Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

ATP-binding cassette sub-family G member 8 (Sterolin-2)

 ABCG8_MOUSE             Reviewed;         673 AA.
Q9DBM0; Q8R543;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
05-DEC-2018, entry version 148.
RecName: Full=ATP-binding cassette sub-family G member 8;
AltName: Full=Sterolin-2 {ECO:0000303|PubMed:11452359, ECO:0000303|PubMed:11907139};
Name=Abcg8;
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] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=11452359; DOI=10.1086/321294;
Lu K., Lee M.-H., Hazard S., Brooks-Wilson A., Hidaka H., Kojima H.,
Ose L., Stalenhoef A.F.H., Mietinnen T., Bjorkhem I., Bruckert E.,
Pandya A., Brewer H.B. Jr., Salen G., Dean M., Srivastava A.K.,
Patel S.B.;
"Two genes that map to the STSL locus cause sitosterolemia: genomic
structure and spectrum of mutations involving sterolin-1 and sterolin-
2, encoded by ABCG5 and ABCG8, respectively.";
Am. J. Hum. Genet. 69:278-290(2001).
[2] {ECO:0000312|EMBL:AAL82898.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
STRAIN=129/Sv {ECO:0000312|EMBL:AAL82898.1};
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Liver;
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).
[4]
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).
[5]
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).
[6]
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).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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).
[8]
DOWN-REGULATION BY ENDOTOXIN.
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).
[9]
DISRUPTION PHENOTYPE, 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).
[10]
SUBUNIT, GLYCOSYLATION AT ASN-619, AND MUTAGENESIS OF ASN-619.
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).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
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).
[12]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-112;
VAL-214; GLY-216; GLY-217 AND GLU-239, AND DOMAIN.
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).
[13]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF
ARG-112 AND GLY-217, ACTIVITY 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).
[14]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY,
GLYCOSYLATION, AND MUTAGENESIS OF 664-LEU--TRP-673.
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).
[15]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
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 the dietary
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:25378657). Plays an
important role in preventing the accumulation of dietary plant
sterols in the body (PubMed:12444248, PubMed:14657202). Required
for normal sterol homeostasis (PubMed:12444248, PubMed:14657202).
The heterodimer with ABCG5 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:25378657}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16867993};
-!- ACTIVITY REGULATION: Cholesterol transport is inhibited by
vanadate and by beryllium fluoride. {ECO:0000269|PubMed:16867993}.
-!- SUBUNIT: Heterodimer with ABCG5. {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:16867993, ECO:0000269|PubMed:18402465}; Multi-
pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9DBM0-1; Sequence=Displayed;
Name=2;
IsoId=Q9DBM0-2; Sequence=VSP_000053;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in liver and jejunum (at protein
level) (PubMed:12444248, PubMed:18402465, PubMed:25378657).
Expressed in jejunum and ileum and, at lower level, in the liver
(PubMed:11907139, PubMed:11099417, PubMed:12444248,
PubMed:15040800, PubMed:25378657). {ECO:0000269|PubMed:11099417,
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). Possibly mediated by the
liver X receptor/retinoic X receptor (LXR/RXR) pathway. 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}.
-!- DOMAIN: A functional Walker motif (consensus sequence G-X-X-G-X-G-
K-[ST]-T) is expected to bind ATP. The essential Lys in this
region is not conserved in ABCG8 (G-S-S-G-C-R-A-S) and is not
required for transport activity mediated by the heterodimer with
ABCG5. {ECO:0000269|PubMed:16352607}.
-!- PTM: N-glycosylated (PubMed:12208867, PubMed:12444248,
PubMed:16867993, PubMed:15054092, PubMed:18402465). 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:15054092, ECO:0000269|PubMed:16867993,
ECO:0000269|PubMed:18402465}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate. They display decreased cholesterol levels, but strongly
increased levels of the food-derived plant sterols campesterol and
beta-sitosterol in blood plasma, liver and spleen
(PubMed:25378657). Besides, mutant mice may have slightly
increased total plasma triglyceride levels. Expression of Abcg5 is
not affected. Mutant mice display decreased biliary sterol
secretion (PubMed:15040800). 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:15040800,
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}.
-!- CAUTION: Seems to have a defective ATP-binding region.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AH011518; AAL82898.1; -; Genomic_DNA.
EMBL; AF351799; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351800; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351801; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351802; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351803; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351804; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351807; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351808; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351809; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF351810; AAL82898.1; JOINED; Genomic_DNA.
EMBL; AF324495; AAK84079.1; -; mRNA.
EMBL; AK004871; BAB23630.1; -; mRNA.
CCDS; CCDS29002.1; -. [Q9DBM0-1]
RefSeq; NP_001272934.1; NM_001286005.1.
RefSeq; NP_001334347.1; NM_001347418.1.
RefSeq; NP_080456.1; NM_026180.3. [Q9DBM0-1]
UniGene; Mm.26581; -.
ProteinModelPortal; Q9DBM0; -.
SMR; Q9DBM0; -.
CORUM; Q9DBM0; -.
STRING; 10090.ENSMUSP00000035246; -.
iPTMnet; Q9DBM0; -.
PhosphoSitePlus; Q9DBM0; -.
SwissPalm; Q9DBM0; -.
PaxDb; Q9DBM0; -.
PRIDE; Q9DBM0; -.
Ensembl; ENSMUST00000045714; ENSMUSP00000035246; ENSMUSG00000024254. [Q9DBM0-1]
GeneID; 67470; -.
KEGG; mmu:67470; -.
UCSC; uc008dta.2; mouse. [Q9DBM0-1]
CTD; 64241; -.
MGI; MGI:1914720; Abcg8.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00940000159739; -.
HOGENOM; HOG000033764; -.
HOVERGEN; HBG050444; -.
InParanoid; Q9DBM0; -.
KO; K05684; -.
OrthoDB; EOG091G0E38; -.
PhylomeDB; Q9DBM0; -.
TreeFam; TF105212; -.
Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
PRO; PR:Q9DBM0; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024254; Expressed in 38 organ(s), highest expression level in jejunum.
ExpressionAtlas; Q9DBM0; baseline and differential.
Genevisible; Q9DBM0; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
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:0015238; F:drug transmembrane transporter activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0015248; F:sterol transporter activity; ISO:MGI.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
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:0015914; P:phospholipid transport; IMP:MGI.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0055092; P:sterol homeostasis; IMP:MGI.
GO; GO:0015918; P:sterol transport; IMP:MGI.
GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Lipid transport; Magnesium; Membrane; Metal-binding;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 673 ATP-binding cassette sub-family G member
8.
/FTId=PRO_0000093397.
TOPO_DOM 1 416 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 417 437 Helical; Name=1.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 438 447 Extracellular.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 448 468 Helical; Name=2.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 469 497 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 498 518 Helical; Name=3.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 519 527 Extracellular.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 528 548 Helical; Name=4.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 549 555 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 556 576 Helical; Name=5.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 577 639 Extracellular.
{ECO:0000250|UniProtKB:Q9H221}.
TRANSMEM 640 660 Helical; Name=6.
{ECO:0000250|UniProtKB:Q9H221}.
TOPO_DOM 661 673 Cytoplasmic.
{ECO:0000250|UniProtKB:Q9H221}.
DOMAIN 48 314 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 411 665 ABC transmembrane type-2.
CARBOHYD 619 619 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15054092}.
VAR_SEQ 377 377 Missing (in isoform 2).
{ECO:0000303|PubMed:11452359,
ECO:0000303|PubMed:11907139}.
/FTId=VSP_000053.
MUTAGEN 112 112 R->K,M: No effect on ATP-binding and on
expression of both ABCG5 and ABCG8. No
effect on sterol transport.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 214 214 V->I: No effect on sterol transport; when
associated with S-216.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 216 216 G->S: No effect on sterol transport; when
associated with I-214.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 217 217 G->D: Abolishes cholesterol transport
activity, and nearly abolishes plant
sterol transport.
{ECO:0000269|PubMed:16352607,
ECO:0000269|PubMed:16867993}.
MUTAGEN 239 239 E->D: No effect on sterol transport.
{ECO:0000269|PubMed:16352607}.
MUTAGEN 239 239 E->Q: Mildly decreases cholesterol
transport. No effect on plant sterol
transport. {ECO:0000269|PubMed:16352607}.
MUTAGEN 619 619 N->A,Q: Abolishes N-glycosylation.
{ECO:0000269|PubMed:15054092}.
MUTAGEN 664 673 Missing: Abolishes expression at the
apical cell membrane. Strongly decreases
cholesterol secretion into bile.
{ECO:0000269|PubMed:18402465}.
CONFLICT 544 544 T -> N (in Ref. 2; AAL82898).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
E1242h ELISA kit ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
U1242h CLIA ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
E1242h ELISA ABC1,ABC-1,ABCA1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,CERP,Cholesterol efflux regulatory protein,Homo sapiens,Human 96T
E1242m ELISA kit Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
E1242m ELISA Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
U1242m CLIA Abc1,ABC-1,Abca1,ATP-binding cassette 1,ATP-binding cassette sub-family A member 1,ATP-binding cassette transporter 1,Mouse,Mus musculus 96T
20-372-60004 ATP-binding cassette - Mouse monoclonal anti-human ABCF_ antibody; ATP-binding cassette. sub-family F (GCN20). member 1. isoform CRA_a; ABC50 protein Monoclonal 0.1 mg
E1181h ELISA ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
E1181h ELISA kit ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
U1181h CLIA ABC transporter 9 protein,ABCB9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,hABCB9,Homo sapiens,Human,KIAA1520,TAPL,TAP-like protein 96T
U1181m CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181m ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
E1181m ELISA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Kiaa1520,mABCB9,Mouse,Mus musculus,TAPL,TAP-like protein 96T
U1181r CLIA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
E1181r ELISA ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
E1181r ELISA kit ABC transporter 9 protein,Abcb9,ATP-binding cassette sub-family B member 9,ATP-binding cassette transporter 9,Rat,Rattus norvegicus,TAPL,TAP-like protein 96T
EM635 ATP-binding cassette sub-family A member 7 Elisa Kit 96T
CG47 ATP-binding cassette sub-family B member 5 ABCB5 500
EH1420 ATP-binding cassette sub-family A member 1 Elisa Kit 96T
ABCC8_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family C member 8 96T
EM796 ATP-binding cassette sub-family G member 3 Elisa Kit 96T
ABCD2_RAT Rat ELISA Kit FOR ATP-binding cassette sub-family D member 2 96T
CG47 ATP-binding cassette sub-family B member 5 ABCB5 lmg
EH1095 ATP-binding cassette sub-family G member 2 Elisa Kit 96T
EH1708 ATP-binding cassette sub-family A member 7 Elisa Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur