##gff-version 3 O70127 UniProtKB Chain 1 1321 . . . ID=PRO_0000093299;Note=Bile salt export pump O70127 UniProtKB Topological domain 1 62 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 63 83 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 84 147 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 148 168 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 169 215 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 216 236 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 237 240 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 241 261 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 262 319 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 320 340 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 341 353 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 354 374 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 375 755 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 756 776 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 777 794 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 795 815 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 816 869 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 870 890 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Transmembrane 891 911 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 912 979 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 980 1000 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 1001 1011 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Transmembrane 1012 1032 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Topological domain 1033 1321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O70127 UniProtKB Domain 62 385 . . . Note=ABC transmembrane type-1 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Domain 420 656 . . . Note=ABC transporter 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O70127 UniProtKB Domain 755 1043 . . . Note=ABC transmembrane type-1 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00441 O70127 UniProtKB Domain 1078 1316 . . . Note=ABC transporter 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O70127 UniProtKB Region 651 674 . . . Note=Interaction with HAX1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15159385;Dbxref=PMID:15159385 O70127 UniProtKB Binding site 455 462 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O70127 UniProtKB Binding site 1113 1120 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00434 O70127 UniProtKB Modified residue 586 586 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95342 O70127 UniProtKB Modified residue 587 587 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95342 O70127 UniProtKB Modified residue 692 692 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9QY30 O70127 UniProtKB Modified residue 703 703 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O70127 UniProtKB Modified residue 706 706 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O70127 UniProtKB Modified residue 1321 1321 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 O70127 UniProtKB Glycosylation 109 109 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Glycosylation 116 116 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Glycosylation 122 122 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Glycosylation 125 125 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255,ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Mutagenesis 109 109 . . . Note=Impairs N-glycosylation%3B when associated with Q-116%3B Q-122 and Q-125. Significantly decreases taurocholate%3B when associated with Q-116%3B Q-122 and Q-125. Significantly decreases protein expression%3B when associated with Q-116%3B Q-122 and Q-125. Affects protein localization at the apical membrane%3B when associated with Q-116%3B Q-122 and Q-125. Does not affect protein localization at the apical membrane. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Mutagenesis 116 116 . . . Note=Impairs N-glycosylation%3B when associated with Q-109%3B Q-122 and Q-125. Significantly decreases taurocholate%3B when associated with Q-109%3B Q-122 and Q-125. Significantly decreases protein expression%3B when associated with Q-109%3B Q-122 and Q-125. Affects protein localization at the apical membrane%3B when associated with Q-109%3B Q-122 and Q-125. Does not affect protein localization at the apical membrane%3B when associated with Q-109%3B Q-122 and Q-125. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Mutagenesis 122 122 . . . Note=Impairs N-glycosylation%3B when associated with Q-109%3B Q-116 and Q-125. Significantly decreases taurocholate%3B when associated with Q-109%3B Q-116 and Q-125. Significantly decreases protein expression%3B when associated with Q-109%3B Q-116 and Q-125. Affects protein localization at the apical membrane%3B when associated with Q-109%3B Q-116 and Q-125. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Mutagenesis 125 125 . . . Note=Impairs N-glycosylation%3B when associated with Q-109%3B Q-116 and Q-122. Significantly decreases taurocholate%3B when associated with Q-109%3B Q-116 and Q-122. Significantly decreases protein expression%3B when associated with Q-109%3B Q-116 and Q-122. Affects protein localization at the apical membrane%3Bwhen associated with Q-109%3B Q-116 and Q-122. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17082223;Dbxref=PMID:17082223 O70127 UniProtKB Mutagenesis 1311 1311 . . . Note=Deacreases ABCB11 internalization. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22262466;Dbxref=PMID:22262466