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Bile salt export pump (ATP-binding cassette sub-family B member 11) (Sister of P-glycoprotein)

 ABCBB_RAT               Reviewed;        1321 AA.
O70127;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Bile salt export pump;
AltName: Full=ATP-binding cassette sub-family B member 11;
AltName: Full=Sister of P-glycoprotein;
Name=Abcb11; Synonyms=Bsep, Spgp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9545351; DOI=10.1074/jbc.273.16.10046;
Gerloff T., Stieger B., Hagenbuch B., Madon J., Landmann L., Roth J.,
Hofmann A.F., Meier P.J.;
"The sister of P-glycoprotein represents the canalicular bile salt
export pump of mammalian liver.";
J. Biol. Chem. 273:10046-10050(1998).
[2]
INTERACTION WITH HAX1.
PubMed=15159385; DOI=10.1074/jbc.M404337200;
Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.;
"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.";
J. Biol. Chem. 279:32761-32770(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703; SER-706 AND
SER-1321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Involved in the ATP-dependent secretion of bile salts
into the canaliculus of hepatocytes.
-!- SUBUNIT: Interacts with HAX1. {ECO:0000269|PubMed:15159385}.
-!- INTERACTION:
Q7TSE9:Hax1; NbExp=5; IntAct=EBI-930036, EBI-930005;
-!- 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.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
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EMBL; U69487; AAC40084.1; -; mRNA.
PIR; T42842; T42842.
RefSeq; NP_113948.1; NM_031760.1.
UniGene; Rn.14539; -.
ProteinModelPortal; O70127; -.
SMR; O70127; -.
BioGrid; 249756; 1.
IntAct; O70127; 2.
STRING; 10116.ENSRNOP00000064279; -.
BindingDB; O70127; -.
ChEMBL; CHEMBL2073674; -.
SwissLipids; SLP:000001598; -.
iPTMnet; O70127; -.
PhosphoSitePlus; O70127; -.
PaxDb; O70127; -.
PRIDE; O70127; -.
GeneID; 83569; -.
KEGG; rno:83569; -.
CTD; 8647; -.
RGD; 619930; Abcb11.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
HOVERGEN; HBG080809; -.
InParanoid; O70127; -.
KO; K05664; -.
PhylomeDB; O70127; -.
PRO; PR:O70127; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0015126; F:canalicular bile acid transmembrane transporter activity; IDA:RGD.
GO; GO:0015238; F:drug transmembrane transporter activity; IDA:RGD.
GO; GO:0015722; P:canalicular bile acid transport; IDA:RGD.
GO; GO:0046618; P:drug export; IDA:RGD.
GO; GO:0042493; P:response to drug; IMP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030278; BSEP.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24221:SF165; PTHR24221:SF165; 3.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 3.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Glycoprotein; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1321 Bile salt export pump.
/FTId=PRO_0000093299.
TOPO_DOM 1 62 Cytoplasmic. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 84 147 Extracellular. {ECO:0000255}.
TRANSMEM 148 168 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 169 215 Cytoplasmic. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 237 240 Extracellular. {ECO:0000255}.
TRANSMEM 241 261 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 262 319 Cytoplasmic. {ECO:0000255}.
TRANSMEM 320 340 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 341 353 Extracellular. {ECO:0000255}.
TRANSMEM 354 374 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 375 755 Cytoplasmic. {ECO:0000255}.
TRANSMEM 756 776 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 777 794 Extracellular. {ECO:0000255}.
TRANSMEM 795 815 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 816 869 Cytoplasmic. {ECO:0000255}.
TRANSMEM 870 890 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TRANSMEM 891 911 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 912 979 Cytoplasmic. {ECO:0000255}.
TRANSMEM 980 1000 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1001 1011 Extracellular. {ECO:0000255}.
TRANSMEM 1012 1032 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1033 1321 Cytoplasmic. {ECO:0000255}.
DOMAIN 62 385 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 420 656 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 755 1043 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1078 1316 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 455 462 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1113 1120 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 651 674 Interaction with HAX1.
{ECO:0000269|PubMed:15159385}.
MOD_RES 586 586 Phosphothreonine.
{ECO:0000250|UniProtKB:O95342}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000250|UniProtKB:O95342}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY30}.
MOD_RES 703 703 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1321 1321 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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