ID   NTCP2_MOUSE             Reviewed;         348 AA.
AC   P70172; Q8VI83; Q925U7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   27-MAR-2024, entry version 160.
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 {ECO:0000303|PubMed:10101301};
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=Ntcp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TRANSPORT ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=ICR;
RX   PubMed=10101301; DOI=10.1093/oxfordjournals.jbchem.a022358;
RA   Saeki T., Matoba K., Furukawa H., Kirifuji K., Kanamoto R., Iwami K.;
RT   "Characterization, cDNA cloning, and functional expression of mouse ileal
RT   sodium-dependent bile acid transporter.";
RL   J. Biochem. 125:846-851(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, AND VARIANTS VAL-29; SER-36; THR-40 AND ILE-178.
RC   STRAIN=C57BL/6J;
RA   Dawson P.A., Craddock A.L., Tietjen M.E., Haywood J.H.;
RT   "Disruption of the ileal bile acid transporter gene in mice.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE, AND VARIANTS VAL-29; SER-36; THR-40 AND ILE-178.
RC   STRAIN=NZB/BlNJ, and SM/J;
RA   Lyons M.A., Korstanje R., Li R., Sheehan S.M., Walsh K.A., Carey M.C.,
RA   Churchill G.A., Paigen B.;
RT   "New genetic determinants of cholesterol gallstone formation revealed in an
RT   intercross of mouse strains NZB and SM.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 1-125.
RA   Saeki T., Kirifuji K., Kanamoto R., Iwami K.;
RT   "Identification of transcription start sites in mouse ileal sodium-
RT   dependent bile acid transporter gene.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Plays a critical role in the sodium-dependent reabsorption of
CC       bile acids from the lumen of the small intestine (PubMed:10101301).
CC       Transports various bile acids, unconjugated or conjugated, such as
CC       cholate and taurocholate (PubMed:10101301). Also responsible for bile
CC       acid transport in the renal proximal tubules, a salvage mechanism that
CC       helps conserve bile acids. Works collaboratively with the Na(+)-
CC       taurocholate cotransporting polypeptide (NTCP), the organic solute
CC       transporter (OST), and the bile salt export pump (BSEP), to ensure
CC       efficacious biological recycling of bile acids during enterohepatic
CC       circulation (By similarity). {ECO:0000250|UniProtKB:Q12908,
CC       ECO:0000269|PubMed:10101301}.
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:10101301};
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:0000250|UniProtKB:Q12908};
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=37 uM for taurocholate {ECO:0000269|PubMed:10101301};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in ileum. {ECO:0000269|PubMed:10101301}.
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; AB002693; BAA19606.1; -; mRNA.
DR   EMBL; D87059; BAA13237.1; -; mRNA.
DR   EMBL; AF271073; AAK55514.1; -; Genomic_DNA.
DR   EMBL; AF266724; AAK55514.1; JOINED; Genomic_DNA.
DR   EMBL; AF266725; AAK55514.1; JOINED; Genomic_DNA.
DR   EMBL; AF266726; AAK55514.1; JOINED; Genomic_DNA.
DR   EMBL; AF266727; AAK55514.1; JOINED; Genomic_DNA.
DR   EMBL; AF266728; AAK55514.1; JOINED; Genomic_DNA.
DR   EMBL; AY529655; AAS20611.1; -; mRNA.
DR   EMBL; AB078635; BAB84081.1; -; Genomic_DNA.
DR   CCDS; CCDS22089.1; -.
DR   RefSeq; NP_035518.1; NM_011388.3.
DR   AlphaFoldDB; P70172; -.
DR   SMR; P70172; -.
DR   BioGRID; 203275; 1.
DR   STRING; 10090.ENSMUSP00000023835; -.
DR   BindingDB; P70172; -.
DR   ChEMBL; CHEMBL2073708; -.
DR   GlyCosmos; P70172; 2 sites, No reported glycans.
DR   GlyGen; P70172; 2 sites.
DR   iPTMnet; P70172; -.
DR   PhosphoSitePlus; P70172; -.
DR   jPOST; P70172; -.
DR   PaxDb; 10090-ENSMUSP00000023835; -.
DR   ProteomicsDB; 287831; -.
DR   Antibodypedia; 11241; 241 antibodies from 31 providers.
DR   DNASU; 20494; -.
DR   Ensembl; ENSMUST00000023835.3; ENSMUSP00000023835.2; ENSMUSG00000023073.3.
DR   GeneID; 20494; -.
DR   KEGG; mmu:20494; -.
DR   UCSC; uc009kub.1; mouse.
DR   AGR; MGI:1201406; -.
DR   CTD; 6555; -.
DR   MGI; MGI:1201406; Slc10a2.
DR   VEuPathDB; HostDB:ENSMUSG00000023073; -.
DR   eggNOG; KOG2718; Eukaryota.
DR   GeneTree; ENSGT00950000182808; -.
DR   HOGENOM; CLU_034788_7_5_1; -.
DR   InParanoid; P70172; -.
DR   OMA; AHYVIMP; -.
DR   OrthoDB; 3035577at2759; -.
DR   PhylomeDB; P70172; -.
DR   TreeFam; TF315811; -.
DR   Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR   BioGRID-ORCS; 20494; 1 hit in 80 CRISPR screens.
DR   PRO; PR:P70172; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P70172; Protein.
DR   Bgee; ENSMUSG00000023073; Expressed in proximal tubule and 35 other cell types or tissues.
DR   ExpressionAtlas; P70172; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005902; C:microvillus; IDA:MGI.
DR   GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR   GO; GO:0008508; F:bile acid:sodium symporter activity; ISO:MGI.
DR   GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
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; P70172; MM.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Lipid transport; Membrane; Phosphoprotein;
KW   Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..348
FT                   /note="Ileal sodium/bile acid cotransporter"
FT                   /id="PRO_0000052340"
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..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..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          328..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         29
FT                   /note="I -> V (in strain: NZB/BlNJ and C57BL/6)"
FT                   /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   VARIANT         36
FT                   /note="T -> S (in strain: NZB/BlNJ and C57BL/6)"
FT                   /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   VARIANT         40
FT                   /note="I -> T (in strain: NZB/BlNJ and C57BL/6)"
FT                   /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT   VARIANT         178
FT                   /note="F -> I (in strain: NZB/BlNJ and C57BL/6)"
FT                   /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
SQ   SEQUENCE   348 AA;  38134 MW;  D00B5E43431875D7 CRC64;
     MDNSSVCPPN ATVCEGDSCV VPESNFNAIL NTVMSTVLTI LLAMVMFSMG CNVEVHKFLG
     HIKRPWGIFV GFLCQFGIMP LTGFILSVAS GILPVQAVVV LIMGCCPGGT GSNILAYWID
     GDMDLSVSMT TCSTLLALGM MPLCLFVYTK MWVDSGTIVI PYDSIGISLV ALVIPVSFGM
     FVNHKWPQKA KIILKIGSIT GVILIVLIAV IGGILYQSAW IIEPKLWIIG TIFPIAGYSL
     GFFLARLAGQ PWYRCRTVAL ETGMQNTQLC STIVQLSFSP EDLNLVFTFP LIYTVFQLVF
     AAVILGIYVT YRKCYGKNDA EFLEKTDNEM DSRPSFDETN KGFQPDEK
//