ID NTCP2_HUMAN Reviewed; 348 AA. AC Q12908; A1L4F4; Q13839; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 08-FEB-2011, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Ileal sodium/bile acid cotransporter; DE AltName: Full=Apical sodium-dependent bile acid transporter; DE Short=ASBT; DE AltName: Full=Ileal Na(+)/bile acid cotransporter; DE AltName: Full=Ileal sodium-dependent bile acid transporter; DE Short=IBAT; DE Short=ISBT; DE AltName: Full=Na(+)-dependent ileal bile acid transporter; DE AltName: Full=Sodium/taurocholate cotransporting polypeptide, ileal; DE AltName: Full=Solute carrier family 10 member 2; GN Name=SLC10A2; Synonyms=ASBT, ISBT, NTCP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-171 AND SER-290, TRANSPORT RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Ileum; RX PubMed=7592981; DOI=10.1074/jbc.270.45.27228; RA Wong M.H., Oelkers P., Dawson P.A.; RT "Identification of a mutation in the ileal sodium-dependent bile acid RT transporter gene that abolishes transport activity."; RL J. Biol. Chem. 270:27228-27234(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORT ACTIVITY, TISSUE RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9458785; DOI=10.1152/ajpgi.1998.274.1.g157; RA Craddock A.L., Love M.W., Daniel R.W., Kirby L.C., Walters H.C., Wong M.H., RA Dawson P.A.; RT "Expression and transport properties of the human ileal and renal sodium- RT dependent bile acid transporter."; RL Am. J. Physiol. 274:G157-G169(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PBAM1 PRO-243 AND MET-262, AND RP VARIANT ALA-171. RX PubMed=9109432; DOI=10.1172/jci119355; RA Oelkers P., Kirby L.C., Heubi J.E., Dawson P.A.; RT "Primary bile acid malabsorption caused by mutations in the ileal sodium- RT dependent bile acid transporter gene (SLC10A2)."; RL J. Clin. Invest. 99:1880-1887(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-171. RX PubMed=12364586; DOI=10.1073/pnas.182412499; RA Chumakov I., Blumenfeld M., Guerassimenko O., Cavarec L., Palicio M., RA Abderrahim H., Bougueleret L., Barry C., Tanaka H., La Rosa P., Puech A., RA Tahri N., Cohen-Akenine A., Delabrosse S., Lissarrague S., Picard F.-P., RA Maurice K., Essioux L., Millasseau P., Grel P., Debailleul V., Simon A.-M., RA Caterina D., Dufaure I., Malekzadeh K., Belova M., Luan J.-J., Bouillot M., RA Sambucy J.-L., Primas G., Saumier M., Boubkiri N., Martin-Saumier S., RA Nasroune M., Peixoto H., Delaye A., Pinchot V., Bastucci M., Guillou S., RA Chevillon M., Sainz-Fuertes R., Meguenni S., Aurich-Costa J., Cherif D., RA Gimalac A., Van Duijn C., Gauvreau D., Ouellette G., Fortier I., RA Raelson J., Sherbatich T., Riazanskay N., Rogaev E., Raeymaekers P., RA Aerssens J., Konings F., Luyten W., Macciardi F., Sham P.C., Straub R.E., RA Weinberger D.R., Cohen N., Cohen D.; RT "Genetic and physiological data implicating the new human gene G72 and the RT gene for D-amino acid oxidase in schizophrenia."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13675-13680(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-171. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-171. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. RC TISSUE=Blood; RA Stengelin S., Becker W., Maier M., Rosenberger J., Kramer W.; RT "Human ileal sodium-dependent bile acid transporter gene (promoter, exon 1 RT and intron 1)."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, TRANSPORT ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9856990; DOI=10.1074/jbc.273.52.34691; RA Weinman S.A., Carruth M.W., Dawson P.A.; RT "Bile acid uptake via the human apical sodium-bile acid cotransporter is RT electrogenic."; RL J. Biol. Chem. 273:34691-34695(1998). RN [10] RP GLYCOSYLATION AT ASN-10, MUTAGENESIS OF ASN-10 AND ASN-328, AND TOPOLOGY. RX PubMed=15350125; DOI=10.1021/bi049270a; RA Zhang E.Y., Phelps M.A., Banerjee A., Khantwal C.M., Chang C., Helsper F., RA Swaan P.W.; RT "Topology scanning and putative three-dimensional structure of the RT extracellular binding domains of the apical sodium-dependent bile acid RT transporter (SLC10A2)."; RL Biochemistry 43:11380-11392(2004). RN [11] RP FUNCTION. RX PubMed=33222321; DOI=10.1002/hep.31651; RA Kunst R.F., Verkade H.J., Oude Elferink R.P.J., van de Graaf S.F.J.; RT "Targeting the Four Pillars of Enterohepatic Bile Salt Cycling; Lessons RT From Genetics and Pharmacology."; RL Hepatology 73:2577-2585(2021). RN [12] RP VARIANTS ILE-98; ILE-159 AND ALA-171. RX PubMed=11742882; DOI=10.1161/hq1201.100262; RA Love M.W., Craddock A.L., Angelin B., Brunzell J.D., Duane W.C., RA Dawson P.A.; RT "Analysis of the ileal bile acid transporter gene, SLC10A2, in subjects RT with familial hypertriglyceridemia."; RL Arterioscler. Thromb. Vasc. Biol. 21:2039-2045(2001). RN [13] RP VARIANTS ILE-98 AND ALA-171. RX PubMed=11589382; DOI=10.1080/003655201750422693; RA Montagnani M., Love M.W., Rossel P., Dawson P.A., Qvist P.; RT "Absence of dysfunctional ileal sodium-bile acid cotransporter gene RT mutations in patients with adult-onset idiopathic bile acid RT malabsorption."; RL Scand. J. Gastroenterol. 36:1077-1080(2001). CC -!- FUNCTION: Plays a critical role in the sodium-dependent reabsorption of CC bile acids from the lumen of the small intestine (PubMed:7592981, CC PubMed:9458785, PubMed:9856990). Transports various bile acids, CC unconjugated or conjugated, such as cholate and taurocholate CC (PubMed:7592981, PubMed:9458785, PubMed:9856990). Also responsible for CC bile acid transport in the renal proximal tubules, a salvage mechanism CC that helps conserve bile acids (Probable). Works collaboratively with CC the Na(+)-taurocholate cotransporting polypeptide (NTCP), the organic CC solute transporter (OST), and the bile salt export pump (BSEP), to CC ensure efficacious biological recycling of bile acids during CC enterohepatic circulation (PubMed:33222321). CC {ECO:0000269|PubMed:7592981, ECO:0000269|PubMed:9458785, CC ECO:0000269|PubMed:9856990, ECO:0000303|PubMed:33222321, CC ECO:0000305|PubMed:9458785}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + CC taurocholate(in); Xref=Rhea:RHEA:71875, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:7592981, CC ECO:0000269|PubMed:9458785, ECO:0000269|PubMed:9856990}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cholate(out) + 2 Na(+)(out) = cholate(in) + 2 Na(+)(in); CC Xref=Rhea:RHEA:71911, ChEBI:CHEBI:29101, ChEBI:CHEBI:29747; CC Evidence={ECO:0000269|PubMed:9458785, ECO:0000269|PubMed:9856990}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + taurochenodeoxycholate(out) = 2 Na(+)(in) + CC taurochenodeoxycholate(in); Xref=Rhea:RHEA:71923, ChEBI:CHEBI:9407, CC ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + tauroursodeoxycholate(out) = 2 Na(+)(in) + CC tauroursodeoxycholate(in); Xref=Rhea:RHEA:71927, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:132028; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycocholate(out) + 2 Na(+)(out) = glycocholate(in) + 2 CC Na(+)(in); Xref=Rhea:RHEA:71935, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + tauronorcholate(out) = 2 Na(+)(in) + CC tauronorcholate(in); Xref=Rhea:RHEA:71915, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:191405; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + tauroallocholate(out) = 2 Na(+)(in) + CC tauroallocholate(in); Xref=Rhea:RHEA:51840, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:191406; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + taurodeoxycholate(out) = 2 Na(+)(in) + CC taurodeoxycholate(in); Xref=Rhea:RHEA:72087, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:36261; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + tauro-beta-muricholate(out) = 2 Na(+)(in) + CC tauro-beta-muricholate(in); Xref=Rhea:RHEA:72179, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:133064; Evidence={ECO:0000250|UniProtKB:Q28727}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=17 uM for taurocholate {ECO:0000269|PubMed:7592981}; CC KM=13.3 uM for taurocholate {ECO:0000269|PubMed:9458785}; CC KM=12 uM for taurocholate {ECO:0000269|PubMed:9856990}; CC KM=33.3 uM for cholate {ECO:0000269|PubMed:9458785}; CC KM=37 uM for cholate {ECO:0000269|PubMed:9856990}; CC KM=2 uM for glycodeoxycholate {ECO:0000269|PubMed:9458785}; CC KM=5.7 uM for glycochenodeoxycholate {ECO:0000269|PubMed:9458785}; CC KM=4.1 uM for glycoursodeoxycholate {ECO:0000269|PubMed:9458785}; CC Vmax=96 pmol/min/mg enzyme with taurocholate as substrate CC {ECO:0000269|PubMed:7592981}; CC Vmax=48 pmol/min/mg enzyme with taurocholate as substrate CC {ECO:0000269|PubMed:9458785}; CC -!- SUBUNIT: Monomer and homodimer. CC -!- INTERACTION: CC Q12908; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-18114847, EBI-10271156; CC Q12908; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-18114847, EBI-12019274; CC Q12908; P52803: EFNA5; NbExp=3; IntAct=EBI-18114847, EBI-1753674; CC Q12908; Q01628: IFITM3; NbExp=3; IntAct=EBI-18114847, EBI-7932862; CC Q12908; Q8IXM6: NRM; NbExp=3; IntAct=EBI-18114847, EBI-10262547; CC Q12908; Q9NZ42: PSENEN; NbExp=3; IntAct=EBI-18114847, EBI-998468; CC Q12908; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-18114847, EBI-10329860; CC Q12908; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-18114847, EBI-347385; CC Q12908; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-18114847, EBI-10243654; CC Q12908; O75841: UPK1B; NbExp=3; IntAct=EBI-18114847, EBI-12237619; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Mainly expressed in ileum and kidney, lower CC expression in cecum. {ECO:0000269|PubMed:9458785}. CC -!- DISEASE: Bile acid malabsorption, primary, 1 (PBAM1) [MIM:613291]: An CC autosomal recessive intestinal disorder associated with chronic watery CC diarrhea, excess fecal bile acids, steatorrhea and interruption of the CC enterohepatic circulation of bile acids. {ECO:0000269|PubMed:9109432}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) CC (TC 2.A.28) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10417; AAC51870.1; -; mRNA. DR EMBL; U67674; AAC95398.1; -; Genomic_DNA. DR EMBL; U67669; AAC95398.1; JOINED; Genomic_DNA. DR EMBL; U67670; AAC95398.1; JOINED; Genomic_DNA. DR EMBL; U67671; AAC95398.1; JOINED; Genomic_DNA. DR EMBL; U67672; AAC95398.1; JOINED; Genomic_DNA. DR EMBL; U67673; AAC95398.1; JOINED; Genomic_DNA. DR EMBL; AE014294; AAN16026.1; -; Genomic_DNA. DR EMBL; AL161771; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX09074.1; -; Genomic_DNA. DR EMBL; BC130521; AAI30522.1; -; mRNA. DR EMBL; BC130523; AAI30524.1; -; mRNA. DR EMBL; Z54350; CAA91161.1; -; Genomic_DNA. DR CCDS; CCDS9506.1; -. DR PIR; I38655; I38655. DR RefSeq; NP_000443.1; NM_000452.2. DR AlphaFoldDB; Q12908; -. DR SMR; Q12908; -. DR BioGRID; 112444; 12. DR IntAct; Q12908; 11. DR STRING; 9606.ENSP00000245312; -. DR BindingDB; Q12908; -. DR ChEMBL; CHEMBL2778; -. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB02659; Cholic Acid. DR DrugBank; DB00091; Cyclosporine. DR DrugBank; DB03619; Deoxycholic acid. DR DrugBank; DB02123; Glycochenodeoxycholic Acid. DR DrugBank; DB09237; Levamlodipine. DR DrugBank; DB16226; Maralixibat. DR DrugBank; DB16261; Odevixibat. DR DrugBank; DB04348; Taurocholic acid. DR DrugBank; DB01586; Ursodeoxycholic acid. DR DrugBank; DB00577; Valaciclovir. DR DrugBank; DB13914; Volixibat. DR DrugCentral; Q12908; -. DR GuidetoPHARMACOLOGY; 960; -. DR TCDB; 2.A.28.1.2; the bile acid:na(+) symporter (bass) family. DR GlyCosmos; Q12908; 1 site, No reported glycans. DR GlyGen; Q12908; 1 site. DR iPTMnet; Q12908; -. DR PhosphoSitePlus; Q12908; -. DR SwissPalm; Q12908; -. DR BioMuta; SLC10A2; -. DR DMDM; 322510055; -. DR MassIVE; Q12908; -. DR PaxDb; 9606-ENSP00000245312; -. DR PeptideAtlas; Q12908; -. DR Antibodypedia; 11241; 241 antibodies from 31 providers. DR DNASU; 6555; -. DR Ensembl; ENST00000245312.5; ENSP00000245312.3; ENSG00000125255.7. DR GeneID; 6555; -. DR KEGG; hsa:6555; -. DR MANE-Select; ENST00000245312.5; ENSP00000245312.3; NM_000452.3; NP_000443.2. DR UCSC; uc001vpy.4; human. DR AGR; HGNC:10906; -. DR CTD; 6555; -. DR DisGeNET; 6555; -. DR GeneCards; SLC10A2; -. DR HGNC; HGNC:10906; SLC10A2. DR HPA; ENSG00000125255; Tissue enriched (intestine). DR MalaCards; SLC10A2; -. DR MIM; 601295; gene. DR MIM; 613291; phenotype. DR neXtProt; NX_Q12908; -. DR OpenTargets; ENSG00000125255; -. DR Orphanet; 449262; NON RARE IN EUROPE: Primary bile acid malabsorption. DR PharmGKB; PA318; -. DR VEuPathDB; HostDB:ENSG00000125255; -. DR eggNOG; KOG2718; Eukaryota. DR GeneTree; ENSGT00950000182808; -. DR HOGENOM; CLU_034788_7_5_1; -. DR InParanoid; Q12908; -. DR OMA; AHYVIMP; -. DR OrthoDB; 3035577at2759; -. DR PhylomeDB; Q12908; -. DR TreeFam; TF315811; -. DR PathwayCommons; Q12908; -. DR Reactome; R-HSA-159418; Recycling of bile acids and salts. DR SignaLink; Q12908; -. DR BioGRID-ORCS; 6555; 6 hits in 1140 CRISPR screens. DR GeneWiki; SLC10A2; -. DR GenomeRNAi; 6555; -. DR Pharos; Q12908; Tclin. DR PRO; PR:Q12908; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q12908; Protein. DR Bgee; ENSG00000125255; Expressed in ileal mucosa and 35 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008508; F:bile acid:sodium symporter activity; IBA:GO_Central. DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR Gene3D; 1.20.1530.20; -; 1. DR InterPro; IPR002657; BilAc:Na_symport/Acr3. DR InterPro; IPR004710; Bilac:Na_transpt. DR InterPro; IPR038770; Na+/solute_symporter_sf. DR NCBIfam; TIGR00841; bass; 1. DR PANTHER; PTHR10361:SF19; ILEAL SODIUM_BILE ACID COTRANSPORTER; 1. DR PANTHER; PTHR10361; SODIUM-BILE ACID COTRANSPORTER; 1. DR Pfam; PF01758; SBF; 1. DR Genevisible; Q12908; HS. PE 1: Evidence at protein level; KW Disease variant; Glycoprotein; Ion transport; Lipid transport; Membrane; KW Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..348 FT /note="Ileal sodium/bile acid cotransporter" FT /id="PRO_0000052339" FT TOPO_DOM 1..28 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 50..82 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 104..126 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 127..147 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 148..157 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 158..178 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 179..195 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 217..224 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 246..284 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 285..305 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 306..348 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 320..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 328 FT /note="Not glycosylated" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P70172" FT CARBOHYD 10 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15350125" FT VARIANT 98 FT /note="V -> I (in dbSNP:rs55971546)" FT /evidence="ECO:0000269|PubMed:11589382, FT ECO:0000269|PubMed:11742882" FT /id="VAR_024837" FT VARIANT 159 FT /note="V -> I (in dbSNP:rs60380298)" FT /evidence="ECO:0000269|PubMed:11742882" FT /id="VAR_024838" FT VARIANT 171 FT /note="S -> A (in dbSNP:rs188096)" FT /evidence="ECO:0000269|PubMed:11589382, FT ECO:0000269|PubMed:11742882, ECO:0000269|PubMed:12364586, FT ECO:0000269|PubMed:15057823, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7592981, ECO:0000269|PubMed:9109432" FT /id="VAR_004613" FT VARIANT 243 FT /note="L -> P (in PBAM1; abolishes taurocholate transport; FT dbSNP:rs121917848)" FT /evidence="ECO:0000269|PubMed:9109432" FT /id="VAR_004614" FT VARIANT 262 FT /note="T -> M (in PBAM1; abolishes taurocholate transport; FT dbSNP:rs72547505)" FT /evidence="ECO:0000269|PubMed:9109432" FT /id="VAR_004615" FT VARIANT 290 FT /note="P -> S (found in a patient with Crohn disease; FT abolishes taurocholate transport; dbSNP:rs56398830)" FT /evidence="ECO:0000269|PubMed:7592981" FT /id="VAR_004616" FT MUTAGEN 10 FT /note="N->D: Abolishes glycosylation." FT /evidence="ECO:0000269|PubMed:15350125" FT MUTAGEN 328 FT /note="N->D: No effect on glycosylation." FT /evidence="ECO:0000269|PubMed:15350125" SQ SEQUENCE 348 AA; 37714 MW; 9794EAA77C3EC4F9 CRC64; MNDPNSCVDN ATVCSGASCV VPESNFNNIL SVVLSTVLTI LLALVMFSMG CNVEIKKFLG HIKRPWGICV GFLCQFGIMP LTGFILSVAF DILPLQAVVV LIIGCCPGGT ASNILAYWVD GDMDLSVSMT TCSTLLALGM MPLCLLIYTK MWVDSGSIVI PYDNIGTSLV SLVVPVSIGM FVNHKWPQKA KIILKIGSIA GAILIVLIAV VGGILYQSAW IIAPKLWIIG TIFPVAGYSL GFLLARIAGL PWYRCRTVAF ETGMQNTQLC STIVQLSFTP EELNVVFTFP LIYSIFQLAF AAIFLGFYVA YKKCHGKNKA EIPESKENGT EPESSFYKAN GGFQPDEK //