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Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 3) (EC 3.6.3.44) (P-glycoprotein 3)

 MDR3_HUMAN              Reviewed;        1286 AA.
P21439; A0A2V7; A4D1D3; A4D1D4; A4D1D5; D6W5P3; D6W5P4; Q14813;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
22-NOV-2017, entry version 183.
RecName: Full=Phosphatidylcholine translocator ABCB4 {ECO:0000305};
AltName: Full=ATP-binding cassette sub-family B member 4 {ECO:0000312|HGNC:HGNC:45};
AltName: Full=Multidrug resistance protein 3 {ECO:0000303|PubMed:2892668};
EC=3.6.3.44;
AltName: Full=P-glycoprotein 3 {ECO:0000250|UniProtKB:Q08201};
Name=ABCB4 {ECO:0000312|HGNC:HGNC:45};
Synonyms=MDR3 {ECO:0000303|PubMed:2892668}, PGY3;
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 2).
PubMed=2906314; DOI=10.1016/0378-1119(88)90057-1;
van der Bliek A.M., Kooiman P.M., Schneider C., Borst P.;
"Sequence of mdr3 cDNA encoding a human P-glycoprotein.";
Gene 71:401-411(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GBD1 ASP-528, AND VARIANTS
VAL-238; VAL-263; GLN-590; ASN-651; GLY-652 AND GLN-788.
NIEHS SNPs program;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-72 (ISOFORM 1).
TISSUE=Liver;
PubMed=7893760; DOI=10.1016/0167-4781(94)00214-N;
Smit J.J., Mol C.A., van Deemter L., Wagenaar E., Schinkel A.H.,
Borst P.;
"Characterization of the promoter region of the human MDR3 P-
glycoprotein gene.";
Biochim. Biophys. Acta 1261:44-56(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 856-1286 (ISOFORM 1), AND ALTERNATIVE
SPLICING.
PubMed=2892668;
van der Bliek A.M., Baas F., ten Houte de Lange T., Kooiman P.M.,
van der Velde-Koerts T., Borst P.;
"The human mdr3 gene encodes a novel P-glycoprotein homologue and
gives rise to alternatively spliced mRNAs in liver.";
EMBO J. 6:3325-3331(1987).
[8]
GENE STRUCTURE.
PubMed=2002063;
Lincke C.R., Smit J.J.M., van der Velde-Koerts T., Borst P.;
"Structure of the human MDR3 gene and physical mapping of the human
MDR locus.";
J. Biol. Chem. 266:5303-5310(1991).
[9]
FUNCTION.
PubMed=7957936; DOI=10.1016/0014-5793(94)01135-4;
Smith A.J., Timmermans-Hereijgers J.L., Roelofsen B., Wirtz K.W.,
van Blitterswijk W.J., Smit J.J., Schinkel A.H., Borst P.;
"The human MDR3 P-glycoprotein promotes translocation of
phosphatidylcholine through the plasma membrane of fibroblasts from
transgenic mice.";
FEBS Lett. 354:263-266(1994).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8898203; DOI=10.1016/S0092-8674(00)81370-7;
van Helvoort A., Smith A.J., Sprong H., Fritzsche I., Schinkel A.H.,
Borst P., van Meer G.;
"MDR1 P-glycoprotein is a lipid translocase of broad specificity,
while MDR3 P-glycoprotein specifically translocates
phosphatidylcholine.";
Cell 87:507-517(1996).
[11]
FUNCTION.
PubMed=9366571; DOI=10.1172/JCI119799;
Crawford A.R., Smith A.J., Hatch V.C., Oude Elferink R.P., Borst P.,
Crawford J.M.;
"Hepatic secretion of phospholipid vesicles in the mouse critically
depends on mdr2 or MDR3 P-glycoprotein expression. Visualization by
electron microscopy.";
J. Clin. Invest. 100:2562-2567(1997).
[12]
INVOLVEMENT IN PFIC3.
PubMed=9419367; DOI=10.1073/pnas.95.1.282;
de Vree J.M.L., Jacquemin E., Sturm E., Cresteil D., Bosma P.J.,
Aten J., Deleuze J.-F., Desrochers M., Burdelski M., Bernard O.,
Oude Elferink R.P.J., Hadchouel M.;
"Mutations in the MDR3 gene cause progressive familial intrahepatic
cholestasis.";
Proc. Natl. Acad. Sci. U.S.A. 95:282-287(1998).
[13]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15258199; DOI=10.1194/jlr.M400132-JLR200;
Shoda J., Inada Y., Tsuji A., Kusama H., Ueda T., Ikegami T.,
Suzuki H., Sugiyama Y., Cohen D.E., Tanaka N.;
"Bezafibrate stimulates canalicular localization of NBD-labeled PC in
HepG2 cells by PPARalpha-mediated redistribution of ABCB4.";
J. Lipid Res. 45:1813-1825(2004).
[14]
FUNCTION, ENZYME REGULATION, GLYCOSYLATION, AND MUTAGENESIS OF LYS-435
AND LYS-1075.
PubMed=17523162; DOI=10.1002/hep.21591;
Morita S.Y., Kobayashi A., Takanezawa Y., Kioka N., Handa T., Arai H.,
Matsuo M., Ueda K.;
"Bile salt-dependent efflux of cellular phospholipids mediated by ATP
binding cassette protein B4.";
Hepatology 46:188-199(2007).
[15]
INTERACTION WITH RACK1, AND SUBCELLULAR LOCATION.
PubMed=19674157; DOI=10.1111/j.1872-034X.2009.00544.x;
Ikebuchi Y., Takada T., Ito K., Yoshikado T., Anzai N., Kanai Y.,
Suzuki H.;
"Receptor for activated C-kinase 1 regulates the cellular localization
and function of ABCB4.";
Hepatol. Res. 39:1091-1107(2009).
[16]
FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=21820390; DOI=10.1053/j.gastro.2011.07.042;
Groen A., Romero M.R., Kunne C., Hoosdally S.J., Dixon P.H.,
Wooding C., Williamson C., Seppen J., Van den Oever K., Mok K.S.,
Paulusma C.C., Linton K.J., Oude Elferink R.P.;
"Complementary functions of the flippase ATP8B1 and the floppase ABCB4
in maintaining canalicular membrane integrity.";
Gastroenterology 141:1927-1937(2011).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=23468132; DOI=10.1194/jlr.M032425;
Morita S.Y., Tsuda T., Horikami M., Teraoka R., Kitagawa S.,
Terada T.;
"Bile salt-stimulated phospholipid efflux mediated by ABCB4 localized
in nonraft membranes.";
J. Lipid Res. 54:1221-1230(2013).
[18]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=24122873; DOI=10.1002/hep.26894;
Ghonem N.S., Ananthanarayanan M., Soroka C.J., Boyer J.L.;
"Peroxisome proliferator-activated receptor alpha activates human
multidrug resistance transporter 3/ATP-binding cassette protein
subfamily B4 transcription and increases rat biliary
phosphatidylcholine secretion.";
Hepatology 59:1030-1042(2014).
[19]
FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS PFIC3
VAL-286 AND PHE-320, AND MUTAGENESIS OF ALA-953.
PubMed=24806754; DOI=10.1002/hep.26970;
Andress E.J., Nicolaou M., Romero M.R., Naik S., Dixon P.H.,
Williamson C., Linton K.J.;
"Molecular mechanistic explanation for the spectrum of cholestatic
disease caused by the S320F variant of ABCB4.";
Hepatology 59:1921-1931(2014).
[20]
VARIANT ICP3 ASP-546, AND CHARACTERIZATION OF VARIANT ICP3 ASP-546.
PubMed=10767346; DOI=10.1093/hmg/9.8.1209;
Dixon P.H., Weerasekera N., Linton K.J., Donaldson O., Chambers J.,
Egginton E., Weaver J., Nelson-Piercy C., de Swiet M., Warnes G.,
Elias E., Higgins C.F., Johnston D.G., McCarthy M.I., Williamson C.;
"Heterozygous MDR3 missense mutation associated with intrahepatic
cholestasis of pregnancy: evidence for a defect in protein
trafficking.";
Hum. Mol. Genet. 9:1209-1217(2000).
[21]
VARIANTS PFIC3 ARG-138; ILE-346; GLY-395; ALA-424; MET-425; PHE-541;
ARG-556; GLY-564; SER-711 AND SER-983, AND VARIANT GLY-652.
PubMed=11313315; DOI=10.1053/gast.2001.23984;
Jacquemin E., De Vree J.M.L., Cresteil D., Sokal E.M., Sturm E.,
Dumont M., Scheffer G.L., Paul M., Burdelski M., Bosma P.J.,
Bernard O., Hadchouel M., Elferink R.P.;
"The wide spectrum of multidrug resistance 3 deficiency: from neonatal
cholestasis to cirrhosis of adulthood.";
Gastroenterology 120:1448-1458(2001).
[22]
VARIANTS GBD1 PHE-320 AND SER-1168, AND VARIANT ALA-175.
PubMed=11313316; DOI=10.1053/gast.2001.23947;
Rosmorduc O., Hermelin B., Poupon R.;
"MDR3 gene defect in adults with symptomatic intrahepatic and
gallbladder cholesterol cholelithiasis.";
Gastroenterology 120:1459-1467(2001).
[23]
VARIANT PFIC3 ASP-535.
PubMed=12671900; DOI=10.1053/gast.2003.50144;
Lucena J.-F., Herrero J.I., Quiroga J., Sangro B.,
Garcia-Foncillas J., Zabalegui N., Sola J., Herraiz M., Medina J.F.,
Prieto J.;
"A multidrug resistance 3 gene mutation causing cholelithiasis,
cholestasis of pregnancy, and adulthood biliary cirrhosis.";
Gastroenterology 124:1037-1042(2003).
[24]
VARIANTS GBD1 ILE-165; THR-301; PHE-320; ASP-528; GLN-591 AND
SER-1168, AND VARIANTS ALA-175; GLN-590; GLY-652; SER-742; GLN-788 AND
THR-934.
PubMed=12891548; DOI=10.1016/S0016-5085(03)00898-9;
Rosmorduc O., Hermelin B., Boelle P.Y., Parc R., Taboury J.,
Poupon R.;
"ABCB4 gene mutation-associated cholelithiasis in adults.";
Gastroenterology 125:452-459(2003).
[25]
VARIANT ICP3 LYS-150, AND VARIANT GLY-652.
PubMed=12746424; DOI=10.1136/jmg.40.5.e70;
Muellenbach R., Linton K.J., Wiltshire S., Weerasekera N.,
Chambers J., Elias E., Higgins C.F., Johnston D.G., McCarthy M.I.,
Williamson C.;
"ABCB4 gene sequence variation in women with intrahepatic cholestasis
of pregnancy.";
J. Med. Genet. 40:E70-E70(2003).
[26]
VARIANTS ALA-175; GLY-652 AND MET-775, AND VARIANTS ICP3 PHE-320;
ASP-528 AND GLU-762.
PubMed=15077010; DOI=10.1097/00008571-200402000-00003;
Pauli-Magnus C., Lang T., Meier Y., Zodan-Marin T., Jung D.,
Breymann C., Zimmermann R., Kenngott S., Beuers U., Reichel C.,
Kerb R., Penger A., Meier P.J., Kullak-Ublick G.A.;
"Sequence analysis of bile salt export pump (ABCB11) and multidrug
resistance p-glycoprotein 3 (ABCB4, MDR3) in patients with
intrahepatic cholestasis of pregnancy.";
Pharmacogenetics 14:91-102(2004).
[27]
VARIANTS GLU-87; SER-95; ALA-175; VAL-367; GLY-450; GLN-590 AND
GLY-652.
PubMed=16763017; DOI=10.1124/dmd.105.008854;
Lang T., Haberl M., Jung D., Drescher A., Schlagenhaufer R., Keil A.,
Mornhinweg E., Stieger B., Kullak-Ublick G.A., Kerb R.;
"Genetic variability, haplotype structures, and ethnic diversity of
hepatic transporters MDR3 (ABCB4) and bile salt export pump
(ABCB11).";
Drug Metab. Dispos. 34:1582-1599(2006).
[28]
VARIANTS PFIC3 GLU-126; PRO-250; VAL-286; PHE-320; LEU-357; VAL-364;
HIS-403; ALA-475; THR-511; LYS-558; ALA-593; VAL-630; PRO-701;
ILE-715; GLU-723; THR-726; VAL-737; ASP-840; SER-954 AND THR-1193, AND
VARIANTS ALA-175; GLN-590 AND MET-775.
PubMed=17726488; DOI=10.1038/sj.ejhg.5201908;
Degiorgio D., Colombo C., Seia M., Porcaro L., Costantino L.,
Zazzeron L., Bordo D., Coviello D.A.;
"Molecular characterization and structural implications of 25 new
ABCB4 mutations in progressive familial intrahepatic cholestasis type
3 (PFIC3).";
Eur. J. Hum. Genet. 15:1230-1238(2007).
[29]
VARIANTS ALA-175; GLN-590; GLY-652; LEU-764 AND GLN-1082.
PubMed=17264802; DOI=10.1097/01.fpc.0000230418.28091.76;
Lang C., Meier Y., Stieger B., Beuers U., Lang T., Kerb R.,
Kullak-Ublick G.A., Meier P.J., Pauli-Magnus C.;
"Mutations and polymorphisms in the bile salt export pump and the
multidrug resistance protein 3 associated with drug-induced liver
injury.";
Pharmacogenet. Genomics 17:47-60(2007).
[30]
VARIANTS GLN-590 AND GLY-652.
PubMed=19261551; DOI=10.1016/j.dld.2008.12.101;
Tavian D., Degiorgio D., Roncaglia N., Vergani P., Cameroni I.,
Colombo R., Coviello D.A.;
"A new splicing site mutation of the ABCB4 gene in intrahepatic
cholestasis of pregnancy with raised serum gamma-GT.";
Dig. Liver Dis. 41:671-675(2009).
[31]
VARIANTS PFIC3 ARG-70; VAL-73; PHE-320 AND HIS-403, AND VARIANT
GLY-652.
PubMed=21119540; DOI=10.1097/MPG.0b013e3181f50363;
Colombo C., Vajro P., Degiorgio D., Coviello D.A., Costantino L.,
Tornillo L., Motta V., Consonni D., Maggiore G., Balli F., Berardi S.,
Calacoci M., Castellano E., Marazzi M.G., Gaslini G., D'Antiga L.,
Ferretti E., Giannini A., Indolfi G., Iorio R., Martelossi S.,
Moretti C., Nebbia G., Oliveri F., Poggiani C., Raggi M., Riva S.,
Sciveres M., Torre G., Zancan L.;
"Clinical features and genotype-phenotype correlations in children
with progressive familial intrahepatic cholestasis type 3 related to
ABCB4 mutations.";
J. Pediatr. Gastroenterol. Nutr. 52:73-83(2011).
[32]
VARIANTS GBD1 MET-34; GLY-47; VAL-286 AND ASP-528, AND VARIANTS
GLN-47; ALA-175; PHE-320; GLN-406; MET-775 AND THR-964.
PubMed=22331132; DOI=10.1007/s00428-012-1202-6;
Wendum D., Barbu V., Rosmorduc O., Arrive L., Flejou J.F., Poupon R.;
"Aspects of liver pathology in adult patients with MDR3/ABCB4 gene
mutations.";
Virchows Arch. 460:291-298(2012).
[33]
VARIANTS GBD1 GLY-47; HIS-71; VAL-73; CYS-78; PHE-99; SER-124;
SER-154; ILE-165; VAL-286; THR-301; PHE-320; GLY-406; SER-510;
THR-511; LYS-513; ASP-528; PHE-541; HIS-545; HIS-549; THR-589;
GLN-591; MET-593; LYS-647; LEU-726; LEU-729; VAL-975 AND TRP-1084, AND
VARIANTS ALA-175; GLN-590; GLN-788 AND THR-934.
PubMed=23533021; DOI=10.1002/hep.26424;
Poupon R., Rosmorduc O., Boelle P.Y., Chretien Y., Corpechot C.,
Chazouilleres O., Housset C., Barbu V.;
"Genotype-phenotype relationships in the low-phospholipid-associated
cholelithiasis syndrome: a study of 156 consecutive patients.";
Hepatology 58:1105-1110(2013).
[34]
VARIANT PFIC3 ARG-481, CHARACTERIZATION OF VARIANTS PFIC3 HIS-403 AND
ARG-481, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24045840; DOI=10.1038/ejhg.2013.214;
Degiorgio D., Corsetto P.A., Rizzo A.M., Colombo C., Seia M.,
Costantino L., Montorfano G., Tomaiuolo R., Bordo D., Sansanelli S.,
Li M., Tavian D., Rastaldi M.P., Coviello D.A.;
"Two ABCB4 point mutations of strategic NBD-motifs do not prevent
protein targeting to the plasma membrane but promote MDR3
dysfunction.";
Eur. J. Hum. Genet. 22:633-639(2014).
[35]
VARIANTS GBD1 MET-34 AND GLY-47, CHARACTERIZATION OF VARIANTS GBD1
MET-34 AND GLY-47, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
THR-34, GLYCOSYLATION, MUTAGENESIS OF THR-34; THR-44 AND SER-49, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=24723470; DOI=10.1002/hep.27170;
Gautherot J., Delautier D., Maubert M.A., Ait-Slimane T., Bolbach G.,
Delaunay J.L., Durand-Schneider A.M., Firrincieli D., Barbu V.,
Chignard N., Housset C., Maurice M., Falguieres T.;
"Phosphorylation of ABCB4 impacts its function: insights from disease-
causing mutations.";
Hepatology 60:610-621(2014).
[36]
VARIANTS PFIC3 ARG-68; MET-201; HIS-459; LEU-479; PRO-978 AND
LYS-1125, CHARACTERIZATION OF VARIANTS PFIC3 ARG-68; MET-201; HIS-459;
LEU-479; PRO-978 AND LYS-1125, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24594635; DOI=10.1136/gutjnl-2014-306896;
Gordo-Gilart R., Andueza S., Hierro L., Martinez-Fernandez P.,
D'Agostino D., Jara P., Alvarez L.;
"Functional analysis of ABCB4 mutations relates clinical outcomes of
progressive familial intrahepatic cholestasis type 3 to the degree of
MDR3 floppase activity.";
Gut 64:147-155(2015).
[37]
VARIANTS GBD1 ARG-536; LEU-726; LEU-1183 AND SER-1185,
CHARACTERIZATION OF VARIANTS GBD1 ARG-536; LEU-726; LEU-1183 AND
SER-1185, CHARACTERIZATION OF VARIANT PFIC3 ASP-535, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=28012258; DOI=10.1002/hep.28929;
Delaunay J.L., Bruneau A., Hoffmann B., Durand-Schneider A.M.,
Barbu V., Jacquemin E., Maurice M., Housset C., Callebaut I.,
Ait-Slimane T.;
"Functional defect of variants in the adenosine triphosphate-binding
sites of ABCB4 and their rescue by the cystic fibrosis transmembrane
conductance regulator potentiator, ivacaftor (VX-770).";
Hepatology 65:560-570(2017).
-!- FUNCTION: Energy-dependent phospholipid efflux translocator that
acts as a positive regulator of biliary lipid secretion. Functions
as a floppase that translocates specifically phosphatidylcholine
(PC) from the inner to the outer leaflet of the canalicular
membrane bilayer into the canaliculi of hepatocytes. Translocation
of PC makes the biliary phospholipids available for extraction
into the canaliculi lumen by bile salt mixed micelles and
therefore protects the biliary tree from the detergent activity of
bile salts (PubMed:7957936, PubMed:8898203, PubMed:9366571,
PubMed:17523162, PubMed:23468132, PubMed:24806754,
PubMed:24723470, PubMed:24594635, PubMed:21820390). Plays a role
in the recruitment of phosphatidylcholine (PC),
phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to
nonraft membranes and to fu rther enrichment of SM and cholesterol
in raft membranes in hepatocytes (PubMed:23468132). Required for
proper phospholipid bile formation (By similarity). Indirectly
involved in cholesterol efflux activity from hepatocytes into the
canalicular lumen in the presence of bile salts in an ATP-
dependent manner (PubMed:24045840). Promotes biliary phospholipid
secretion as canaliculi-containing vesicles from the canalicular
plasma membrane (PubMed:9366571, PubMed:28012258). In cooperation
with ATP8B1, functions to protect hepatocytes from the deleterious
detergent activity of bile salts (PubMed:21820390). Does not
confer multidrug resistance (By similarity).
{ECO:0000250|UniProtKB:P21440, ECO:0000269|PubMed:17523162,
ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:23468132,
ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24594635,
ECO:0000269|PubMed:24723470, ECO:0000269|PubMed:24806754,
ECO:0000269|PubMed:28012258, ECO:0000269|PubMed:7957936,
ECO:0000269|PubMed:8898203, ECO:0000269|PubMed:9366571}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + xenobiotic(In) = ADP + phosphate
+ xenobiotic(Out).
-!- ENZYME REGULATION: Translocation activity is inhibited by the
ATPase inhibitor vanadate and the calcium channel blocker
verapamil (PubMed:17523162, PubMed:23468132). Translocation
activity is enhanced by the addition of the bile salt taurocholate
(PubMed:17523162, PubMed:23468132). {ECO:0000269|PubMed:17523162,
ECO:0000269|PubMed:23468132}.
-!- SUBUNIT: May interact with RACK1 (PubMed:19674157). Interacts with
HAX1 (By similarity). {ECO:0000250|UniProtKB:Q08201,
ECO:0000269|PubMed:19674157}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23468132,
ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24806754,
ECO:0000269|PubMed:28012258}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane
{ECO:0000269|PubMed:15258199, ECO:0000269|PubMed:19674157,
ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:24122873,
ECO:0000269|PubMed:24594635, ECO:0000269|PubMed:24723470,
ECO:0000269|PubMed:8898203}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441}. Membrane raft
{ECO:0000269|PubMed:23468132}. Cytoplasm
{ECO:0000269|PubMed:24045840}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000250|UniProtKB:Q08201}. Note=Localized at
the apical canalicular membrane of the epithelial cells lining the
lumen of the bile canaliculi and biliary ductules (By similarity).
Transported from the Golgi to the apical bile canalicular membrane
in a RACK1-dependent manner (PubMed:19674157). Redistributed into
pseudocanaliculi formed between cells in a bezafibrate- or PPARA-
dependent manner (PubMed:15258199). Localized preferentially in
lipid nonraft domains of canalicular plasma membranes
(PubMed:23468132). {ECO:0000250|UniProtKB:P21440,
ECO:0000269|PubMed:15258199, ECO:0000269|PubMed:19674157,
ECO:0000269|PubMed:23468132}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P21439-1; Sequence=Displayed;
Name=2;
IsoId=P21439-2; Sequence=VSP_023263;
Name=3;
IsoId=P21439-3; Sequence=VSP_046258, VSP_023263;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- INDUCTION: Up-regulated by PPARA (PubMed:24122873). Up-regulated
by compounds that cause peroxisome proliferation, such as
fenofibrate (at protein level). Up-regulated by bezafibrate
(PubMed:15258199). Up-regulated by compounds that cause peroxisome
proliferation, such as fenofibrate, bezafibrate and gemfibrozil
(PubMed:24122873). {ECO:0000269|PubMed:15258199,
ECO:0000269|PubMed:24122873}.
-!- PTM: Phosphorylated (PubMed:24723470). Phosphorylation on Thr-34
is required for PC efflux activity. Phosphorylation occurs on
serine and threonine residues in a protein kinase A- or C-
dependent manner (PubMed:24723470). May be phosphorylated on Thr-
44 and Ser-49 (PubMed:24723470). {ECO:0000269|PubMed:24723470}.
-!- PTM: Glycosylated (PubMed:17523162, PubMed:24723470,
PubMed:21820390). {ECO:0000269|PubMed:17523162,
ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:24723470}.
-!- DISEASE: Cholestasis, progressive familial intrahepatic, 3 (PFIC3)
[MIM:602347]: A disorder characterized by early onset of
cholestasis that progresses to hepatic fibrosis, cirrhosis, and
end-stage liver disease before adulthood.
{ECO:0000269|PubMed:11313315, ECO:0000269|PubMed:12671900,
ECO:0000269|PubMed:17726488, ECO:0000269|PubMed:21119540,
ECO:0000269|PubMed:24045840, ECO:0000269|PubMed:24594635,
ECO:0000269|PubMed:24806754, ECO:0000269|PubMed:28012258,
ECO:0000269|PubMed:9419367}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cholestasis of pregnancy, intrahepatic 3 (ICP3)
[MIM:614972]: A liver disorder of pregnancy. It presents during
the second or, more commonly, the third trimester of pregnancy
with intense pruritus which becomes more severe with advancing
gestation and cholestasis. It causes fetal distress, spontaneous
premature delivery and intrauterine death. Patients have
spontaneous and progressive disappearance of cholestasis after
delivery. Cholestasis results from abnormal biliary transport from
the liver into the small intestine. {ECO:0000269|PubMed:10767346,
ECO:0000269|PubMed:12746424, ECO:0000269|PubMed:15077010}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Gallbladder disease 1 (GBD1) [MIM:600803]: One of the
major digestive diseases. Gallstones composed of cholesterol
(cholelithiasis) are the common manifestations in western
countries. Most people with gallstones, however, remain
asymptomatic through their lifetimes.
{ECO:0000269|PubMed:11313316, ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:22331132, ECO:0000269|PubMed:23533021,
ECO:0000269|PubMed:24723470, ECO:0000269|PubMed:28012258,
ECO:0000269|Ref.2}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA84542.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/abcb4/";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P21439";
-----------------------------------------------------------------------
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EMBL; M23234; AAA36207.1; -; mRNA.
EMBL; EF034088; ABJ53424.1; -; Genomic_DNA.
EMBL; AC005045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236949; EAL24174.1; -; Genomic_DNA.
EMBL; CH236949; EAL24175.1; -; Genomic_DNA.
EMBL; CH236949; EAL24176.1; -; Genomic_DNA.
EMBL; CH471091; EAW76946.1; -; Genomic_DNA.
EMBL; CH471091; EAW76947.1; -; Genomic_DNA.
EMBL; CH471091; EAW76948.1; -; Genomic_DNA.
EMBL; CH471091; EAW76950.1; -; Genomic_DNA.
EMBL; CH471091; EAW76951.1; -; Genomic_DNA.
EMBL; CH471091; EAW76952.1; -; Genomic_DNA.
EMBL; Z35284; CAA84542.1; ALT_SEQ; mRNA.
EMBL; X06181; CAA29547.1; -; mRNA.
CCDS; CCDS5605.1; -. [P21439-2]
CCDS; CCDS5606.1; -. [P21439-1]
CCDS; CCDS5607.1; -. [P21439-3]
PIR; JS0051; DVHU3.
RefSeq; NP_000434.1; NM_000443.3. [P21439-2]
RefSeq; NP_061337.1; NM_018849.2. [P21439-1]
RefSeq; NP_061338.1; NM_018850.2. [P21439-3]
RefSeq; XP_011514615.1; XM_011516313.2. [P21439-3]
UniGene; Hs.654403; -.
ProteinModelPortal; P21439; -.
SMR; P21439; -.
BioGrid; 111263; 2.
IntAct; P21439; 3.
STRING; 9606.ENSP00000265723; -.
ChEMBL; CHEMBL1743129; -.
DrugBank; DB01394; Colchicine.
DrugBank; DB06414; Etravirine.
DrugBank; DB06207; Silodosin.
SwissLipids; SLP:000000384; -.
TCDB; 3.A.1.201.3; the atp-binding cassette (abc) superfamily.
iPTMnet; P21439; -.
PhosphoSitePlus; P21439; -.
BioMuta; ABCB4; -.
DMDM; 126302568; -.
MaxQB; P21439; -.
PaxDb; P21439; -.
PeptideAtlas; P21439; -.
PRIDE; P21439; -.
Ensembl; ENST00000265723; ENSP00000265723; ENSG00000005471. [P21439-1]
Ensembl; ENST00000358400; ENSP00000351172; ENSG00000005471. [P21439-3]
Ensembl; ENST00000359206; ENSP00000352135; ENSG00000005471. [P21439-2]
Ensembl; ENST00000453593; ENSP00000392983; ENSG00000005471. [P21439-3]
GeneID; 5244; -.
KEGG; hsa:5244; -.
UCSC; uc003uiv.2; human. [P21439-1]
CTD; 5244; -.
DisGeNET; 5244; -.
EuPathDB; HostDB:ENSG00000005471.15; -.
GeneCards; ABCB4; -.
HGNC; HGNC:45; ABCB4.
HPA; HPA049395; -.
HPA; HPA053288; -.
MalaCards; ABCB4; -.
MIM; 171060; gene.
MIM; 600803; phenotype.
MIM; 602347; phenotype.
MIM; 614972; phenotype.
neXtProt; NX_P21439; -.
OpenTargets; ENSG00000005471; -.
Orphanet; 69665; Intrahepatic cholestasis of pregnancy.
Orphanet; 69663; Low phospholipid associated cholelithiasis.
Orphanet; 79305; Progressive familial intrahepatic cholestasis type 3.
PharmGKB; PA268; -.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00530000062896; -.
HOVERGEN; HBG080809; -.
InParanoid; P21439; -.
KO; K05659; -.
OMA; GSAKTME; -.
OrthoDB; EOG091G0HVA; -.
PhylomeDB; P21439; -.
TreeFam; TF105193; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5678771; Defective ABCB4 causes progressive familial intrahepatic cholestasis 3, intrahepatic cholestasis of pregnancy 3 and gallbladder disease 1.
GeneWiki; ABCB4; -.
GenomeRNAi; 5244; -.
PRO; PR:P21439; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000005471; -.
CleanEx; HS_ABCB4; -.
ExpressionAtlas; P21439; baseline and differential.
Genevisible; P21439; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0046581; C:intercellular canaliculus; IEA:Ensembl.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0008525; F:phosphatidylcholine transporter activity; IDA:UniProtKB.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; IDA:UniProtKB.
GO; GO:0005548; F:phospholipid transporter activity; TAS:Reactome.
GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IEA:UniProtKB-EC.
GO; GO:0032782; P:bile acid secretion; ISS:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0033231; P:carbohydrate export; IEA:Ensembl.
GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:1903413; P:cellular response to bile acid; IDA:UniProtKB.
GO; GO:1905231; P:cellular response to borneol; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071217; P:cellular response to external biotic stimulus; IEA:Ensembl.
GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
GO; GO:0036146; P:cellular response to mycotoxin; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0043215; P:daunorubicin transport; IEA:Ensembl.
GO; GO:0046618; P:drug export; IEA:Ensembl.
GO; GO:1990962; P:drug transport across blood-brain barrier; IEA:Ensembl.
GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl.
GO; GO:0009914; P:hormone transport; IEA:Ensembl.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0055088; P:lipid homeostasis; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:UniProtKB.
GO; GO:0061092; P:positive regulation of phospholipid translocation; IDA:UniProtKB.
GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:UniProtKB.
GO; GO:2001025; P:positive regulation of response to drug; IEA:Ensembl.
GO; GO:1904478; P:regulation of intestinal absorption; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0097327; P:response to antineoplastic agent; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:1905233; P:response to codeine; IEA:Ensembl.
GO; GO:1905237; P:response to cyclosporin A; IEA:Ensembl.
GO; GO:0042493; P:response to drug; TAS:ProtInc.
GO; GO:1901557; P:response to fenofibrate; ISS:UniProtKB.
GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:1905235; P:response to quercetin; IEA:Ensembl.
GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:ProtInc.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030275; MDR3.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24221:SF241; PTHR24221:SF241; 2.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Disease mutation; Glycoprotein;
Hydrolase; Intrahepatic cholestasis; Lipid transport; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1286 Phosphatidylcholine translocator ABCB4.
/FTId=PRO_0000093333.
TOPO_DOM 1 50 Cytoplasmic. {ECO:0000250}.
TRANSMEM 51 73 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 74 118 Extracellular. {ECO:0000250}.
TRANSMEM 119 139 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 140 188 Cytoplasmic. {ECO:0000250}.
TRANSMEM 189 210 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 211 217 Extracellular. {ECO:0000250}.
TRANSMEM 218 238 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 239 296 Cytoplasmic. {ECO:0000250}.
TRANSMEM 297 318 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 319 332 Extracellular. {ECO:0000250}.
TRANSMEM 333 354 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 355 711 Cytoplasmic. {ECO:0000250}.
TRANSMEM 712 732 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 733 755 Extracellular. {ECO:0000250}.
TRANSMEM 756 776 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 777 831 Cytoplasmic. {ECO:0000250}.
TRANSMEM 832 852 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 853 853 Extracellular. {ECO:0000250}.
TRANSMEM 854 873 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 874 933 Cytoplasmic. {ECO:0000250}.
TRANSMEM 934 956 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 957 972 Extracellular. {ECO:0000250}.
TRANSMEM 973 994 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 995 1286 Cytoplasmic. {ECO:0000250}.
DOMAIN 57 359 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 394 630 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 711 999 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1034 1279 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 429 436 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1069 1076 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 625 647 Interaction with HAX1. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P21440}.
MOD_RES 34 34 Phosphothreonine.
{ECO:0000269|PubMed:24723470}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 929 975 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046258.
VAR_SEQ 1094 1100 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:2906314}.
/FTId=VSP_023263.
VARIANT 34 34 T -> M (in GBD1; reduces efflux activity
for PC in a phosphorylation-dependent
manner; dbSNP:rs142794414).
{ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:24723470}.
/FTId=VAR_073728.
VARIANT 47 47 R -> G (in GBD1; partly retained
intracellularly; reduces efflux activity
for PC in a phosphorylation-dependent
manner). {ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:23533021,
ECO:0000269|PubMed:24723470}.
/FTId=VAR_073729.
VARIANT 47 47 R -> Q (found in patients with
cholangitis; unknown pathological
significance; dbSNP:rs372685632).
{ECO:0000269|PubMed:22331132}.
/FTId=VAR_073730.
VARIANT 68 68 G -> R (in PFIC3; retained in the
reticulum endoplasmic; greatly reduced
expression).
{ECO:0000269|PubMed:24594635}.
/FTId=VAR_073731.
VARIANT 70 70 G -> R (in PFIC3).
{ECO:0000269|PubMed:21119540}.
/FTId=VAR_073732.
VARIANT 71 71 L -> H (in GBD1; dbSNP:rs780641693).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073733.
VARIANT 73 73 L -> V (in PFIC3 and GBD1;
dbSNP:rs8187788).
{ECO:0000269|PubMed:21119540,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_073734.
VARIANT 78 78 F -> C (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073735.
VARIANT 87 87 D -> E. {ECO:0000269|PubMed:16763017}.
/FTId=VAR_043078.
VARIANT 95 95 P -> S (in dbSNP:rs377268767).
{ECO:0000269|PubMed:16763017}.
/FTId=VAR_043079.
VARIANT 99 99 S -> F (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073736.
VARIANT 124 124 G -> S (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073737.
VARIANT 126 126 G -> E (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073738.
VARIANT 138 138 W -> R (in PFIC3; dbSNP:rs72552781).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043080.
VARIANT 150 150 R -> K (in ICP3; dbSNP:rs757693457).
{ECO:0000269|PubMed:12746424}.
/FTId=VAR_043081.
VARIANT 154 154 F -> S (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073739.
VARIANT 165 165 F -> I (in GBD1).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_043082.
VARIANT 175 175 T -> A (found in patients with
gallbladder and cholestasis; unknown
pathological significance;
dbSNP:rs58238559).
{ECO:0000269|PubMed:11313316,
ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:17264802,
ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_023501.
VARIANT 201 201 T -> M (in PFIC3; greatly reduced
expression; alters efflux activity for
PC; dbSNP:rs753318087).
{ECO:0000269|PubMed:24594635}.
/FTId=VAR_073740.
VARIANT 238 238 L -> V (in dbSNP:rs45596335).
{ECO:0000269|Ref.2}.
/FTId=VAR_020223.
VARIANT 250 250 A -> P (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073741.
VARIANT 263 263 I -> V (in dbSNP:rs45547936).
{ECO:0000269|Ref.2}.
/FTId=VAR_030763.
VARIANT 286 286 A -> V (in PFIC3 and GBD1; does not alter
plasma membrane location; inhibits efflux
activity for PC; dbSNP:rs765478923).
{ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:23533021,
ECO:0000269|PubMed:24806754}.
/FTId=VAR_073742.
VARIANT 301 301 M -> T (in GBD1; dbSNP:rs72552779).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_043083.
VARIANT 320 320 S -> F (in ICP3, GBD1 and PFIC3; unknown
pathological significance; does not alter
plasma membrane location; does not
inhibit efflux activity for PC;
dbSNP:rs72552778).
{ECO:0000269|PubMed:11313316,
ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:21119540,
ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:23533021,
ECO:0000269|PubMed:24806754}.
/FTId=VAR_023502.
VARIANT 346 346 S -> I (in PFIC3; dbSNP:rs67876345).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043084.
VARIANT 357 357 F -> L (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073743.
VARIANT 364 364 A -> V (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073744.
VARIANT 367 367 I -> V. {ECO:0000269|PubMed:16763017}.
/FTId=VAR_043085.
VARIANT 395 395 E -> G (in PFIC3; dbSNP:rs72552777).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043086.
VARIANT 403 403 Y -> H (in PFIC3; does not alter
cytoplasmic and cell membrane location;
inhibits efflux activity for PC and
cholesterol; dbSNP:rs121918443).
{ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:21119540,
ECO:0000269|PubMed:24045840}.
/FTId=VAR_073745.
VARIANT 406 406 R -> G (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073746.
VARIANT 406 406 R -> Q (found in patients with
cholangitis; unknown pathological
significance; dbSNP:rs763807769).
{ECO:0000269|PubMed:22331132}.
/FTId=VAR_073747.
VARIANT 424 424 T -> A (in PFIC3).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043087.
VARIANT 425 425 V -> M (in PFIC3).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043088.
VARIANT 450 450 E -> G. {ECO:0000269|PubMed:16763017}.
/FTId=VAR_043089.
VARIANT 459 459 D -> H (in PFIC3; retained in the
reticulum endoplasmic; greatly reduced
expression).
{ECO:0000269|PubMed:24594635}.
/FTId=VAR_073748.
VARIANT 475 475 V -> A (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073749.
VARIANT 479 479 P -> L (in PFIC3; greatly reduced
expression; alters efflux activity for
PC). {ECO:0000269|PubMed:24594635}.
/FTId=VAR_073750.
VARIANT 481 481 L -> R (in PFIC3; does not alter
cytoplasmic and cell membrane location;
inhibits efflux activity for PC and
cholesterol).
{ECO:0000269|PubMed:24045840}.
/FTId=VAR_073751.
VARIANT 510 510 N -> S (in GBD1; dbSNP:rs375315619).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073752.
VARIANT 511 511 A -> T (in PFIC3 and GBD1).
{ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_073753.
VARIANT 513 513 E -> K (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073754.
VARIANT 528 528 E -> D (in GBD1; unknown pathological
significance; dbSNP:rs8187797).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:22331132,
ECO:0000269|PubMed:23533021,
ECO:0000269|Ref.2}.
/FTId=VAR_043090.
VARIANT 535 535 G -> D (in PFIC3; reduced
phosphatidylcholine transporter activity;
does not alter plasma membrane location).
{ECO:0000269|PubMed:12671900,
ECO:0000269|PubMed:28012258}.
/FTId=VAR_043091.
VARIANT 536 536 G -> R (in GBD1; loss of
phosphatidylcholine transporter activity;
does not alter plasma membrane location).
{ECO:0000269|PubMed:28012258}.
/FTId=VAR_079611.
VARIANT 541 541 I -> F (in PFIC3 and GBD1;
dbSNP:rs66904256).
{ECO:0000269|PubMed:11313315,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_043092.
VARIANT 545 545 R -> H (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073755.
VARIANT 546 546 A -> D (in ICP3; disruption of protein
trafficking with subsequent lack of
functional protein at the cell surface;
dbSNP:rs121918441).
{ECO:0000269|PubMed:10767346}.
/FTId=VAR_023503.
VARIANT 549 549 R -> H (in GBD1; dbSNP:rs761238221).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073756.
VARIANT 556 556 L -> R (in PFIC3).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043093.
VARIANT 558 558 E -> K (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073757.
VARIANT 564 564 D -> G (in PFIC3).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043094.
VARIANT 589 589 H -> T (in GBD1; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073758.
VARIANT 590 590 R -> Q (found in patients with
gallbladder and cholestasis; unknown
pathological significance;
dbSNP:rs45575636).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:17264802,
ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:19261551,
ECO:0000269|PubMed:23533021,
ECO:0000269|Ref.2}.
/FTId=VAR_043095.
VARIANT 591 591 L -> Q (in GBD1; dbSNP:rs72552776).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_043096.
VARIANT 593 593 T -> A (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073759.
VARIANT 593 593 T -> M (in GBD1; dbSNP:rs571555115).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073760.
VARIANT 630 630 M -> V (in PFIC3; dbSNP:rs372476723).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073761.
VARIANT 647 647 E -> K (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073762.
VARIANT 651 651 T -> N (in dbSNP:rs45476795).
{ECO:0000269|Ref.2}.
/FTId=VAR_030765.
VARIANT 652 652 R -> G (found in patients with
gallbladder and cholestasis; unknown
pathological significance;
dbSNP:rs2230028).
{ECO:0000269|PubMed:11313315,
ECO:0000269|PubMed:12746424,
ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:16763017,
ECO:0000269|PubMed:17264802,
ECO:0000269|PubMed:19261551,
ECO:0000269|PubMed:21119540,
ECO:0000269|Ref.2}.
/FTId=VAR_020225.
VARIANT 701 701 L -> P (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073763.
VARIANT 711 711 F -> S (in PFIC3; dbSNP:rs72552773).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043097.
VARIANT 715 715 T -> I (in PFIC3; dbSNP:rs138773456).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073764.
VARIANT 723 723 G -> E (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073765.
VARIANT 726 726 P -> L (in GBD1; loss of
phosphatidylcholine transporter activity;
does not alter plasma membrane location;
dbSNP:rs141677867).
{ECO:0000269|PubMed:23533021,
ECO:0000269|PubMed:28012258}.
/FTId=VAR_073766.
VARIANT 726 726 P -> T (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073767.
VARIANT 729 729 S -> L (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073768.
VARIANT 737 737 A -> V (in PFIC3; dbSNP:rs147134978).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073769.
VARIANT 742 742 G -> S. {ECO:0000269|PubMed:12891548}.
/FTId=VAR_043098.
VARIANT 762 762 G -> E (in ICP3).
{ECO:0000269|PubMed:15077010}.
/FTId=VAR_043099.
VARIANT 764 764 I -> L (in a heterozygous patient with
risperidone-induced cholestasis).
{ECO:0000269|PubMed:17264802}.
/FTId=VAR_043100.
VARIANT 775 775 T -> M (found in patients with
cholangitis; unknown pathological
significance; dbSNP:rs148052192).
{ECO:0000269|PubMed:15077010,
ECO:0000269|PubMed:17726488,
ECO:0000269|PubMed:22331132}.
/FTId=VAR_043101.
VARIANT 788 788 R -> Q (found in patients with
gallbladder and cholestasis; unknown
pathological significance;
dbSNP:rs8187801).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:23533021,
ECO:0000269|Ref.2}.
/FTId=VAR_024359.
VARIANT 840 840 A -> D (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073770.
VARIANT 934 934 A -> T (found in patients with
gallbladder and cholestasis; unknown
pathological significance;
dbSNP:rs61730509).
{ECO:0000269|PubMed:12891548,
ECO:0000269|PubMed:23533021}.
/FTId=VAR_043102.
VARIANT 954 954 G -> S (in PFIC3; dbSNP:rs779829759).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073771.
VARIANT 964 964 V -> T (requires 2 nucleotide
substitutions; found in patients with
cholangitis; unknown pathological
significance).
{ECO:0000269|PubMed:22331132}.
/FTId=VAR_073772.
VARIANT 975 975 L -> V (in GBD1; dbSNP:rs759787957).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073773.
VARIANT 978 978 S -> P (in PFIC3; alters efflux activity
for PC). {ECO:0000269|PubMed:24594635}.
/FTId=VAR_073774.
VARIANT 983 983 G -> S (in PFIC3; dbSNP:rs56187107).
{ECO:0000269|PubMed:11313315}.
/FTId=VAR_043103.
VARIANT 1082 1082 L -> Q (in a heterozygous patient with
amoxicillin/clavulanic acid-induced
cholestasis).
{ECO:0000269|PubMed:17264802}.
/FTId=VAR_043104.
VARIANT 1084 1084 R -> W (in GBD1).
{ECO:0000269|PubMed:23533021}.
/FTId=VAR_073775.
VARIANT 1125 1125 E -> K (in PFIC3; alters efflux activity
for PC). {ECO:0000269|PubMed:24594635}.
/FTId=VAR_073776.
VARIANT 1161 1161 Missing (in GBD1).
/FTId=VAR_043105.
VARIANT 1168 1168 P -> S (in GBD1; dbSNP:rs121918442).
{ECO:0000269|PubMed:11313316,
ECO:0000269|PubMed:12891548}.
/FTId=VAR_023504.
VARIANT 1183 1183 S -> L (in GBD1; severely reduced
phosphatidylcholine transporter activity;
does not alter plasma membrane location).
{ECO:0000269|PubMed:28012258}.
/FTId=VAR_079612.
VARIANT 1185 1185 G -> S (in GBD1; loss of
phosphatidylcholine transporter activity;
does not alter plasma membrane location).
{ECO:0000269|PubMed:28012258}.
/FTId=VAR_079613.
VARIANT 1193 1193 A -> T (in PFIC3).
{ECO:0000269|PubMed:17726488}.
/FTId=VAR_073777.
MUTAGEN 34 34 T->D: Does not inhibit efflux activity
for PC. {ECO:0000269|PubMed:24723470}.
MUTAGEN 44 44 T->A: Reduces efflux activity for PC.
Does not alter apical membrane location.
{ECO:0000269|PubMed:24723470}.
MUTAGEN 49 49 S->A: Reduces efflux activity for PC.
Does not alter apical membrane location.
{ECO:0000269|PubMed:24723470}.
MUTAGEN 435 435 K->M: Inhibits efflux activity for PC and
cholesterol, but does not alter
glycosylation and surface expression in
the presence of taurocholate.
{ECO:0000269|PubMed:17523162}.
MUTAGEN 953 953 A->D: Accumulates predominantly in
intracellular compartments with only a
small fraction at the plasma membrane and
inhibits partially the efflux activity
for PC. {ECO:0000269|PubMed:24806754}.
MUTAGEN 1075 1075 K->M: Inhibits efflux activity for PC and
cholesterol, but does not alter
glycosylation and surface expression in
the presence of taurocholate.
{ECO:0000269|PubMed:17523162}.
SEQUENCE 1286 AA; 141523 MW; 9A9066F2292F2CCF CRC64;
MDLEAAKNGT AWRPTSAEGD FELGISSKQK RKKTKTVKMI GVLTLFRYSD WQDKLFMSLG
TIMAIAHGSG LPLMMIVFGE MTDKFVDTAG NFSFPVNFSL SLLNPGKILE EEMTRYAYYY
SGLGAGVLVA AYIQVSFWTL AAGRQIRKIR QKFFHAILRQ EIGWFDINDT TELNTRLTDD
ISKISEGIGD KVGMFFQAVA TFFAGFIVGF IRGWKLTLVI MAISPILGLS AAVWAKILSA
FSDKELAAYA KAGAVAEEAL GAIRTVIAFG GQNKELERYQ KHLENAKEIG IKKAISANIS
MGIAFLLIYA SYALAFWYGS TLVISKEYTI GNAMTVFFSI LIGAFSVGQA APCIDAFANA
RGAAYVIFDI IDNNPKIDSF SERGHKPDSI KGNLEFNDVH FSYPSRANVK ILKGLNLKVQ
SGQTVALVGS SGCGKSTTVQ LIQRLYDPDE GTINIDGQDI RNFNVNYLRE IIGVVSQEPV
LFSTTIAENI CYGRGNVTMD EIKKAVKEAN AYEFIMKLPQ KFDTLVGERG AQLSGGQKQR
IAIARALVRN PKILLLDEAT SALDTESEAE VQAALDKARE GRTTIVIAHR LSTVRNADVI
AGFEDGVIVE QGSHSELMKK EGVYFKLVNM QTSGSQIQSE EFELNDEKAA TRMAPNGWKS
RLFRHSTQKN LKNSQMCQKS LDVETDGLEA NVPPVSFLKV LKLNKTEWPY FVVGTVCAIA
NGGLQPAFSV IFSEIIAIFG PGDDAVKQQK CNIFSLIFLF LGIISFFTFF LQGFTFGKAG
EILTRRLRSM AFKAMLRQDM SWFDDHKNST GALSTRLATD AAQVQGATGT RLALIAQNIA
NLGTGIIISF IYGWQLTLLL LAVVPIIAVS GIVEMKLLAG NAKRDKKELE AAGKIATEAI
ENIRTVVSLT QERKFESMYV EKLYGPYRNS VQKAHIYGIT FSISQAFMYF SYAGCFRFGA
YLIVNGHMRF RDVILVFSAI VFGAVALGHA SSFAPDYAKA KLSAAHLFML FERQPLIDSY
SEEGLKPDKF EGNITFNEVV FNYPTRANVP VLQGLSLEVK KGQTLALVGS SGCGKSTVVQ
LLERFYDPLA GTVFVDFGFQ LLDGQEAKKL NVQWLRAQLG IVSQEPILFD CSIAENIAYG
DNSRVVSQDE IVSAAKAANI HPFIETLPHK YETRVGDKGT QLSGGQKQRI AIARALIRQP
QILLLDEATS ALDTESEKVV QEALDKAREG RTCIVIAHRL STIQNADLIV VFQNGRVKEH
GTHQQLLAQK GIYFSMVSVQ AGTQNL


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