ID   ABCBB_RAT               Reviewed;        1321 AA.
AC   O70127;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Bile salt export pump {ECO:0000303|PubMed:16332456};
DE            EC=7.6.2.- {ECO:0000269|PubMed:16332456};
DE   AltName: Full=ATP-binding cassette sub-family B member 11;
DE   AltName: Full=Sister of P-glycoprotein {ECO:0000303|PubMed:9545351};
GN   Name=Abcb11 {ECO:0000312|RGD:619930};
GN   Synonyms=Bsep {ECO:0000303|PubMed:16332456}, Spgp
GN   {ECO:0000303|PubMed:9545351};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=9545351; DOI=10.1074/jbc.273.16.10046;
RA   Gerloff T., Stieger B., Hagenbuch B., Madon J., Landmann L., Roth J.,
RA   Hofmann A.F., Meier P.J.;
RT   "The sister of P-glycoprotein represents the canalicular bile salt export
RT   pump of mammalian liver.";
RL   J. Biol. Chem. 273:10046-10050(1998).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11113123; DOI=10.1074/jbc.m007794200;
RA   Kipp H., Pichetshote N., Arias I.M.;
RT   "Transporters on demand: intrahepatic pools of canalicular ATP binding
RT   cassette transporters in rat liver.";
RL   J. Biol. Chem. 276:7218-7224(2001).
RN   [3]
RP   INTERACTION WITH HAX1.
RX   PubMed=15159385; DOI=10.1074/jbc.m404337200;
RA   Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.;
RT   "Identification of HAX-1 as a protein that binds bile salt export protein
RT   and regulates its abundance in the apical membrane of Madin-Darby canine
RT   kidney cells.";
RL   J. Biol. Chem. 279:32761-32770(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15121884; DOI=10.1091/mbc.e03-10-0737;
RA   Wakabayashi Y., Lippincott-Schwartz J., Arias I.M.;
RT   "Intracellular trafficking of bile salt export pump (ABCB11) in polarized
RT   hepatic cells: constitutive cycling between the canalicular membrane and
RT   rab11-positive endosomes.";
RL   Mol. Biol. Cell 15:3485-3496(2004).
RN   [5]
RP   CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=16332456; DOI=10.1016/j.bbalip.2005.10.006;
RA   Hayashi H., Takada T., Suzuki H., Onuki R., Hofmann A.F., Sugiyama Y.;
RT   "Transport by vesicles of glycine- and taurine-conjugated bile salts and
RT   taurolithocholate 3-sulfate: a comparison of human BSEP with rat Bsep.";
RL   Biochim. Biophys. Acta 1738:54-62(2005).
RN   [6]
RP   CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=15901796; DOI=10.1124/jpet.105.084830;
RA   Hirano M., Maeda K., Hayashi H., Kusuhara H., Sugiyama Y.;
RT   "Bile salt export pump (BSEP/ABCB11) can transport a nonbile acid
RT   substrate, pravastatin.";
RL   J. Pharmacol. Exp. Ther. 314:876-882(2005).
RN   [7]
RP   GLYCOSYLATION AT ASN-109; ASN-116; ASN-122 AND ASN-125, MUTAGENESIS OF
RP   ASN-109; ASN-116; ASN-122 AND ASN-125, CATALYTIC ACTIVITY, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17082223; DOI=10.1152/ajpgi.00415.2006;
RA   Mochizuki K., Kagawa T., Numari A., Harris M.J., Itoh J., Watanabe N.,
RA   Mine T., Arias I.M.;
RT   "Two N-linked glycans are required to maintain the transport activity of
RT   the bile salt export pump (ABCB11) in MDCK II cells.";
RL   Am. J. Physiol. 292:G818-G828(2007).
RN   [8]
RP   CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RC   TISSUE=Liver;
RX   PubMed=18985798; DOI=10.1002/bdd.629;
RA   Yabuuchi H., Tanaka K., Maeda M., Takemura M., Oka M., Ohashi R., Tamai I.;
RT   "Cloning of the dog bile salt export pump (BSEP; ABCB11) and functional
RT   comparison with the human and rat proteins.";
RL   Biopharm. Drug Dispos. 29:441-448(2008).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18245269; DOI=10.1124/mol.107.041459;
RA   Matsushima S., Maeda K., Hayashi H., Debori Y., Schinkel A.H.,
RA   Schuetz J.D., Kusuhara H., Sugiyama Y.;
RT   "Involvement of multiple efflux transporters in hepatic disposition of
RT   fexofenadine.";
RL   Mol. Pharmacol. 73:1474-1483(2008).
RN   [10]
RP   UBIQUITINATION.
RX   PubMed=18829893; DOI=10.1124/mol.108.049288;
RA   Hayashi H., Sugiyama Y.;
RT   "Short-chain ubiquitination is associated with the degradation rate of a
RT   cell-surface-resident bile salt export pump (BSEP/ABCB11).";
RL   Mol. Pharmacol. 75:143-150(2009).
RN   [11]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-1311.
RX   PubMed=22262466; DOI=10.1002/hep.25591;
RA   Hayashi H., Inamura K., Aida K., Naoi S., Horikawa R., Nagasaka H.,
RA   Takatani T., Fukushima T., Hattori A., Yabuki T., Horii I., Sugiyama Y.;
RT   "AP2 adaptor complex mediates bile salt export pump internalization and
RT   modulates its hepatocanalicular expression and transport function.";
RL   Hepatology 55:1889-1900(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703; SER-706 AND SER-1321,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24643070; DOI=10.1371/journal.pone.0091921;
RA   Homolya L., Fu D., Sengupta P., Jarnik M., Gillet J.P., Vitale-Cross L.,
RA   Gutkind J.S., Lippincott-Schwartz J., Arias I.M.;
RT   "LKB1/AMPK and PKA control ABCB11 trafficking and polarization in
RT   hepatocytes.";
RL   PLoS ONE 9:e91921-e91921(2014).
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:16332456,
CC       PubMed:15901796, PubMed:17082223, PubMed:18985798, PubMed:9545351).
CC       Transports taurine-conjugated bile salts more rapidly than glycine-
CC       conjugated bile salts (PubMed:16332456). 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 (PubMed:15901796,
CC       PubMed:18245269). {ECO:0000269|PubMed:15901796,
CC       ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:17082223,
CC       ECO:0000269|PubMed:18245269, ECO:0000269|PubMed:18985798,
CC       ECO:0000269|PubMed:9545351}.
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:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50049;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456,
CC         ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18985798,
CC         ECO:0000269|PubMed:9545351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC         Evidence={ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456,
CC         ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18985798};
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:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:16332456};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:16332456, ECO:0000269|PubMed:9545351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:16332456};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:16332456, ECO:0000269|PubMed:9545351};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:16332456};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50081;
CC         Evidence={ECO:0000269|PubMed:16332456};
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:0000269|PubMed:15901796};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909;
CC         Evidence={ECO:0000305|PubMed:15901796};
CC   -!- ACTIVITY REGULATION: The uptake of taurocholate is inhibited by
CC       taurolithocholate sulfate with an IC(50) of 52.9 uM (PubMed:16332456).
CC       Pravastatin competitively inhibits the transport of taurocholic acid
CC       (PubMed:15901796, PubMed:18985798). Cyclosporin A, glibenclamide,
CC       rifampicin and troglitazonestrongly competitively inhibit the transport
CC       activity of taurocholate (PubMed:18985798). The canalicular transport
CC       activity of taurocholate is strongly dependent on canalicular membrane
CC       cholesterol content. 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:15901796, ECO:0000269|PubMed:16332456,
CC       ECO:0000269|PubMed:18985798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.7 uM for taurocholate {ECO:0000269|PubMed:16332456};
CC         KM=25.7 uM for glycocholate {ECO:0000269|PubMed:16332456};
CC         KM=10.2 uM for taurochenodeoxycholate {ECO:0000269|PubMed:16332456};
CC         KM=5.6 uM for glycochenodeoxycholate {ECO:0000269|PubMed:16332456};
CC         KM=22.2 uM for taurocholate {ECO:0000269|PubMed:18985798};
CC         Vmax=2200 pmol/min/mg enzyme for taurocholate transport
CC         {ECO:0000269|PubMed:16332456};
CC         Vmax=237 pmol/min/mg enzyme for taurocholate transport
CC         {ECO:0000269|PubMed:18985798};
CC   -!- SUBUNIT: Interacts with HAX1 (PubMed:15159385). 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 (PubMed:22262466). {ECO:0000269|PubMed:15159385,
CC       ECO:0000269|PubMed:22262466}.
CC   -!- INTERACTION:
CC       O70127; Q7TSE9: Hax1; NbExp=5; IntAct=EBI-930036, EBI-930005;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:17082223,
CC       ECO:0000269|PubMed:9545351}; Multi-pass membrane protein {ECO:0000255}.
CC       Recycling endosome membrane {ECO:0000269|PubMed:11113123,
CC       ECO:0000269|PubMed:15121884}; Multi-pass membrane protein
CC       {ECO:0000255}. Endosome {ECO:0000269|PubMed:11113123}. Cell membrane
CC       {ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466,
CC       ECO:0000269|PubMed:24643070}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Internalized at the canalicular membrane through
CC       interaction with the adapter protein complex 2 (AP-2)
CC       (PubMed:22262466). At steady state, localizes in the canalicular
CC       membrane but is also present in recycling endosomes. ABCB11 constantly
CC       and rapidly exchanges between the two sites through tubulo-vesicles
CC       carriers that move along microtubules (PubMed:15121884,
CC       PubMed:11113123). Microtubule-dependent trafficking of ABCB11 is
CC       enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-
CC       mediated pathway (PubMed:24643070, PubMed:11113123). Trafficking of
CC       newly synthesized ABCB11 through endosomal compartment to the bile
CC       canalicular membrane is accelerated by cAMP but not by taurocholate
CC       (PubMed:11113123). Cell membrane expression is up-regulated by
CC       short- and medium-chain fatty acids (By similarity).
CC       {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:11113123,
CC       ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466,
CC       ECO:0000269|PubMed:24643070}.
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       {ECO:0000269|PubMed:9545351}.
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: Ubiquitinated; short-chain ubiquitination regulates cell-Surface
CC       expression of ABCB11. {ECO:0000269|PubMed:18829893}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
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; U69487; AAC40084.1; -; mRNA.
DR   PIR; T42842; T42842.
DR   RefSeq; NP_113948.1; NM_031760.1.
DR   AlphaFoldDB; O70127; -.
DR   SMR; O70127; -.
DR   BioGRID; 249756; 1.
DR   IntAct; O70127; 2.
DR   STRING; 10116.ENSRNOP00000064279; -.
DR   BindingDB; O70127; -.
DR   ChEMBL; CHEMBL2073674; -.
DR   DrugCentral; O70127; -.
DR   SwissLipids; SLP:000001598; -.
DR   GlyCosmos; O70127; 4 sites, No reported glycans.
DR   GlyGen; O70127; 4 sites.
DR   iPTMnet; O70127; -.
DR   PhosphoSitePlus; O70127; -.
DR   PaxDb; 10116-ENSRNOP00000064279; -.
DR   Ensembl; ENSRNOT00000075107.3; ENSRNOP00000064279.3; ENSRNOG00000050860.3.
DR   Ensembl; ENSRNOT00055040726; ENSRNOP00055033081; ENSRNOG00055023634.
DR   Ensembl; ENSRNOT00060005254; ENSRNOP00060003888; ENSRNOG00060003171.
DR   Ensembl; ENSRNOT00065027401; ENSRNOP00065021530; ENSRNOG00065016450.
DR   GeneID; 83569; -.
DR   KEGG; rno:83569; -.
DR   AGR; RGD:619930; -.
DR   CTD; 8647; -.
DR   RGD; 619930; Abcb11.
DR   eggNOG; KOG0055; Eukaryota.
DR   GeneTree; ENSGT00940000157564; -.
DR   InParanoid; O70127; -.
DR   OMA; GFGQEEQ; -.
DR   OrthoDB; 5487044at2759; -.
DR   PhylomeDB; O70127; -.
DR   Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR   Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   PRO; PR:O70127; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR   GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
DR   GO; GO:0046691; C:intracellular canaliculus; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IMP:UniProtKB.
DR   GO; GO:0015432; F:ABC-type bile acid transporter activity; IDA:UniProtKB.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IMP: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; IDA:RGD.
DR   GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0015721; P:bile acid and bile salt transport; IDA:UniProtKB.
DR   GO; GO:0008206; P:bile acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR   GO; GO:0015722; P:canalicular bile acid transport; IDA:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR   GO; GO:0055091; P:phospholipid homeostasis; ISS:UniProtKB.
DR   GO; GO:0120189; P:positive regulation of bile acid secretion; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR   GO; GO:1904251; P:regulation of bile acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0120188; P:regulation of bile acid secretion; IEP:RGD.
DR   GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:RGD.
DR   GO; GO:0055085; P:transmembrane transport; IDA:RGD.
DR   GO; GO:0046618; P:xenobiotic export from cell; IMP:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IMP:UniProtKB.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; IMP: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; 3.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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.
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_0000093299"
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:0000269|PubMed:15159385"
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:0000250|UniProtKB:Q9QY30"
FT   MOD_RES         703
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         706
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17082223"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17082223"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17082223"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:17082223"
FT   MUTAGEN         109
FT                   /note="N->Q: Impairs N-glycosylation; when associated with
FT                   Q-116; Q-122 and Q-125. Significantly decreases
FT                   taurocholate; when associated with Q-116; Q-122 and Q-125.
FT                   Significantly decreases protein expression; when associated
FT                   with Q-116; Q-122 and Q-125. Affects protein localization
FT                   at the apical membrane; when associated with Q-116; Q-122
FT                   and Q-125. Does not affect protein localization at the
FT                   apical membrane."
FT                   /evidence="ECO:0000269|PubMed:17082223"
FT   MUTAGEN         116
FT                   /note="N->Q: Impairs N-glycosylation; when associated with
FT                   Q-109; Q-122 and Q-125. Significantly decreases
FT                   taurocholate; when associated with Q-109; Q-122 and Q-125.
FT                   Significantly decreases protein expression; when associated
FT                   with Q-109; Q-122 and Q-125. Affects protein localization
FT                   at the apical membrane; when associated with Q-109; Q-122
FT                   and Q-125. Does not affect protein localization at the
FT                   apical membrane; when associated with Q-109; Q-122 and
FT                   Q-125."
FT                   /evidence="ECO:0000269|PubMed:17082223"
FT   MUTAGEN         122
FT                   /note="N->Q: Impairs N-glycosylation; when associated with
FT                   Q-109; Q-116 and Q-125. Significantly decreases
FT                   taurocholate; when associated with Q-109; Q-116 and Q-125.
FT                   Significantly decreases protein expression; when associated
FT                   with Q-109; Q-116 and Q-125. Affects protein localization
FT                   at the apical membrane; when associated with Q-109; Q-116
FT                   and Q-125."
FT                   /evidence="ECO:0000269|PubMed:17082223"
FT   MUTAGEN         125
FT                   /note="N->Q: Impairs N-glycosylation; when associated with
FT                   Q-109; Q-116 and Q-122. Significantly decreases
FT                   taurocholate; when associated with Q-109; Q-116 and Q-122.
FT                   Significantly decreases protein expression; when associated
FT                   with Q-109; Q-116 and Q-122. Affects protein localization
FT                   at the apical membrane;when associated with Q-109; Q-116
FT                   and Q-122."
FT                   /evidence="ECO:0000269|PubMed:17082223"
FT   MUTAGEN         1311
FT                   /note="Y->A: Deacreases ABCB11 internalization."
FT                   /evidence="ECO:0000269|PubMed:22262466"
SQ   SEQUENCE   1321 AA;  146258 MW;  5443F4EF7B9FB1F6 CRC64;
     MSDSVILRSV KKFGEENHAF ESDGSHNNDK KSRLQDKMKE GDIRVGFFEL FRFSSSKDIW
     LMLMGGVCAL LHGMAQPGIL IIFGIMTDIF IKYDIERQEL EIPGKACVNN TIVWINSSFH
     QNMTNGTVCG LVDIESEMIK FSGIYAGVGM TVLILGYFQI RLWVITGARQ IRRMRKIYFR
     RIMRMEIGWF DCTSVGELNS RFADDIEKIN DAIADQLAHF LQRMSTAMCG LLLGFYRGWK
     LTLVILAVSP LIGIGAAVIG LSIAKFTELE LKAYAKAGSI ADEVLSSIRT VAAFGGENKE
     VERYEKNLVF AQRWGIWKGM VMGFFTGYMW CLIFFCYALA FWYGSTLVLD EEEYTPGTLV
     QIFLCVILAA MNIGHASSCL EIFSTGCSAA TNIFQTIDRQ PVIDCMSGDG YKLDRIKGEI
     EFHNVTFHYP SRPDVKILDN LSMVIKPGET TALVGSSGAG KSTALQLIQR FYDPCEGMVT
     LDGHDIRSLN IRWLRDQIGI VEQEPVLFST TIAENIRFGR EDATMEDIVQ AAKDANAYNF
     IMALPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEARVQEA
     LNKIQHGHTI ISVAHRLSTV RAADVIIGFE HGVAVERGTH EELLERKGVY FMLVTLQSQG
     DNAHKETSIM GKDATEGGTL ERTFSRGSYR DSLRASIRQR SKSQLSLLTH DPPLAVADHK
     SSYKDSKDND VLVEEVEPAP VRRILKYNIP EWHYILVGSL SAAINGAVTP IYSLLFSQLL
     GTFSLLDKEQ QRSEIHSMCL FFVILGCVSI FTQFLQGYTF AKSGELLTKR LRKFGFKAML
     GQDIGWFDDL RNNPGVLTTR LATDASQVQG ATGSQVGMMV NSFTNIIAAL LIAFFFSWKL
     SLIITIFFPF LALSGAVQTK MLTGFASQDK QALEKAGQIT SEALSNIRTV AGIGVEGRFI
     KAFEVELQTS YKTAVRKANI YGLCFAFSQG IAFLANSAAY RYGGYLIAYE GLGFSHVFRV
     VSSVALSATA VGRTFSYTPS YAKAKISAAR FFQLLDRKPP INVYSEAGEK WDNFQGKIDF
     IDCKFTYPSR PDIQVLNGLS VSVNPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGTVMID
     GHDSKKVNIQ FLRSNIGIVS QEPVLFDCSI MDNIKYGDNT KEISVERAIA AAKQAQLHDF
     VMSLPEKYET NVGIQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQTA
     LDKAREGRTC IVIAHRLSTI QNSDIIAVVS QGVVIEKGTH EKLMAQKGAY YKLVITGAPI
     S
//