Abcb11
entrez
83569
canonical
uniprot
O70127
canonical
ensembl
ENSRNOG00000050860
resolver
ensembl
ENSRNOG00055023634
resolver
ensembl
ENSRNOG00060003171
resolver
ensembl
ENSRNOG00065016450
resolver
ensp
ENSRNOP00000064279
resolver
ensp
ENSRNOP00055033081
resolver
ensp
ENSRNOP00060003888
resolver
ensp
ENSRNOP00065021530
resolver
enst
ENSRNOT00000075107
resolver
enst
ENSRNOT00055040726
resolver
enst
ENSRNOT00060005254
resolver
enst
ENSRNOT00065027401
resolver
genesymbol
Abcb11
resolver
genesymbol_syn
Bsep
resolver
genesymbol_syn
Spgp
resolver
uniprot
A0A2P1EA62
resolver
uniprot_entry
A0A2P1EA62_RAT
resolver
uniprot_entry
ABCBB_RAT
resolver
activity_regulation
ACTIVITY REGULATION: The uptake of taurocholate is inhibited by taurolithocholate sulfate with an IC(50) of 52.9 uM (PubMed:16332456). Pravastatin competitively inhibits the transport of taurocholic acid (PubMed:15901796, PubMed:18985798). Cyclosporin A, glibenclamide, rifampicin and troglitazonestrongly competitively inhibit the transport activity of taurocholate (PubMed:18985798). The canalicular transport activity of taurocholate is strongly dependent on canalicular membrane cholesterol content. The uptake of taurocholate is increased by short- and medium-chain fatty acids. Cholesterol increases transport capacity of taurocholate without affecting the affinity for the substrate (By similarity). {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:18985798}.
uniprot
proteins
amino_acid_sequence
MSDSVILRSVKKFGEENHAFESDGSHNNDKKSRLQDKMKEGDIRVGFFELFRFSSSKDIWLMLMGGVCALLHGMAQPGILIIFGIMTDIFIKYDIERQELEIPGKACVNNTIVWINSSFHQNMTNGTVCGLVDIESEMIKFSGIYAGVGMTVLILGYFQIRLWVITGARQIRRMRKIYFRRIMRMEIGWFDCTSVGELNSRFADDIEKINDAIADQLAHFLQRMSTAMCGLLLGFYRGWKLTLVILAVSPLIGIGAAVIGLSIAKFTELELKAYAKAGSIADEVLSSIRTVAAFGGENKEVERYEKNLVFAQRWGIWKGMVMGFFTGYMWCLIFFCYALAFWYGSTLVLDEEEYTPGTLVQIFLCVILAAMNIGHASSCLEIFSTGCSAATNIFQTIDRQPVIDCMSGDGYKLDRIKGEIEFHNVTFHYPSRPDVKILDNLSMVIKPGETTALVGSSGAGKSTALQLIQRFYDPCEGMVTLDGHDIRSLNIRWLRDQIGIVEQEPVLFSTTIAENIRFGREDATMEDIVQAAKDANAYNFIMALPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEARVQEALNKIQHGHTIISVAHRLSTVRAADVIIGFEHGVAVERGTHEELLERKGVYFMLVTLQSQGDNAHKETSIMGKDATEGGTLERTFSRGSYRDSLRASIRQRSKSQLSLLTHDPPLAVADHKSSYKDSKDNDVLVEEVEPAPVRRILKYNIPEWHYILVGSLSAAINGAVTPIYSLLFSQLLGTFSLLDKEQQRSEIHSMCLFFVILGCVSIFTQFLQGYTFAKSGELLTKRLRKFGFKAMLGQDIGWFDDLRNNPGVLTTRLATDASQVQGATGSQVGMMVNSFTNIIAALLIAFFFSWKLSLIITIFFPFLALSGAVQTKMLTGFASQDKQALEKAGQITSEALSNIRTVAGIGVEGRFIKAFEVELQTSYKTAVRKANIYGLCFAFSQGIAFLANSAAYRYGGYLIAYEGLGFSHVFRVVSSVALSATAVGRTFSYTPSYAKAKISAARFFQLLDRKPPINVYSEAGEKWDNFQGKIDFIDCKFTYPSRPDIQVLNGLSVSVNPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGTVMIDGHDSKKVNIQFLRSNIGIVSQEPVLFDCSIMDNIKYGDNTKEISVERAIAAAKQAQLHDFVMSLPEKYETNVGIQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQTALDKAREGRTCIVIAHRLSTIQNSDIIAVVSQGVVIEKGTHEKLMAQKGAYYKLVITGAPIS
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
function
FUNCTION: Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner (PubMed:15901796, PubMed:16332456, PubMed:17082223, PubMed:18985798, PubMed:9545351). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts (PubMed:16332456). Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (PubMed:15901796, PubMed:18245269). {ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:18245269, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:9545351}.
uniprot
proteins
mass_dalton
146258
uniprot
proteins
mutagenesis
MUTAGEN 109; /note="N->Q: Impairs N-glycosylation; when associated with Q-116; Q-122 and Q-125. Significantly decreases taurocholate; when associated with Q-116; Q-122 and Q-125. Significantly decreases protein expression; when associated with Q-116; Q-122 and Q-125. Affects protein localization at the apical membrane; when associated with Q-116; Q-122 and Q-125. Does not affect protein localization at the apical membrane."; /evidence="ECO:0000269|PubMed:17082223"; MUTAGEN 116; /note="N->Q: Impairs N-glycosylation; when associated with Q-109; Q-122 and Q-125. Significantly decreases taurocholate; when associated with Q-109; Q-122 and Q-125. Significantly decreases protein expression; when associated with Q-109; Q-122 and Q-125. Affects protein localization at the apical membrane; when associated with Q-109; Q-122 and Q-125. Does not affect protein localization at the apical membrane; when associated with Q-109; Q-122 and Q-125."; /evidence="ECO:0000269|PubMed:17082223"; MUTAGEN 122; /note="N->Q: Impairs N-glycosylation; when associated with Q-109; Q-116 and Q-125. Significantly decreases taurocholate; when associated with Q-109; Q-116 and Q-125. Significantly decreases protein expression; when associated with Q-109; Q-116 and Q-125. Affects protein localization at the apical membrane; when associated with Q-109; Q-116 and Q-125."; /evidence="ECO:0000269|PubMed:17082223"; MUTAGEN 125; /note="N->Q: Impairs N-glycosylation; when associated with Q-109; Q-116 and Q-122. Significantly decreases taurocholate; when associated with Q-109; Q-116 and Q-122. Significantly decreases protein expression; when associated with Q-109; Q-116 and Q-122. Affects protein localization at the apical membrane;when associated with Q-109; Q-116 and Q-122."; /evidence="ECO:0000269|PubMed:17082223"; MUTAGEN 1311; /note="Y->A: Decreases ABCB11 internalization."; /evidence="ECO:0000269|PubMed:22262466
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface expression of ABCB11. {ECO:0000269|PubMed:18829893}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O95342}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCB family
uniprot
proteins
protein_family
Multidrug resistance exporter (TC 3.A.1.201) subfamily
uniprot
proteins
pubmed
11113123
uniprot
proteins
pubmed
15121884
uniprot
proteins
pubmed
15159385
uniprot
proteins
pubmed
15901796
uniprot
proteins
pubmed
16332456
uniprot
proteins
pubmed
17082223
uniprot
proteins
pubmed
18245269
uniprot
proteins
pubmed
18829893
uniprot
proteins
pubmed
18985798
uniprot
proteins
pubmed
22262466
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24643070
uniprot
proteins
pubmed
9545351
uniprot
proteins
sequence_length
1321
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:17082223, ECO:0000269|PubMed:9545351}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:15121884}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:11113123}. Cell membrane {ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24643070}; Multi-pass membrane protein {ECO:0000255}. Note=Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2) (PubMed:22262466). At steady state, localizes in the canalicular membrane but is also present in recycling endosomes. ABCB11 constantly and rapidly exchanges between the two sites through tubulo-vesicles carriers that move along microtubules (PubMed:11113123, PubMed:15121884). Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway (PubMed:11113123, PubMed:24643070). Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (PubMed:11113123). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (By similarity). {ECO:0000250|UniProtKB:O95342, ECO:0000269|PubMed:11113123, ECO:0000269|PubMed:15121884, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24643070}.
uniprot
proteins
transmembrane_region
TRANSMEM 63..83; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 216..236; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 241..261; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 320..340; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 354..374; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 756..776; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 795..815; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 870..890; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 891..911; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 980..1000; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 1012..1032; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins