ABCBB_MOUSE
ID ABCBB_MOUSE Reviewed; 1321 AA.
AC Q9QY30; A2AUN4; Q9QZE8;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Bile salt export pump {ECO:0000303|Ref.4};
DE EC=7.6.2.- {ECO:0000269|PubMed:23764895};
DE AltName: Full=ATP-binding cassette sub-family B member 11;
DE AltName: Full=Sister of P-glycoprotein {ECO:0000250|UniProtKB:O70127};
GN Name=Abcb11 {ECO:0000312|MGI:MGI:1351619};
GN Synonyms=Bsep {ECO:0000303|Ref.4}, Spgp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10607905; DOI=10.1016/s0378-1119(99)00460-6;
RA Green R.M., Hoda F., Ward K.L.;
RT "Molecular cloning and characterization of the murine bile salt export
RT pump.";
RL Gene 241:117-123(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 463-635.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Salkar R., Suchy F.J., Ananthanarayanan M.;
RT "Molecular cloning of mouse liver bile salt export pump (bsep).";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11172067; DOI=10.1073/pnas.98.4.2011;
RA Wang R., Salem M., Yousef I.M., Tuchweber B., Lam P., Childs S.J.,
RA Helgason C.D., Ackerley C., Phillips M.J., Ling V.;
RT "Targeted inactivation of sister of P-glycoprotein gene (spgp) in mice
RT results in nonprogressive but persistent intrahepatic cholestasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2011-2016(2001).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=14570929; DOI=10.1074/jbc.m307363200;
RA Figge A., Lammert F., Paigen B., Henkel A., Matern S., Korstanje R.,
RA Shneider B.L., Chen F., Stoltenberg E., Spatz K., Hoda F., Cohen D.E.,
RA Green R.M.;
RT "Hepatic overexpression of murine Abcb11 increases hepatobiliary lipid
RT secretion and reduces hepatic steatosis.";
RL J. Biol. Chem. 279:2790-2799(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=19228692; DOI=10.1074/jbc.m808667200;
RA Paulusma C.C., de Waart D.R., Kunne C., Mok K.S., Elferink R.P.;
RT "Activity of the bile salt export pump (ABCB11) is critically dependent on
RT canalicular membrane cholesterol content.";
RL J. Biol. Chem. 284:9947-9954(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22619174; DOI=10.1074/jbc.m111.329318;
RA Zhang Y., Li F., Patterson A.D., Wang Y., Krausz K.W., Neale G., Thomas S.,
RA Nachagari D., Vogel P., Vore M., Gonzalez F.J., Schuetz J.D.;
RT "Abcb11 deficiency induces cholestasis coupled to impaired beta-fatty acid
RT oxidation in mice.";
RL J. Biol. Chem. 287:24784-24794(2012).
RN [11]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=23764895; DOI=10.1152/ajpgi.00082.2013;
RA Wang R., Liu L., Sheps J.A., Forrest D., Hofmann A.F., Hagey L.R., Ling V.;
RT "Defective canalicular transport and toxicity of dietary ursodeoxycholic
RT acid in the abcb11-/- mouse: transport and gene expression studies.";
RL Am. J. Physiol. 305:G286-G294(2013).
CC -!- FUNCTION: Catalyzes the transport of the major hydrophobic bile salts,
CC such as taurine and glycine-conjugated cholic acid across the
CC canalicular membrane of hepatocytes in an ATP-dependent manner,
CC therefore participates in hepatic bile acid homeostasis and
CC consequently to lipid homeostasis through regulation of biliary lipid
CC secretion in a bile salts dependent manner (PubMed:14570929,
CC PubMed:11172067, PubMed:23764895, PubMed:22619174, PubMed:19228692).
CC Transports taurine-conjugated bile salts more rapidly than glycine-
CC conjugated bile salts (By similarity). Also transports non-bile acid
CC compounds, such as pravastatin and fexofenadine in an ATP-dependent
CC manner and may be involved in their biliary excretion (By similarity).
CC {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:11172067,
CC ECO:0000269|PubMed:14570929, ECO:0000269|PubMed:19228692,
CC ECO:0000269|PubMed:22619174, ECO:0000269|PubMed:23764895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50049;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:19228692};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000305|PubMed:19228692};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycochenodeoxycholate(in) + H2O = ADP +
CC glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50060,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurochenodeoxycholate(in) = ADP + H(+) +
CC phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:50064,
CC ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycoursodeoxycholate(in) + H2O = ADP +
CC glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + tauroursodeoxycholate(in) = ADP + H(+) + phosphate
CC + tauroursodeoxycholate(out); Xref=Rhea:RHEA:50072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23764895};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073;
CC Evidence={ECO:0000269|PubMed:23764895};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurodeoxycholate(in) = ADP + H(+) + phosphate +
CC taurodeoxycholate(out); Xref=Rhea:RHEA:50080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36261,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) +
CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pravastatin(in) = ADP + H(+) + phosphate +
CC pravastatin(out); Xref=Rhea:RHEA:63908, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:63660, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909;
CC Evidence={ECO:0000250|UniProtKB:O95342};
CC -!- ACTIVITY REGULATION: The uptake of taurocholate is inhibited by
CC taurolithocholate sulfate with an IC(50) of 9 uM. Pravastatin
CC competitively inhibits the transport of taurocholic acid. Cyclosporin
CC A, glibenclamide, rifampicin and troglitazonestrongly competitively
CC inhibit the transport activity of taurocholate (By similarity). The
CC canalicular transport activity of taurocholate is strongly dependent on
CC canalicular membrane cholesterol content (By similarity)
CC (PubMed:19228692). The uptake of taurocholate is increased by
CC short- and medium-chain fatty acids. Cholesterol increases transport
CC capacity of taurocholate without affecting the affinity for the
CC substrate (By similarity). {ECO:0000250|UniProtKB:O95342,
CC ECO:0000269|PubMed:19228692}.
CC -!- SUBUNIT: Interacts with HAX1 (By similarity). Interacts with the
CC adapter protein complex 2 (AP-2) throught AP2A2 or AP2A1; this
CC interaction regulates cell membrane expression of ABCB11 through its
CC internalization in a clathrin-dependent manner and its subsequent
CC degradation (By similarity). {ECO:0000250|UniProtKB:O70127,
CC ECO:0000250|UniProtKB:O95342}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Endosome
CC {ECO:0000250|UniProtKB:O70127}. Cell membrane
CC {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O70127}. Note=Internalized at the canalicular
CC membrane through interaction with the adapter protein complex 2 (AP-2).
CC At steady state, localizes in the canalicular membrane but is also
CC present in recycling endosomes. ABCB11 constantly and rapidly exchanges
CC between the two sites through tubulo-vesicles carriers that move along
CC microtubules. Microtubule-dependent trafficking of ABCB11 is enhanced
CC by taurocholate and cAMP and regulated by STK11 through a PKA-mediated
CC pathway. Trafficking of newly synthesized ABCB11 through endosomal
CC compartment to the bile canalicular membrane is accelerated by cAMP but
CC not by taurocholate (By similarity). Cell membrane expression is up-
CC regulated by short- and medium-chain fatty acids (By similarity).
CC {ECO:0000250|UniProtKB:O70127, ECO:0000250|UniProtKB:O95342}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly, if not exclusively in the
CC liver, where it was further localized to the canalicular microvilli and
CC to subcanalicular vesicles of the hepatocytes by in situ.
CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC containing a hydrophobic membrane-anchoring domain and an ATP binding
CC cassette (ABC) domain.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
CC -!- PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface
CC expression of ABCB11. {ECO:0000250|UniProtKB:O95342}.
CC -!- DISRUPTION PHENOTYPE: Transgenic mice with up-regulated liver
CC canalicular membrane expression of Abcb11 appear healthy and normal and
CC demonstrate any difference in longevity. Transgenic mice exhibit a
CC normal reproductive rate and gender distribution and are born in a
CC normal Mendelian distribution. Transgenic mice have food consumption
CC identical to their background strain controls. Transgenic mice manifest
CC increases of both bile flow and biliary lipid secretion and are
CC resistant to the development of hepatic steatosis (PubMed:14570929).
CC Homozygous Abcb11 knockout mice on a mixed genetic background are
CC viable and fertile, but displayed growth retardation. Their body weight
CC is about 20% lower than their wild-type littermates at weaning (21 days
CC after birth). They tend to have a lower body weight throughout their
CC life, but display only mild non progressive cholestasis
CC (PubMed:11172067). Homozygous Abcb11 knockout mice on a pure C57BL/6J
CC background exhibit a progressive intrahepatic cholestasis due to an
CC hepatic bile acid retention and an alteration of lipid metabolism
CC (PubMed:22619174). {ECO:0000269|PubMed:11172067,
CC ECO:0000269|PubMed:14570929, ECO:0000269|PubMed:22619174}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; AF133903; AAF14372.1; -; mRNA.
DR EMBL; AL929170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27032.1; -; Genomic_DNA.
DR EMBL; AF186585; AAD56419.1; -; mRNA.
DR CCDS; CCDS16090.1; -.
DR RefSeq; NP_066302.2; NM_021022.3.
DR RefSeq; XP_006499732.1; XM_006499669.3.
DR AlphaFoldDB; Q9QY30; -.
DR SMR; Q9QY30; -.
DR STRING; 10090.ENSMUSP00000099771; -.
DR ChEMBL; CHEMBL2073695; -.
DR GlyGen; Q9QY30; 4 sites.
DR iPTMnet; Q9QY30; -.
DR PhosphoSitePlus; Q9QY30; -.
DR SwissPalm; Q9QY30; -.
DR jPOST; Q9QY30; -.
DR MaxQB; Q9QY30; -.
DR PaxDb; Q9QY30; -.
DR PRIDE; Q9QY30; -.
DR ProteomicsDB; 296470; -.
DR Antibodypedia; 1033; 241 antibodies from 34 providers.
DR DNASU; 27413; -.
DR Ensembl; ENSMUST00000102709; ENSMUSP00000099770; ENSMUSG00000027048.
DR Ensembl; ENSMUST00000102710; ENSMUSP00000099771; ENSMUSG00000027048.
DR GeneID; 27413; -.
DR KEGG; mmu:27413; -.
DR UCSC; uc008jya.1; mouse.
DR CTD; 8647; -.
DR MGI; MGI:1351619; Abcb11.
DR VEuPathDB; HostDB:ENSMUSG00000027048; -.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000157564; -.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q9QY30; -.
DR OMA; LFMLPMT; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q9QY30; -.
DR TreeFam; TF105193; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR BioGRID-ORCS; 27413; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9QY30; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QY30; protein.
DR Bgee; ENSMUSG00000027048; Expressed in left lobe of liver and 24 other tissues.
DR ExpressionAtlas; Q9QY30; baseline and differential.
DR Genevisible; Q9QY30; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR GO; GO:0046691; C:intracellular canaliculus; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015126; F:canalicular bile acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0015722; P:canalicular bile acid transport; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:UniProtKB.
DR GO; GO:0120189; P:positive regulation of bile acid secretion; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:1904251; P:regulation of bile acid metabolic process; IMP:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:1904486; P:response to 17alpha-ethynylestradiol; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR GO; GO:0046618; P:xenobiotic export from cell; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR030278; BSEP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR PANTHER; PTHR24221:SF165; PTHR24221:SF165; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endosome; Glycoprotein; Lipid transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1321
FT /note="Bile salt export pump"
FT /id="PRO_0000093297"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 84..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 169..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 237..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 262..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 341..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 375..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 777..794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 816..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 912..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1001..1011
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1033..1321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 62..385
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 420..656
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 755..1043
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1078..1316
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 651..674
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000250"
FT REGION 662..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1113..1120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70127"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95342"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70127"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 104
FT /note="E -> G (in Ref. 1; AAF14372)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="L -> P (in Ref. 3; AAD56419)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="T -> V (in Ref. 3; AAD56419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1321 AA; 146749 MW; C71F8D3D0A352BA8 CRC64;
MSDSVILRSV KKFGEENHAF ESDGFHNNDK KSRLQDKKKG EGARVGFFEL FRFSSSKDNW
LMFMGSVCAL LHGMAQPGMI IVFGILTDIF VEYDIERQEL SIPEKVCMNN TIVWINSSFN
QNMTNGTSCG LVDINSEVIK FSGIYAGVGV AVLILGYFQI RLWVITGARQ IRKMRKFYFR
RIMRMEIGWF DCTSVGELNS RFSDDINKID EAIADQMALF LQRLSTALSG LLLGFYRGWK
LTLVILAVSP LIGIGAAVIG LSVAKFTELE LKAYAKAGSI ADEVLSSIRT VAAFGGENKE
VERYEKNLMF AQRWGIWKGM VMGFFTGYMW CLIFFCYALA FWYGSRLVLD EGEYTPGTLI
QIFLCVIIAA MNIGNASSCL EIFSTGCSAA SSIFQTIDRQ PVMDCMSGDG YKLDRIKGEI
EFHNVTFHYP SRPEVKILNN LSMVIKPGET TAFVGSSGAG KSTALQLIQR FYDPCEGMVT
LDGHDIRSLN IRWLRDQIGI VEQEPVLFST TIAENIRLGR EEATMEDIVQ AAKDANAYNF
IMALPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRKPKIL LLDMATSALD NESEAKVQGA
LNKIQHGHTI ISVAHRLSTV RSADVIIGFE HGTAVERGTH EELLERKGVY FMLVTLQSQE
DNTHKETGIK GKDTTEGDTP ERTFSRGSYQ DSLRASIRQR SKSQLSHLSH EPPLAIGDHK
SSYEDRKDND VLVEEVEPAP VRRILKYNIS EWPYILVGAL CAAINGAVTP IYSLLFSQIL
KTFSLVDKEQ QRSEIYSMCL FFVILGCVSL FTQFLQGYNF AKSGELLTKR LRKFGFKAML
RQDIGWFDDL KNNPGVLTTR LATDASQVQG ATGSQVGMMV NSFTNIFVAV LIAFLFNWKL
SLVISVFFPF LALSGAVQTK MLTGFASQDK EILEKAGQIT NEALSNIRTV AGIGVEGRFI
KAFEVELEKS YKTAIRKANV YGLCYAFSQG ISFLANSAAY RYGGYLIVYE DLNFSYVFRV
VSSIAMSATA VGRTFSYTPS YAKAKISAAR FFQLLDRKPP IDVYSGAGEK WDNFQGKIDF
IDCKFTYPSR PDIQVLNGLS VSVDPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGTVMID
GHDSKKVNVQ FLRSNIGIVS QEPVLFDCSI MDNIKYGDNT KEISVERAIA AAKQAQLHDF
VMSLPEKYET NVGIQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQLA
LDKAREGRTC IVIAHRLSTI QNSDIIAVMS QGVVIEKGTH KKLMDQKGAY YKLVITGAPI
S
