SO1B2_MOUSE
ID SO1B2_MOUSE Reviewed; 689 AA.
AC Q9JJL3; Q9JI79; Q9JJJ1;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Solute carrier organic anion transporter family member 1B2;
DE AltName: Full=Liver-specific organic anion transporter 1;
DE Short=LST-1;
DE AltName: Full=SLC21A6;
DE AltName: Full=Solute carrier family 21 member 10;
GN Name=Slco1b2; Synonyms=Oatp1b2, Slc21a10;
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] (ISOFORM 1).
RC STRAIN=129/SvJ, and BALB/cJ; TISSUE=Liver;
RX PubMed=10833452; DOI=10.1006/bbrc.2000.2830;
RA Ogura K., Choudhuri S., Klaassen C.D.;
RT "Full-length cDNA cloning and genomic organization of the mouse liver-
RT specific organic anion transporter-1 (lst-1).";
RL Biochem. Biophys. Res. Commun. 272:563-570(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 245-689 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Ananthnarayanan M., Balasubramanian N.V.;
RT "Molecular cloning of mouse hepatic liver-specific transporter (lst-1/oatp-
RT c/slc21a6).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290 AND THR-662, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND THR-662, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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: Mediates the Na(+)-independent uptake of organic anions such
CC as taurochlate, bromosulfophthalein and steroid conjugates such as
CC estrone-3-sulfate, 17-beta-glucuronosyl estradiol,
CC dehydroepiandrosterone sulfate and prostaglandin E2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JJL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJL3-2; Sequence=VSP_006149;
CC -!- TISSUE SPECIFICITY: Liver specific.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AB031959; BAB03272.1; -; mRNA.
DR EMBL; AB037202; BAA98050.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF250912; AAF74719.1; -; mRNA.
DR CCDS; CCDS20678.1; -. [Q9JJL3-1]
DR PIR; JC7286; JC7286.
DR RefSeq; NP_065241.1; NM_020495.1. [Q9JJL3-1]
DR RefSeq; XP_006507026.1; XM_006506963.2. [Q9JJL3-1]
DR RefSeq; XP_017177100.1; XM_017321611.1. [Q9JJL3-1]
DR AlphaFoldDB; Q9JJL3; -.
DR SMR; Q9JJL3; -.
DR STRING; 10090.ENSMUSP00000044326; -.
DR GlyGen; Q9JJL3; 3 sites.
DR iPTMnet; Q9JJL3; -.
DR PhosphoSitePlus; Q9JJL3; -.
DR SwissPalm; Q9JJL3; -.
DR jPOST; Q9JJL3; -.
DR MaxQB; Q9JJL3; -.
DR PaxDb; Q9JJL3; -.
DR PeptideAtlas; Q9JJL3; -.
DR PRIDE; Q9JJL3; -.
DR ProteomicsDB; 261309; -. [Q9JJL3-1]
DR ProteomicsDB; 261310; -. [Q9JJL3-2]
DR DNASU; 28253; -.
DR Ensembl; ENSMUST00000042812; ENSMUSP00000044326; ENSMUSG00000030236. [Q9JJL3-1]
DR GeneID; 28253; -.
DR KEGG; mmu:28253; -.
DR UCSC; uc009eoq.1; mouse. [Q9JJL3-1]
DR CTD; 28253; -.
DR MGI; MGI:1351899; Slco1b2.
DR VEuPathDB; HostDB:ENSMUSG00000030236; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_4_0_1; -.
DR InParanoid; Q9JJL3; -.
DR OMA; KKTRYCN; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9JJL3; -.
DR TreeFam; TF317540; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-879518; Transport of organic anions.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 28253; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9JJL3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JJL3; protein.
DR Bgee; ENSMUSG00000030236; Expressed in left lobe of liver and 22 other tissues.
DR ExpressionAtlas; Q9JJL3; baseline and differential.
DR Genevisible; Q9JJL3; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; ISO:MGI.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISS:MGI.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0006857; P:oligopeptide transport; ISO:MGI.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..689
FT /note="Solute carrier organic anion transporter family
FT member 1B2"
FT /id="PRO_0000191051"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..192
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..348
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..392
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..420
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..556
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..591
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..625
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..643
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 448..505
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 658..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941"
FT MOD_RES 662
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6L6"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 454..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 460..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 469..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 398
FT /note="T -> TAKLYVDVGYVDLRSVRITP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006149"
FT CONFLICT 455
FT /note="N -> H (in Ref. 2; AAF74719)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="L -> R (in Ref. 2; AAF74719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 76729 MW; 46FBBA1C98FFB97A CRC64;
MDQTQHPSKA AQPLRSEKTR HCDGFRIFLA ALSFSYICKA LGGVIMKSSI TQIERRFDIP
SSISGLIDGG FEIGNLLVIV FVSYFGSKLH RPKLIGTGCF IMGIGSILTA LPHFFMGYYR
YATENDISSL HNSTLTCLVN QTTSLTGTSP EIMEKGCEKG SNSYTWIYVL MGNMLRGIGE
TPIVPLGVSY IDDFAKEGNS SMYLGTLHTI AMIGPILGFI MSSVFAKLYV DVGYVDLRSV
RITPQDARWV GAWWLGFIVN GLLCIICSIP FFFLPKIPKR SQKERKNSAS LHVLKTDEDK
NPVTNPTTQE KQAPANLTGF LWSLRSILTN EQYVIFLILT LLQISSFIGS FTYLFKFIEQ
QFGQTASQAN FLLGVITIPT MASGMFLGGY LIKRLKLTLL GITKFVFFTT TMAYVFYLSY
FLLICENKAF AGLTLTYDGM NPVDSHIDVP LSYCNSDCIC DKNQWEPVCG ENGVTYISPC
LAGCKSFRGD KKLMNIEFYD CSCVSGSGFQ KGNHSARLGE CPRDKCKTKY YFYITFQVII
SFFTALGSTS LMLILIRSVQ PELKSLGMGF HSLVVRTLGG ILAPVYYGAL IDRTCMKWSV
TSCGARGACR LYNSRLFGMI YVGLSIALKT PILLLYVALI YVMKRKMKRN DNKILENGRK
FTDEGNPEPV NNNGYSCVPS DEKNSETPL
