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O70127 (ABCBB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bile salt export pump
Alternative name(s):
ATP-binding cassette sub-family B member 11
Sister of P-glycoprotein
Gene names
Name:Abcb11
Synonyms:Bsep, Spgp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes.

Subunit structure

Interacts with HAX1. Ref.2

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed predominantly, if not exclusively in the liver, where it was further localized to the canalicular microvilli and to subcanalicular vesicles of the hepatocytes by in situ.

Domain

Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanalicular bile acid transport

Inferred from direct assay Ref.1. Source: RGD

drug export

Inferred from direct assay PubMed 15901796. Source: RGD

drug transmembrane transport

Inferred from direct assay PubMed 15901796. Source: GOC

response to drug

Inferred from mutant phenotype PubMed 15901796. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 12702498. Source: RGD

response to oxidative stress

Inferred from expression pattern PubMed 16452108. Source: RGD

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 14762791. Source: RGD

Golgi membrane

Inferred from direct assay PubMed 10748167. Source: RGD

apical plasma membrane

Inferred from direct assay PubMed 12370274. Source: RGD

integral component of membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

intercellular canaliculus

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from direct assay PubMed 12702498. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled to transmembrane movement of substances

Inferred from Biological aspect of Ancestor. Source: RefGenome

canalicular bile acid transmembrane transporter activity

Inferred from direct assay Ref.1. Source: RGD

drug transmembrane transporter activity

Inferred from direct assay PubMed 15901796. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hax1Q7TSE95EBI-930036,EBI-930005

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13211321Bile salt export pump
PRO_0000093299

Regions

Topological domain1 – 6262Cytoplasmic Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 14764Extracellular Potential
Transmembrane148 – 16821Helical; Potential
Topological domain169 – 21547Cytoplasmic Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 2404Extracellular Potential
Transmembrane241 – 26121Helical; Potential
Topological domain262 – 31958Cytoplasmic Potential
Transmembrane320 – 34021Helical; Potential
Topological domain341 – 35313Extracellular Potential
Transmembrane354 – 37421Helical; Potential
Topological domain375 – 755381Cytoplasmic Potential
Transmembrane756 – 77621Helical; Potential
Topological domain777 – 79418Extracellular Potential
Transmembrane795 – 81521Helical; Potential
Topological domain816 – 86954Cytoplasmic Potential
Transmembrane870 – 89021Helical; Potential
Transmembrane891 – 91121Helical; Potential
Topological domain912 – 97968Cytoplasmic Potential
Transmembrane980 – 100021Helical; Potential
Topological domain1001 – 101111Extracellular Potential
Transmembrane1012 – 103221Helical; Potential
Topological domain1033 – 1321289Cytoplasmic Potential
Domain62 – 385324ABC transmembrane type-1 1
Domain420 – 656237ABC transporter 1
Domain755 – 1043289ABC transmembrane type-1 2
Domain1078 – 1316239ABC transporter 2
Nucleotide binding455 – 4628ATP 1 Potential
Nucleotide binding1113 – 11208ATP 2 Potential
Region651 – 67424Interaction with HAX1

Amino acid modifications

Modified residue6921Phosphoserine By similarity
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1251N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O70127 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 5443F4EF7B9FB1F6

FASTA1,321146,258
        10         20         30         40         50         60 
MSDSVILRSV KKFGEENHAF ESDGSHNNDK KSRLQDKMKE GDIRVGFFEL FRFSSSKDIW 

        70         80         90        100        110        120 
LMLMGGVCAL LHGMAQPGIL IIFGIMTDIF IKYDIERQEL EIPGKACVNN TIVWINSSFH 

       130        140        150        160        170        180 
QNMTNGTVCG LVDIESEMIK FSGIYAGVGM TVLILGYFQI RLWVITGARQ IRRMRKIYFR 

       190        200        210        220        230        240 
RIMRMEIGWF DCTSVGELNS RFADDIEKIN DAIADQLAHF LQRMSTAMCG LLLGFYRGWK 

       250        260        270        280        290        300 
LTLVILAVSP LIGIGAAVIG LSIAKFTELE LKAYAKAGSI ADEVLSSIRT VAAFGGENKE 

       310        320        330        340        350        360 
VERYEKNLVF AQRWGIWKGM VMGFFTGYMW CLIFFCYALA FWYGSTLVLD EEEYTPGTLV 

       370        380        390        400        410        420 
QIFLCVILAA MNIGHASSCL EIFSTGCSAA TNIFQTIDRQ PVIDCMSGDG YKLDRIKGEI 

       430        440        450        460        470        480 
EFHNVTFHYP SRPDVKILDN LSMVIKPGET TALVGSSGAG KSTALQLIQR FYDPCEGMVT 

       490        500        510        520        530        540 
LDGHDIRSLN IRWLRDQIGI VEQEPVLFST TIAENIRFGR EDATMEDIVQ AAKDANAYNF 

       550        560        570        580        590        600 
IMALPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEARVQEA 

       610        620        630        640        650        660 
LNKIQHGHTI ISVAHRLSTV RAADVIIGFE HGVAVERGTH EELLERKGVY FMLVTLQSQG 

       670        680        690        700        710        720 
DNAHKETSIM GKDATEGGTL ERTFSRGSYR DSLRASIRQR SKSQLSLLTH DPPLAVADHK 

       730        740        750        760        770        780 
SSYKDSKDND VLVEEVEPAP VRRILKYNIP EWHYILVGSL SAAINGAVTP IYSLLFSQLL 

       790        800        810        820        830        840 
GTFSLLDKEQ QRSEIHSMCL FFVILGCVSI FTQFLQGYTF AKSGELLTKR LRKFGFKAML 

       850        860        870        880        890        900 
GQDIGWFDDL RNNPGVLTTR LATDASQVQG ATGSQVGMMV NSFTNIIAAL LIAFFFSWKL 

       910        920        930        940        950        960 
SLIITIFFPF LALSGAVQTK MLTGFASQDK QALEKAGQIT SEALSNIRTV AGIGVEGRFI 

       970        980        990       1000       1010       1020 
KAFEVELQTS YKTAVRKANI YGLCFAFSQG IAFLANSAAY RYGGYLIAYE GLGFSHVFRV 

      1030       1040       1050       1060       1070       1080 
VSSVALSATA VGRTFSYTPS YAKAKISAAR FFQLLDRKPP INVYSEAGEK WDNFQGKIDF 

      1090       1100       1110       1120       1130       1140 
IDCKFTYPSR PDIQVLNGLS VSVNPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGTVMID 

      1150       1160       1170       1180       1190       1200 
GHDSKKVNIQ FLRSNIGIVS QEPVLFDCSI MDNIKYGDNT KEISVERAIA AAKQAQLHDF 

      1210       1220       1230       1240       1250       1260 
VMSLPEKYET NVGIQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQTA 

      1270       1280       1290       1300       1310       1320 
LDKAREGRTC IVIAHRLSTI QNSDIIAVVS QGVVIEKGTH EKLMAQKGAY YKLVITGAPI 


S 

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References

[1]"The sister of P-glycoprotein represents the canalicular bile salt export pump of mammalian liver."
Gerloff T., Stieger B., Hagenbuch B., Madon J., Landmann L., Roth J., Hofmann A.F., Meier P.J.
J. Biol. Chem. 273:10046-10050(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells."
Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.
J. Biol. Chem. 279:32761-32770(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69487 mRNA. Translation: AAC40084.1.
PIRT42842.
RefSeqNP_113948.1. NM_031760.1.
UniGeneRn.14539.

3D structure databases

ProteinModelPortalO70127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO70127. 2 interactions.

Chemistry

BindingDBO70127.
ChEMBLCHEMBL2073674.

PTM databases

PhosphoSiteO70127.

Proteomic databases

PRIDEO70127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83569.
KEGGrno:83569.

Organism-specific databases

CTD8647.
RGD619930. Abcb11.

Phylogenomic databases

HOVERGENHBG080809.
KOK05664.
PhylomeDBO70127.

Gene expression databases

GenevestigatorO70127.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 3 hits.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio616061.
PROO70127.

Entry information

Entry nameABCBB_RAT
AccessionPrimary (citable) accession number: O70127
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families