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

 ABCG5_HUMAN             Reviewed;         651 AA.
Q9H222; Q2T9G2; Q96QZ2; Q96QZ3;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
31-JAN-2018, entry version 161.
RecName: Full=ATP-binding cassette sub-family G member 5;
AltName: Full=Sterolin-1;
Name=ABCG5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-604, FUNCTION, AND
TISSUE SPECIFICITY.
TISSUE=Liver;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS STSL HIS-389; HIS-419
AND PRO-419, VARIANT GLU-604, FUNCTION, AND TISSUE SPECIFICITY.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 (ISOFORM 1), VARIANTS STSL GLN-146;
HIS-389; PRO-419; HIS-419 AND SER-550, AND VARIANT GLU-604.
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).
[7]
REVIEW.
PubMed=11590207;
Schmitz G., Langmann T., Heimerl S.;
"Role of ABCG1 and other ABCG family members in lipid metabolism.";
J. Lipid Res. 42:1513-1520(2001).
[8]
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).
[9]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16893193; DOI=10.1021/bi0608055;
Wang Z., Stalcup L.D., Harvey B.J., Weber J., Chloupkova M.,
Dumont M.E., Dean M., Urbatsch I.L.;
"Purification and ATP hydrolysis of the putative cholesterol
transporters ABCG5 and ABCG8.";
Biochemistry 45:9929-9939(2006).
[10]
FUNCTION, SUBUNIT, GLYCOSYLATION, ENZYME REGULATION, AND MUTAGENESIS
OF 92-LYS-THR-93.
PubMed=20210363; DOI=10.1021/bi902064g;
Johnson B.J., Lee J.Y., Pickert A., Urbatsch I.L.;
"Bile acids stimulate ATP hydrolysis in the purified cholesterol
transporter ABCG5/G8.";
Biochemistry 49:3403-3411(2010).
[11] {ECO:0000244|PDB:5DO7}
X-RAY CRYSTALLOGRAPHY (3.93 ANGSTROMS) IN COMPLEX WITH ABCG8,
FUNCTION, ENZYME REGULATION, MUTAGENESIS OF TYR-432 AND ALA-540,
SUBUNIT, AND TOPOLOGY.
PubMed=27144356; DOI=10.1038/nature17666;
Lee J.Y., Kinch L.N., Borek D.M., Wang J., Wang J., Urbatsch I.L.,
Xie X.S., Grishin N.V., Cohen J.C., Otwinowski Z., Hobbs H.H.,
Rosenbaum D.M.;
"Crystal structure of the human sterol transporter ABCG5/ABCG8.";
Nature 533:561-564(2016).
[12]
VARIANT STSL LYS-437, AND VARIANTS VAL-523; TYR-600; GLU-604 AND
VAL-622.
PubMed=11668628; DOI=10.1002/humu.1206;
Hubacek J.A., Berge K.E., Cohen J.C., Hobbs H.H.;
"Mutations in ATP-cassette binding proteins G5 (ABCG5) and G8 (ABCG8)
causing sitosterolemia.";
Hum. Mutat. 18:359-360(2001).
[13]
CHARACTERIZATION OF VARIANTS STSL GLN-146; HIS-389; PRO-419; HIS-419
AND LYS-437, AND FUNCTION.
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).
-!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that
mediates Mg(2+)- and ATP-dependent sterol transport across the
cell membrane (PubMed:27144356). 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:11099417, PubMed:11138003,
PubMed:27144356, PubMed:15054092). Required for normal sterol
homeostasis (PubMed:11099417, PubMed:11138003, PubMed:15054092).
The heterodimer with ABCG8 has ATPase activity (PubMed:16893193,
PubMed:20210363, PubMed:27144356). {ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:15054092, ECO:0000269|PubMed:16893193,
ECO:0000269|PubMed:20210363, ECO:0000269|PubMed:27144356,
ECO:0000303|PubMed:11590207, ECO:0000305|PubMed:11099417}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q99PE8};
-!- ENZYME REGULATION: The ATPase activity of the heterodimer is
stimulated by cholate. Taurocholate, glycocholate,
taurochenodeoxycholate, glycochenodeoxycholate and
taurodeoxycholate also stimulate ATPase activity, but to a lower
degree. Glycodeoxycholate has no significant effect on ATPase
activity. ATPase activity is inhibited by vanadate and by
berillium fluoride. {ECO:0000269|PubMed:20210363,
ECO:0000269|PubMed:27144356}.
-!- SUBUNIT: Heterodimer with ABCG8. {ECO:0000269|PubMed:16893193,
ECO:0000269|PubMed:20210363, ECO:0000269|PubMed:27144356}.
-!- INTERACTION:
Q9H221:ABCG8; NbExp=2; IntAct=EBI-1761423, EBI-3908684;
Q9H221-1:ABCG8; NbExp=5; IntAct=EBI-16205983, EBI-16205990;
P16333:NCK1; NbExp=2; IntAct=EBI-1761423, EBI-389883;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16893193,
ECO:0000305|PubMed:27144356}; Multi-pass membrane protein
{ECO:0000269|PubMed:27144356}. Apical cell membrane
{ECO:0000269|PubMed:14504269}; Multi-pass membrane protein
{ECO:0000269|PubMed:27144356}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H222-1; Sequence=Displayed;
Name=2;
IsoId=Q9H222-2; Sequence=VSP_055770;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels
in the small intestine and colon. {ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11138003}.
-!- 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:0000250|UniProtKB:Q99PE8}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16893193,
ECO:0000269|PubMed:20210363}.
-!- DISEASE: Sitosterolemia (STSL) [MIM:210250]: Rare autosomal
recessive disorder characterized by increased intestinal
absorption of all sterols including cholesterol, plant and
shellfish sterols, and decreased biliary excretion of dietary
sterols into bile. Sitosterolemia patients have
hypercholesterolemia, very high levels of plant sterols in the
plasma, and frequently develop tendon and tuberous xanthomas,
accelerated atherosclerosis and premature coronary artery disease.
{ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628, ECO:0000269|PubMed:15054092}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9H222";
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EMBL; AF320293; AAG40003.1; -; mRNA.
EMBL; AF312715; AAG53099.1; -; mRNA.
EMBL; AC011242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00286.1; -; Genomic_DNA.
EMBL; BC111541; AAI11542.1; -; mRNA.
EMBL; AF404106; AAK85387.1; -; Genomic_DNA.
EMBL; AF404107; AAK85388.1; -; Genomic_DNA.
CCDS; CCDS1814.1; -. [Q9H222-1]
RefSeq; NP_071881.1; NM_022436.2. [Q9H222-1]
UniGene; Hs.132992; -.
PDB; 5DO7; X-ray; 3.93 A; A/C=1-651.
PDBsum; 5DO7; -.
ProteinModelPortal; Q9H222; -.
SMR; Q9H222; -.
BioGrid; 122124; 1.
DIP; DIP-42630N; -.
IntAct; Q9H222; 5.
MINT; MINT-2840498; -.
STRING; 9606.ENSP00000260645; -.
DrugBank; DB00973; Ezetimibe.
TCDB; 3.A.1.204.5; the atp-binding cassette (abc) superfamily.
iPTMnet; Q9H222; -.
PhosphoSitePlus; Q9H222; -.
BioMuta; ABCG5; -.
DMDM; 17432917; -.
PaxDb; Q9H222; -.
PRIDE; Q9H222; -.
Ensembl; ENST00000260645; ENSP00000260645; ENSG00000138075. [Q9H222-1]
GeneID; 64240; -.
KEGG; hsa:64240; -.
UCSC; uc002rtn.3; human. [Q9H222-1]
CTD; 64240; -.
DisGeNET; 64240; -.
EuPathDB; HostDB:ENSG00000138075.11; -.
GeneCards; ABCG5; -.
GeneReviews; ABCG5; -.
HGNC; HGNC:13886; ABCG5.
HPA; HPA016514; -.
MalaCards; ABCG5; -.
MIM; 210250; phenotype.
MIM; 605459; gene.
neXtProt; NX_Q9H222; -.
OpenTargets; ENSG00000138075; -.
Orphanet; 2882; Sitosterolemia.
PharmGKB; PA24411; -.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00870000136471; -.
HOGENOM; HOG000033763; -.
HOVERGEN; HBG050443; -.
InParanoid; Q9H222; -.
KO; K05683; -.
OMA; NAVNLFP; -.
OrthoDB; EOG091G0FOJ; -.
PhylomeDB; Q9H222; -.
TreeFam; TF105212; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
Reactome; R-HSA-5679090; Defective ABCG8 causes gallbladder disease 4 and sitosterolemia.
Reactome; R-HSA-5679096; Defective ABCG5 causes sitosterolemia.
SIGNOR; Q9H222; -.
GeneWiki; ABCG5; -.
GenomeRNAi; 64240; -.
PRO; PR:Q9H222; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138075; -.
CleanEx; HS_ABCG5; -.
ExpressionAtlas; Q9H222; baseline and differential.
Genevisible; Q9H222; HS.
GO; GO:0016324; C:apical plasma membrane; IMP:BHF-UCL.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IDA:UniProtKB.
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; IPI:BHF-UCL.
GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central.
GO; GO:0007588; P:excretion; IGI:BHF-UCL.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; IMP:BHF-UCL.
GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; IMP:BHF-UCL.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disease mutation; Glycoprotein; Lipid transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 651 ATP-binding cassette sub-family G member
5.
/FTId=PRO_0000093393.
TOPO_DOM 1 383 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 384 404 Helical; Name=1.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 405 421 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 422 442 Helical; Name=2.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 443 467 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 468 489 Helical; Name=3.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 490 500 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 501 521 Helical; Name=4.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 522 528 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 529 549 Helical; Name=5.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 550 623 Extracellular.
{ECO:0000269|PubMed:27144356}.
TRANSMEM 624 644 Helical; Name=6.
{ECO:0000269|PubMed:27144356}.
TOPO_DOM 645 651 Cytoplasmic.
{ECO:0000269|PubMed:27144356}.
DOMAIN 52 293 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 388 645 ABC transmembrane type-2.
NP_BIND 86 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 395 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055770.
VARIANT 50 50 R -> C (in dbSNP:rs6756629).
/FTId=VAR_048142.
VARIANT 146 146 E -> Q (in STSL; decreased maturation of
glycan chains; dbSNP:rs758551848).
{ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012244.
VARIANT 389 389 R -> H (in STSL; loss of normal
maturation of glycan chains;
dbSNP:rs119480069).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012245.
VARIANT 419 419 R -> H (in STSL; loss of normal
maturation of glycan chains;
dbSNP:rs119479067).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012246.
VARIANT 419 419 R -> P (in STSL; strongly decreased
maturation of glycan chains;
dbSNP:rs119479067).
{ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_012247.
VARIANT 437 437 N -> K (in STSL; loss of normal
maturation of glycan chains;
dbSNP:rs575266356).
{ECO:0000269|PubMed:11668628,
ECO:0000269|PubMed:15054092}.
/FTId=VAR_020781.
VARIANT 517 517 T -> S (in dbSNP:rs17031672).
/FTId=VAR_033457.
VARIANT 523 523 I -> V (in dbSNP:rs140899003).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020782.
VARIANT 550 550 R -> S (in STSL).
{ECO:0000269|PubMed:11452359}.
/FTId=VAR_012248.
VARIANT 600 600 C -> Y (in dbSNP:rs779109455).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020783.
VARIANT 604 604 Q -> E (in dbSNP:rs6720173).
{ECO:0000269|PubMed:11099417,
ECO:0000269|PubMed:11138003,
ECO:0000269|PubMed:11452359,
ECO:0000269|PubMed:11668628}.
/FTId=VAR_012249.
VARIANT 622 622 M -> V (in dbSNP:rs140374206).
{ECO:0000269|PubMed:11668628}.
/FTId=VAR_020784.
MUTAGEN 92 93 KT->RA: Abolishes increase of the very
low basal ATPase activity by cholate.
{ECO:0000269|PubMed:20210363}.
MUTAGEN 432 432 Y->A: Strongly decreases cholesterol
secretion into bile.
{ECO:0000269|PubMed:27144356}.
MUTAGEN 540 540 A->F: Strongly decreases cholesterol
secretion into bile.
{ECO:0000269|PubMed:27144356}.
SEQUENCE 651 AA; 72504 MW; 950BABFCBB6A1536 CRC64;
MGDLSSLTPG GSMGLQVNRG SQSSLEGAPA TAPEPHSLGI LHASYSVSHR VRPWWDITSC
RQQWTRQILK DVSLYVESGQ IMCILGSSGS GKTTLLDAMS GRLGRAGTFL GEVYVNGRAL
RREQFQDCFS YVLQSDTLLS SLTVRETLHY TALLAIRRGN PGSFQKKVEA VMAELSLSHV
ADRLIGNYSL GGISTGERRR VSIAAQLLQD PKVMLFDEPT TGLDCMTANQ IVVLLVELAR
RNRIVVLTIH QPRSELFQLF DKIAILSFGE LIFCGTPAEM LDFFNDCGYP CPEHSNPFDF
YMDLTSVDTQ SKEREIETSK RVQMIESAYK KSAICHKTLK NIERMKHLKT LPMVPFKTKD
SPGVFSKLGV LLRRVTRNLV RNKLAVITRL LQNLIMGLFL LFFVLRVRSN VLKGAIQDRV
GLLYQFVGAT PYTGMLNAVN LFPVLRAVSD QESQDGLYQK WQMMLAYALH VLPFSVVATM
IFSSVCYWTL GLHPEVARFG YFSAALLAPH LIGEFLTLVL LGIVQNPNIV NSVVALLSIA
GVLVGSGFLR NIQEMPIPFK IISYFTFQKY CSEILVVNEF YGLNFTCGSS NVSVTTNPMC
AFTQGIQFIE KTCPGATSRF TMNFLILYSF IPALVILGIV VFKIRDHLIS R


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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


 

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