UniProtKB - Q9N0V3 (ABCBB_RABIT)
Bile salt export pump
ABCB11
Functioni
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. Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts. Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion.
By similarityCatalytic activityi
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- ATP + glycochenodeoxycholate(in) + H2O = ADP + glycochenodeoxycholate(out) + H+ + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- ATP + H2O + taurochenodeoxycholate(in) = ADP + H+ + phosphate + taurochenodeoxycholate(out)By similarityThis reaction proceeds in the forwardBy similarity direction.
- ATP + glycoursodeoxycholate(in) + H2O = ADP + glycoursodeoxycholate(out) + H+ + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- ATP + H2O + tauroursodeoxycholate(in) = ADP + H+ + phosphate + tauroursodeoxycholate(out)By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H+ + phosphate + taurolithocholate 3-sulfate(out)By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
Activity regulationi
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 455 – 462 | ATP 1PROSITE-ProRule annotation | 8 | |
Nucleotide bindingi | 1113 – 1120 | ATP 2PROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ABC-type bile acid transporter activity Source: UniProtKB
- ABC-type xenobiotic transporter activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- bile acid transmembrane transporter activity Source: UniProtKB
- canalicular bile acid transmembrane transporter activity Source: UniProtKB
GO - Biological processi
- bile acid and bile salt transport Source: UniProtKB
- bile acid metabolic process Source: UniProtKB
- canalicular bile acid transport Source: UniProtKB
- cholesterol homeostasis Source: UniProtKB
- fatty acid metabolic process Source: UniProtKB
- lipid homeostasis Source: UniProtKB
- phospholipid homeostasis Source: UniProtKB
- positive regulation of bile acid secretion Source: UniProtKB
- protein ubiquitination Source: UniProtKB
- regulation of bile acid metabolic process Source: UniProtKB
- regulation of fatty acid beta-oxidation Source: UniProtKB
- xenobiotic export Source: UniProtKB
- xenobiotic metabolic process Source: UniProtKB
- xenobiotic transmembrane transport Source: UniProtKB
Keywordsi
Molecular function | Translocase |
Biological process | Lipid transport, Transport |
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Bile salt export pump1 Publication (EC:7.6.2.-By similarity)Alternative name(s): ATP-binding cassette sub-family B member 11 Sister of P-glycoprotein |
Gene namesi | Name:ABCB11By similarity Synonyms:BSEP1 Publication, SPGP1 Publication |
Organismi | Oryctolagus cuniculus (Rabbit) |
Taxonomic identifieri | 9986 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Apical cell membrane By similarity; Multi-pass membrane protein By similarity
- Cell membrane By similarity; Multi-pass membrane protein By similarity
Endosome
- Recycling endosome membrane By similarity; Multi-pass membrane protein By similarity
- Endosome By similarity
Note: Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2). 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. Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway. Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (By similarity). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (By similarity).By similarity
Endosome
- endosome Source: UniProtKB
- recycling endosome Source: UniProtKB
- recycling endosome membrane Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- intracellular canaliculus Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- cell surface Source: UniProtKB
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 62 | CytoplasmicSequence analysisAdd BLAST | 62 | |
Transmembranei | 63 – 83 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 84 – 147 | ExtracellularSequence analysisAdd BLAST | 64 | |
Transmembranei | 148 – 168 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 169 – 215 | CytoplasmicSequence analysisAdd BLAST | 47 | |
Transmembranei | 216 – 236 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 237 – 240 | ExtracellularSequence analysis | 4 | |
Transmembranei | 241 – 261 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 262 – 319 | CytoplasmicSequence analysisAdd BLAST | 58 | |
Transmembranei | 320 – 340 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 341 – 353 | ExtracellularSequence analysisAdd BLAST | 13 | |
Transmembranei | 354 – 374 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 375 – 755 | CytoplasmicSequence analysisAdd BLAST | 381 | |
Transmembranei | 756 – 776 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 777 – 794 | ExtracellularSequence analysisAdd BLAST | 18 | |
Transmembranei | 795 – 815 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 816 – 869 | CytoplasmicSequence analysisAdd BLAST | 54 | |
Transmembranei | 870 – 890 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Transmembranei | 891 – 911 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 912 – 979 | CytoplasmicSequence analysisAdd BLAST | 68 | |
Transmembranei | 980 – 1000 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 1001 – 1011 | ExtracellularSequence analysisAdd BLAST | 11 | |
Transmembranei | 1012 – 1032 | HelicalPROSITE-ProRule annotationAdd BLAST | 21 | |
Topological domaini | 1033 – 1321 | CytoplasmicSequence analysisAdd BLAST | 289 |
Keywords - Cellular componenti
Cell membrane, Endosome, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000093298 | 1 – 1321 | Bile salt export pumpAdd BLAST | 1321 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 109 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 116 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 122 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 125 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 586 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 587 | PhosphoserineBy similarity | 1 | |
Modified residuei | 690 | PhosphoserineBy similarity | 1 | |
Modified residuei | 701 | PhosphoserineBy similarity | 1 | |
Modified residuei | 704 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1214 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1321 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
PRIDEi | Q9N0V3 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Interacts with HAX1 (By similarity).
Interacts with the adapter protein complex 2 (AP-2) throught AP2A2 or AP2A1; this interaction regulates cell membrane expression of ABCB11 through its internalization in a clathrin-dependent manner and its subsequent degradation (By similarity).
By similarityProtein-protein interaction databases
STRINGi | 9986.ENSOCUP00000001184 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 62 – 385 | ABC transmembrane type-1 1PROSITE-ProRule annotationAdd BLAST | 324 | |
Domaini | 420 – 656 | ABC transporter 1PROSITE-ProRule annotationAdd BLAST | 237 | |
Domaini | 755 – 1043 | ABC transmembrane type-1 2PROSITE-ProRule annotationAdd BLAST | 289 | |
Domaini | 1078 – 1316 | ABC transporter 2PROSITE-ProRule annotationAdd BLAST | 239 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 651 – 672 | Interaction with HAX1By similarityAdd BLAST | 22 | |
Regioni | 659 – 735 | DisorderedSequence analysisAdd BLAST | 77 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 683 – 704 | Polar residuesSequence analysisAdd BLAST | 22 | |
Compositional biasi | 711 – 735 | Basic and acidic residuesSequence analysisAdd BLAST | 25 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0055, Eukaryota |
InParanoidi | Q9N0V3 |
Family and domain databases
Gene3Di | 1.20.1560.10, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR011527, ABC1_TM_dom IPR036640, ABC1_TM_sf IPR003439, ABC_transporter-like_ATP-bd IPR017871, ABC_transporter-like_CS IPR030278, BSEP IPR027417, P-loop_NTPase IPR039421, Type_1_exporter |
PANTHERi | PTHR24221, PTHR24221, 1 hit PTHR24221:SF165, PTHR24221:SF165, 1 hit |
Pfami | View protein in Pfam PF00664, ABC_membrane, 2 hits PF00005, ABC_tran, 2 hits |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits SSF90123, SSF90123, 2 hits |
PROSITEi | View protein in PROSITE PS50929, ABC_TM1F, 2 hits PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MSDSVILRSV KKFGEENHGF ESDGSYNNEK KSRLQDKKKS DSVRIGFFQL
60 70 80 90 100
FRFSSWTDIW LMCMGSLCAC IHGIAQPGVL LIFGTMTDVF IDYDTELQEL
110 120 130 140 150
KIPGKACVNN TIVWINSSLN QNVTNGTRCG LLDIESEMIR FAGYYAGIGI
160 170 180 190 200
AVLTTGYIQI CFWGIAAAHQ IQKMRKSYFR KIMRMGIGWV DCNSVGKLNT
210 220 230 240 250
PFSVDFNKIN DSSADQLAIF IQGMTSPIFG FLVGFSQWWK LTLVIISVSP
260 270 280 290 300
LIGLGAAIIG LSVSKFTDYE LKAYAKAGSV ADEVISSMRT VAAFGGEKKE
310 320 330 340 350
VERYEKNLVF AQRWGIRKGI VMGFFTGYMW CLIFFCYALA FWYGSKLVLE
360 370 380 390 400
EGEYSPGALV QIFLSVIIGA LNLGNASPCL EAFAAGRAAA SSIFETIDRK
410 420 430 440 450
PIIDCMSEDG YKLERIKGEI EFHNVTFHYP SRPEVKILNN LSMVIKPGEM
460 470 480 490 500
TALVGPSGAG KSTALQLIHR FYGPTEGMVT VESHDIRSSH IQWLRNQIGI
510 520 530 540 550
VEQEPVLFFH TIAEKIRYGR EDATMEDLIQ AAKEANAYNF IMDLPQQFDT
560 570 580 590 600
LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEAMVQEA
610 620 630 640 650
LSKTQHGHTI VSVAHRPATI RTADVIIGCE HGAAVERGTE EELLERKGVY
660 670 680 690 700
FALVTLQSQR NQGDQEENEK DATEDDIPEK TFSRGNYQDS LRASLRQRSK
710 720 730 740 750
SQLSYLAHEP PMAVEDHKST HEEDRKDKDL PAQEDIEPAS VRRIMKLNAP
760 770 780 790 800
EWPYMLLGSM GAAVNGAVTP LYAFLFSQIL GTFSLPDKEE QRSQINGICL
810 820 830 840 850
LFVTLGCVSF FTQFLQGYTF AKSGELLTKR LRKFGFRAML GQDIGWFDDL
860 870 880 890 900
RNSPGALTTR LATDASQVQG ATGSQIGMMV NSFTNVTVAM IIAFLFSWKL
910 920 930 940 950
TLGIVCFFPF LALSGALQTK MLTGFASRDK QALEKAGQIT SEALSNIRTV
960 970 980 990 1000
AGIGKERKFI ETFEAELEKP YKMAIKKANV YGLCFGFSQC ITFIANSASY
1010 1020 1030 1040 1050
RYGGYLISNE GLHFSYVFRV ISAVVLSATA LGRASSYTPS YAKAKISAAR
1060 1070 1080 1090 1100
FFQLLDRQPP INVYSSAGEK WDNFQGKIDF VDCKFTYPSR PDIQVLNGLS
1110 1120 1130 1140 1150
VSMSPRQTLA FVGSSGCGKS TSIQLLERFY DPDHGKVMID GHDSRKVNIQ
1160 1170 1180 1190 1200
FLRSNIGIVS QEPVLFACSI KDNIKYGDNT QEIPMERIIA AAKKAQVHDF
1210 1220 1230 1240 1250
VMSLPEKYET NVGSQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD
1260 1270 1280 1290 1300
TESEKTVQVA LDKAREGRTC IVIAHRLSTI QNSDIIAVMS QGMVIEKGTH
1310 1320
EELMVQKGAY YKLVTTGSPI S
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF249879 mRNA Translation: AAF65552.1 |
RefSeqi | NP_001075552.1, NM_001082083.1 |
Genome annotation databases
GeneIDi | 100008767 |
KEGGi | ocu:100008767 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF249879 mRNA Translation: AAF65552.1 |
RefSeqi | NP_001075552.1, NM_001082083.1 |
3D structure databases
AlphaFoldDBi | Q9N0V3 |
SMRi | Q9N0V3 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9986.ENSOCUP00000001184 |
Proteomic databases
PRIDEi | Q9N0V3 |
Genome annotation databases
GeneIDi | 100008767 |
KEGGi | ocu:100008767 |
Organism-specific databases
CTDi | 8647 |
Phylogenomic databases
eggNOGi | KOG0055, Eukaryota |
InParanoidi | Q9N0V3 |
Family and domain databases
Gene3Di | 1.20.1560.10, 1 hit 3.40.50.300, 2 hits |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR011527, ABC1_TM_dom IPR036640, ABC1_TM_sf IPR003439, ABC_transporter-like_ATP-bd IPR017871, ABC_transporter-like_CS IPR030278, BSEP IPR027417, P-loop_NTPase IPR039421, Type_1_exporter |
PANTHERi | PTHR24221, PTHR24221, 1 hit PTHR24221:SF165, PTHR24221:SF165, 1 hit |
Pfami | View protein in Pfam PF00664, ABC_membrane, 2 hits PF00005, ABC_tran, 2 hits |
SMARTi | View protein in SMART SM00382, AAA, 2 hits |
SUPFAMi | SSF52540, SSF52540, 2 hits SSF90123, SSF90123, 2 hits |
PROSITEi | View protein in PROSITE PS50929, ABC_TM1F, 2 hits PS00211, ABC_TRANSPORTER_1, 1 hit PS50893, ABC_TRANSPORTER_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | ABCBB_RABIT | |
Accessioni | Q9N0V3Primary (citable) accession number: Q9N0V3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 24, 2001 |
Last sequence update: | October 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 116 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families