants of cholesterol gallstone
formation from quantitative trait locus mapping in mice.";
Gastroenterology 125:868-881(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28965.1};
TISSUE=Liver {ECO:0000312|EMBL:BAE28965.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11099417; DOI=10.1126/science.290.5497.1771;
Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J.,
Kwiterovich P., Shan B., Barnes R., Hobbs H.H.;
"Accumulation of dietary cholesterol in sitosterolemia caused by
mutations in adjacent ABC transporters.";
Science 290:1771-1775(2000).
[8]
SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=12208867; DOI=10.1172/JCI16000;
Graf G.A., Li W.P., Gerard R.D., Gelissen I., White A., Cohen J.C.,
Hobbs H.H.;
"Coexpression of ATP-binding cassette proteins ABCG5 and ABCG8 permits
their transport to the apical surface.";
J. Clin. Invest. 110:659-669(2002).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=12444248; DOI=10.1073/pnas.252582399;
Yu L., Hammer R.E., Li-Hawkins J., Von Bergmann K., Lutjohann D.,
Cohen J.C., Hobbs H.H.;
"Disruption of Abcg5 and Abcg8 in mice reveals their crucial role in
biliary cholesterol secretion.";
Proc. Natl. Acad. Sci. U.S.A. 99:16237-16242(2002).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14504269; DOI=10.1074/jbc.M310223200;
Graf G.A., Yu L., Li W.P., Gerard R., Tuma P.L., Cohen J.C.,
Hobbs H.H.;
"ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and
biliary cholesterol excretion.";
J. Biol. Chem. 278:48275-48282(2003).
[11]
DOWN-REGULATION BY ENDOTOXIN, AND INDUCTION.
PubMed=12777468; DOI=10.1194/jlr.M300100-JLR200;
Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C.,
Feingold K.R.;
"Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
ABCG1 in J774 murine macrophages: differential role of LXR.";
J. Lipid Res. 44:1728-1736(2003).
[12]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=15040800; DOI=10.1186/1741-7015-2-5;
Klett E.L., Lu K., Kosters A., Vink E., Lee M.H., Altenburg M.,
Shefer S., Batta A.K., Yu H., Chen J., Klein R., Looije N.,
Oude-Elferink R., Groen A.K., Maeda N., Salen G., Patel S.B.;
"A mouse model of sitosterolemia: absence of Abcg8/sterolin-2 results
in failure to secrete biliary cholesterol.";
BMC Med. 2:5-5(2004).
[13]
SUBUNIT, GLYCOSYLATION AT ASN-585 AND ASN-592, AND MUTAGENESIS OF
ASN-585 AND ASN-592.
PubMed=15054092; DOI=10.1074/jbc.M402634200;
Graf G.A., Cohen J.C., Hobbs H.H.;
"Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and
trafficking.";
J. Biol. Chem. 279:24881-24888(2004).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION VIA THE OXYSTEROLS
RECEPTOR LXR PATHWAY.
PubMed=14657202; DOI=10.1194/jlr.M300377-JLR200;
Yu L., von Bergmann K., Lutjohann D., Hobbs H.H., Cohen J.C.;
"Selective sterol accumulation in ABCG5/ABCG8-deficient mice.";
J. Lipid Res. 45:301-307(2004).
[15]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, COFACTOR, DOMAIN, AND
MUTAGENESIS OF LYS-93; ILE-194; SER-196; GLY-197 AND GLU-219.
PubMed=16352607; DOI=10.1074/jbc.M512277200;
Zhang D.W., Graf G.A., Gerard R.D., Cohen J.C., Hobbs H.H.;
"Functional asymmetry of nucleotide-binding domains in ABCG5 and
ABCG8.";
J. Biol. Chem. 281:4507-4516(2006).
[16]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF
LYS-93, ENZYME REGULATION, AND COFACTOR.
PubMed=16867993; DOI=10.1074/jbc.M605603200;
Wang J., Sun F., Zhang D.W., Ma Y., Xu F., Belani J.D., Cohen J.C.,
Hobbs H.H., Xie X.S.;
"Sterol transfer by ABCG5 and ABCG8: in vitro assay and
reconstitution.";
J. Biol. Chem. 281:27894-27904(2006).
[17]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY,
GLYCOSYLATION, PALMITOYLATION AT CYS-61, AND MUTAGENESIS OF CYS-61.
PubMed=18402465; DOI=10.1021/bi800292v;
Wang J., Zhang D.W., Lei Y., Xu F., Cohen J.C., Hobbs H.H., Xie X.S.;
"Purification and reconstitution of sterol transfer by native mouse
ABCG5 and ABCG8.";
Biochemistry 47:5194-5204(2008).
[18]
DISEASE, FUNCTION, VARIANT TRAC 492-TRP--ARG-652 DEL, AND
CHARACTERIZATION OF VARIANT TRAC 492-TRP--ARG-652 DEL.
PubMed=19846887; DOI=10.1182/blood-2009-05-219808;
Chase T.H., Lyons B.L., Bronson R.T., Foreman O., Donahue L.R.,
Burzenski L.M., Gott B., Lane P., Harris B., Ceglarek U., Thiery J.,
Wittenburg H., Thon J.N., Italiano J.E. Jr., Johnson K.R.,
Shultz L.D.;
"The mouse mutation 'thrombocytopenia and cardiomyopathy' (trac)
disrupts Abcg5: a spontaneous single gene model for human hereditary
phytosterolemia/sitosterolemia.";
Blood 115:1267-1276(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[20]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=25378657; DOI=10.1194/jlr.M054544;
Wang J., Mitsche M.A., Luetjohann D., Cohen J.C., Xie X.S.,
Hobbs H.H.;
"Relative roles of ABCG5/ABCG8 in liver and intestine.";
J. Lipid Res. 56:319-330(2015).
-!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that
mediates Mg(2+)- and ATP-dependent sterol transport across the
cell membrane (PubMed:16352607, PubMed:16867993, PubMed:18402465).
Plays an essential role in the selective transport of dietary
plant sterols and cholesterol in and out of the enterocytes and in
the selective sterol excretion by the liver into bile
(PubMed:12444248, PubMed:14504269, PubMed:14657202,
PubMed:19846887, PubMed:25378657). Required for normal sterol
homeostasis (PubMed:12444248, PubMed:14657202). The heterodimer
with ABCG8 has ATPase activity (PubMed:16352607, PubMed:16867993).
{ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:14504269,
ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:16352607,
ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465,
ECO:0000269|PubMed:19846887, ECO:0000269|PubMed:25378657}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16352607,
ECO:0000269|PubMed:16867993};
-!- ENZYME REGULATION: Cholesterol transport is inhibited by vanadate
and by beryllium fluoride. {ECO:0000269|PubMed:16867993}.
-!- SUBUNIT: Heterodimer with ABCG8. {ECO:0000269|PubMed:12208867,
ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:15054092,
ECO:0000269|PubMed:16352607, ECO:0000269|PubMed:16867993,
ECO:0000269|PubMed:18402465}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12208867,
ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-
pass membrane protein {ECO:0000305}. Apical cell membrane
{ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269,
ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:16867993,
ECO:0000269|PubMed:18402465}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in liver and jejunum
(PubMed:12444248, PubMed:15040800, PubMed:18402465,
PubMed:25378657). Detected on enterocyte villi (at protein level)
(PubMed:15040800). Expressed in jejunum, ileum and, at lower
level, in the liver (PubMed:11138003, PubMed:11907139,
PubMed:11099417, PubMed:12444248, PubMed:25378657).
{ECO:0000269|PubMed:11099417, ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11907139, ECO:0000269|PubMed:12444248,
ECO:0000269|PubMed:15040800, ECO:0000269|PubMed:18402465,
ECO:0000269|PubMed:25378657}.
-!- INDUCTION: Up-regulated in liver and small intestine by
cholesterol feeding (PubMed:11099417). Up-regulated via the
oxysterols receptor LXR/retinoic X receptor (LXR/RXR) pathway
(PubMed:14657202). Endotoxin (LPS) significantly decreased mRNA
levels in the liver but not in the small intestine
(PubMed:12777468). {ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:12777468, ECO:0000269|PubMed:14657202}.
-!- DOMAIN: The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T)
is expected to bind ATP. Within this motif, the conserved Lys is
essential for transport activity mediated by the heterodimer with
ABCG8. {ECO:0000269|PubMed:16352607}.
-!- PTM: N-glycosylated (PubMed:12208867, PubMed:12444248,
PubMed:16867993, PubMed:15040800, PubMed:15054092,
PubMed:18402465, PubMed:25378657). N-glycosylation is important
for efficient export out of the endoplasmic reticulum
(PubMed:15054092). {ECO:0000269|PubMed:12208867,
ECO:0000269|PubMed:12444248, ECO:0000269|PubMed:15040800,
ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16867993,
ECO:0000269|PubMed:18402465, ECO:0000269|PubMed:25378657}.
-!- DISEASE: Note=A spontaneous mutation gives raise to
thrombocytopenia and cardiomyopathy (trac), with recessive
inheritance and fully penetrant phenotype. Mice are small,
infertile, and have shortened lifespan.
{ECO:0000269|PubMed:19846887}.
-!- DISRUPTION PHENOTYPE: Mice deficient for both Abcg5 and Abcg8
appear healthy and are fertile, but display strongly increased
levels of the food-derived plant sterols sitosterol and
campesterol in liver and blood plasma (PubMed:12444248,
PubMed:14657202, PubMed:25378657). When mice are fed chow
containing 0.02% cholesterol, cholesterol levels in blood plasma
and in liver are considerably lower than in wild-type
(PubMed:12444248, PubMed:14657202). In spite of the increased
plasma and liver levels of plant sterols, and the decreased
cholesterol levels, the total sterol levels in plasma and liver
are closely similar in wild-type and mutant mice
(PubMed:14657202). When mice are fed chow containing 2%
cholesterol, plasma cholesterol levels remain stable in wild-type,
but increase 2.4-fold in mutant mice. In the liver of mice kept on
chow containing 2% cholesterol, cholesterol levels increase 3-fold
for wild-type mice and 18-fold for mutant mice, resulting in much
higher cholesterol levels than in wild-type livers
(PubMed:12444248). Dietary cholesterol absorption appears normal
in mutant mice, but the absorption of dietary cholestanol,
campesterol and sitosterol is increased (PubMed:12444248). At the
same time, mutant mice have very low cholesterol levels in bile,
suggesting that the increased hepatic cholesterol levels are due
to impaired cholesterol secretion into bile (PubMed:12444248).
Likewise, the levels of the food-derived plant sterols
stigmasterol, sitosterol, campesterol and brassicasterol are
strongly decreased in bile from mutant mice (PubMed:14657202). In
contrast, biliary phospholipid and bile acid levels appear
unchanged relative to wild-type (PubMed:12444248). The blood
plasma of mice with liver-specific or intestine-specific
disruption of Abcg5 and Abcg8 has nearly normal levels of
cholesterol, and mildly increased levels of sitosterol and
campesterol (PubMed:25378657). Mice with intestine-specific
disruption of Abcg5 and Abcg8 have strongly increased levels of
sitosterol and campesterol in enterocytes, similar to that
observed for mice with complete gene disruption (PubMed:25378657).
In addition, they display strongly increased levels of sitosterol
and campesterol in bile (PubMed:25378657). Mice with liver-
specific disruption of Abcg5 and Abcg8 have slightly increased
levels of campesterol and sitosterol in the liver, and normal, low
levels of sitosterol and campesterol in bile (PubMed:25378657).
Enterocytes and liver from mice with liver-specific or intestine-
specific disruption of Abcg5 and Abcg8 have normal cholesterol
levels (PubMed:25378657). {ECO:0000269|PubMed:12444248,
ECO:0000269|PubMed:14657202, ECO:0000269|PubMed:25378657}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
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EMBL; AF312713; AAG53097.1; -; mRNA.
EMBL; AH011511; AAL82586.1; -; Genomic_DNA.
EMBL; AF351786; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351787; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351789; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351790; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351791; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351792; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351793; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351794; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351795; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351796; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AF351797; AAL82586.1; JOINED; Genomic_DNA.
EMBL; AY195873; AAO45094.1; -; mRNA.
EMBL; AK149569; BAE28965.1; -; mRNA.
EMBL; CH466537; EDL38580.1; -; Genomic_DNA.
EMBL; BC106766; AAI06767.1; -; mRNA.
CCDS; CCDS29001.1; -.
RefSeq; NP_114090.1; NM_031884.2.
UniGene; Mm.289590; -.
ProteinModelPortal; Q99PE8; -.
SMR; Q99PE8; -.
CORUM; Q99PE8; -.
STRING; 10090.ENSMUSP00000069495; -.
iPTMnet; Q99PE8; -.
PhosphoSitePlus; Q99PE8; -.
SwissPalm; Q99PE8; -.
MaxQB; Q99PE8; -.
PaxDb; Q99PE8; -.
PRIDE; Q99PE8; -.
Ensembl; ENSMUST00000066175; ENSMUSP00000069495; ENSMUSG00000040505.
GeneID; 27409; -.
KEGG; mmu:27409; -.
UCSC; uc008dsz.1; mouse.
CTD; 64240; -.
MGI; MGI:1351659; Abcg5.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00740000114855; -.
HOGENOM; HOG000033763; -.
HOVERGEN; HBG050443; -.
InParanoid; Q99PE8; -.
KO; K05683; -.
OMA; NAVNLFP; -.
OrthoDB; EOG091G0FOJ; -.
PhylomeDB; Q99PE8; -.
TreeFam; TF105212; -.
Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
PRO; PR:Q99PE8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000040505; -.
ExpressionAtlas; Q99PE8; baseline and differential.
Genevisible; Q99PE8; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; ISO:MGI.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:0007588; P:excretion; IMP:BHF-UCL.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; ISO:MGI.
GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; ISO:MGI.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disease mutation;
Glycoprotein; Lipid transport; Lipoprotein; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Palmitate; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 652 ATP-binding cassette sub-family G member
5.
/FTId=PRO_0000093394.
TOPO_DOM 1 384 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 385 405 Helical; Name=1.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 406 422 Extracellular.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 423 443 Helical; Name=2.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 444 468 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 469 490 Helical; Name=3.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 491 501 Extracellular.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 502 522 Helical; Name=4.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 523 529 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 530 550 Helical; Name=5.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 551 624 Extracellular.
{ECO:0000250|UniProtKB:Q9H222}.
TRANSMEM 625 645 Helical; Name=6.
{ECO:0000250|UniProtKB:Q9H222}.
TOPO_DOM 646 652 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H222}.
DOMAIN 39 294 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 389 646 ABC transmembrane type-2.
NP_BIND 87 94 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
LIPID 61 61 S-palmitoyl cysteine.
{ECO:0000269|PubMed:18402465}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 585 585 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15054092}.
CARBOHYD 592 592 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15054092}.
VARIANT 462 652 Missing (in trac; strongly increased
levels of sitosterol, brassicasterol and
campesterol in blood plasma).
{ECO:0000269|PubMed:19846887}.
MUTAGEN 61 61 C->A: Abolishes palmitoylation. No effect
on function and subcellular location.
{ECO:0000269|PubMed:18402465}.
MUTAGEN 93 93 K->M: Disrupts sterol transport activity.
Decreases expression of both ABCG5 and
ABCG8. {ECO:0000269|PubMed:16352607,
ECO:0000269|PubMed:16867993}.
MUTAGEN 93 93 K->R: Strongly reduces cholesterol
transport activity, but has little effect
on biliary secretion of campesterol and
sitosterol. No effect on ATP-binding and
on expression of ABCG5 and ABCG8.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 194 194 I->V: No effect on cholesterol and
sitosterol transport activity; when
associated with G-196.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 196 196 S->G: No effect on cholesterol and
sitosterol transport activity; when
associated with V-194.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 197 197 G->D: No effect on cholesterol and
sitosterol transport activity. Mildly
reduced expression of ABCG5 and ABCG8.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 219 219 E->D: Decreases expression of both ABCG5
and ABCG8. Disrupts sterol transport
activity. {ECO:0000269|PubMed:16352607}.
MUTAGEN 219 219 E->Q: Strongly decreases expression of
both ABCG5 and ABCG8. Disrupts sterol
transport activity.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 585 585 N->Q: Loss of one N-glycosylation site.
Abolishes N-glycosylation; when
associated with Q-592.
{ECO:0000269|PubMed:15054092}.
MUTAGEN 592 592 N->Q: Loss of one N-glycosylation site.
Abolishes N-glycosylation; when
associated with Q-585.
{ECO:0000269|PubMed:15054092}.
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


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