ABCBB_RAT
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 03-AUG-2022, entry version 151.
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},
GN Spgp {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 GlyGen; O70127; 4 sites.
DR iPTMnet; O70127; -.
DR PhosphoSitePlus; O70127; -.
DR PaxDb; O70127; -.
DR PRIDE; O70127; -.
DR Ensembl; ENSRNOT00000075107; ENSRNOP00000064279; ENSRNOG00000050860.
DR GeneID; 83569; -.
DR KEGG; rno:83569; -.
DR CTD; 8647; -.
DR RGD; 619930; Abcb11.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000157564; -.
DR InParanoid; O70127; -.
DR OrthoDB; 186078at2759; -.
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:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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: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; 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:0010468; P:regulation of gene expression; IEP:RGD.
DR GO; GO:1904486; P:response to 17alpha-ethynylestradiol; IEP:RGD.
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 Gene3D; 1.20.1560.10; -; 3.
DR Gene3D; 3.40.50.300; -; 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; 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_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 Q-
FT 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
