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   27-MAR-2024, entry version 182.
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.ENSMUSP00000099770; -.
DR   ChEMBL; CHEMBL2073695; -.
DR   GlyCosmos; Q9QY30; 4 sites, No reported glycans.
DR   GlyGen; Q9QY30; 4 sites.
DR   iPTMnet; Q9QY30; -.
DR   PhosphoSitePlus; Q9QY30; -.
DR   SwissPalm; Q9QY30; -.
DR   jPOST; Q9QY30; -.
DR   MaxQB; Q9QY30; -.
DR   PaxDb; 10090-ENSMUSP00000099771; -.
DR   ProteomicsDB; 296470; -.
DR   Pumba; Q9QY30; -.
DR   Antibodypedia; 1033; 286 antibodies from 34 providers.
DR   DNASU; 27413; -.
DR   Ensembl; ENSMUST00000102709.8; ENSMUSP00000099770.2; ENSMUSG00000027048.16.
DR   Ensembl; ENSMUST00000102710.10; ENSMUSP00000099771.4; ENSMUSG00000027048.16.
DR   GeneID; 27413; -.
DR   KEGG; mmu:27413; -.
DR   UCSC; uc008jya.1; mouse.
DR   AGR; MGI:1351619; -.
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; GFGQEEQ; -.
DR   OrthoDB; 5487044at2759; -.
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 79 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 cell types or tissues.
DR   ExpressionAtlas; Q9QY30; baseline and differential.
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:0000139; C:Golgi membrane; ISO:MGI.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; 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   CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR   CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR   CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR43394:SF11; ALPHA-FACTOR-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; Q9QY30; MM.
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
//