SO1B2_RAT
ID SO1B2_RAT Reviewed; 687 AA.
AC Q9QZX8; Q9JHF6; Q9JIM2;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
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=rLST-1;
DE AltName: Full=Sodium-independent organic anion-transporting polypeptide 4;
DE Short=OATP-4;
DE AltName: Full=Solute carrier family 21 member 10;
GN Name=Slco1b2; Synonyms=Oatp1b2, Slc21a10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=10500057; DOI=10.1016/s0016-5085(99)70333-1;
RA Kakyo M., Unno M., Tokui T., Nakagomi R., Nishio T., Iwasashi H., Nakai D.,
RA Seki M., Suzuki M., Naitoh T., Matsuno S., Yawo H., Abe T.;
RT "Molecular characterization and functional regulation of a novel rat liver-
RT specific organic anion transporter rlst-1.";
RL Gastroenterology 117:770-775(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10903899; DOI=10.1006/bbrc.2000.3105;
RA Choudhuri S., Ogura K., Klaassen C.D.;
RT "Cloning of the full-length coding sequence of rat liver-specific organic
RT anion transporter-1 (rlst-1) and a splice variant and partial
RT characterization of the rat lst-1 gene.";
RL Biochem. Biophys. Res. Commun. 274:79-86(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10838093; DOI=10.1016/s0014-5793(00)01596-9;
RA Cattori V., Hagenbuch B., Hagenbuch N., Stieger B., Ha R.,
RA Winterhalter K.H., Meier P.J.;
RT "Identification of organic anion transporting polypeptide 4 (Oatp4) as a
RT major full-length isoform of the liver-specific transporter-1 (rlst-1) in
RT rat liver.";
RL FEBS Lett. 474:242-245(2000).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11713643; DOI=10.1007/s004240100697;
RA Cattori V., van Montfoort J.E., Stieger B., Landmann L., Meijer D.K.,
RA Winterhalter K.H., Meier P.J., Hagenbuch B.;
RT "Localization of organic anion transporting polypeptide 4 (Oatp4) in rat
RT liver and comparison of its substrate specificity with Oatp1, Oatp2 and
RT Oatp3.";
RL Pflugers Arch. 443:188-195(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; THR-660 AND SER-667, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein. Note=Confined to the basolateral plasma membrane of
CC hepatocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=rLST-1a;
CC IsoId=Q9QZX8-2; Sequence=Displayed;
CC Name=2; Synonyms=rLST-1b;
CC IsoId=Q9QZX8-1; Sequence=VSP_006150;
CC Name=3; Synonyms=rLST-1c;
CC IsoId=Q9QZX8-3; Sequence=VSP_006151;
CC -!- TISSUE SPECIFICITY: Liver specific. Expression is highest in central
CC perivenous hepatocytes and lowest in the periportal region. Isoform 1
CC predominates. Not detected in heart, brain, kidney, skeletal muscle,
CC lung, testis or spleen.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AF147740; AAF02526.1; -; mRNA.
DR EMBL; AF208545; AAF87098.1; -; mRNA.
DR EMBL; AF217450; AAF87099.1; -; mRNA.
DR EMBL; AF272571; AAF90136.1; -; Genomic_DNA.
DR EMBL; AF272558; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272559; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272560; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272561; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272562; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272563; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272564; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272565; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272566; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272567; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272568; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272569; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AF272570; AAF90136.1; JOINED; Genomic_DNA.
DR EMBL; AJ271682; CAB92299.1; -; mRNA.
DR RefSeq; NP_001257515.1; NM_001270586.1. [Q9QZX8-1]
DR RefSeq; NP_001257516.1; NM_001270587.1. [Q9QZX8-3]
DR RefSeq; NP_113838.1; NM_031650.3. [Q9QZX8-2]
DR AlphaFoldDB; Q9QZX8; -.
DR SMR; Q9QZX8; -.
DR IntAct; Q9QZX8; 1.
DR STRING; 10116.ENSRNOP00000013409; -.
DR BindingDB; Q9QZX8; -.
DR ChEMBL; CHEMBL1781861; -.
DR TCDB; 2.A.60.1.8; the organo anion transporter (oat) family.
DR GlyGen; Q9QZX8; 3 sites.
DR iPTMnet; Q9QZX8; -.
DR PhosphoSitePlus; Q9QZX8; -.
DR PaxDb; Q9QZX8; -.
DR PRIDE; Q9QZX8; -.
DR Ensembl; ENSRNOT00000013409; ENSRNOP00000013409; ENSRNOG00000030538. [Q9QZX8-2]
DR Ensembl; ENSRNOT00000013514; ENSRNOP00000013514; ENSRNOG00000030538. [Q9QZX8-3]
DR GeneID; 58978; -.
DR KEGG; rno:58978; -.
DR UCSC; RGD:69300; rat. [Q9QZX8-2]
DR CTD; 28253; -.
DR RGD; 69300; Slco1b2.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_4_0_1; -.
DR InParanoid; Q9QZX8; -.
DR OMA; KKTRYCN; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9QZX8; -.
DR TreeFam; TF317540; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR Reactome; R-RNO-9754706; Atorvastatin ADME.
DR PRO; PR:Q9QZX8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000030538; Expressed in liver and 9 other tissues.
DR Genevisible; Q9QZX8; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0035673; F:oligopeptide transmembrane transporter activity; IDA:RGD.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; TAS:RGD.
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; IDA:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0006857; P:oligopeptide transport; IDA:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 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..687
FT /note="Solute carrier organic anion transporter family
FT member 1B2"
FT /id="PRO_0000191052"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..623
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 450..507
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 286..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJL3"
FT MOD_RES 660
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 456..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 462..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 471..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 207..240
FT /note="GTLHTIAMIGPILGFIMSSVFAKIYVDVGYVDLN -> D (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10903899"
FT /id="VSP_006151"
FT VAR_SEQ 407..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10500057"
FT /id="VSP_006150"
SQ SEQUENCE 687 AA; 76767 MW; E6A17786FD136CC6 CRC64;
MDHTQQSRKA AEAQPSRSKQ TRFCDGFKLF LAALSFSYIC KALGGVVMKS SITQIERRFD
IPSSISGLID GGFEIGNLLV IVFVSYFGSK LHRPKLIGIG CFIMGIGSIL TALPHFFMGY
YKYAKENDIG SLGNSTLTCF INQMTSPTGP SPEIVEKGCE KGLKSHMWIY VLMGNMLRGI
GETPIVPLGI SYLDDFAKEG HTSMHLGTLH TIAMIGPILG FIMSSVFAKI YVDVGYVDLN
SVRITPNDAR WVGAWWLSFI VNGLLCITSS IPFFFLPKIP KRSQEERKNS VSLHAPKTDE
EKKHMTNLTK QEEQDPSNMT GFLRSLRSIL TNEIYVIFLI LTLLQVSGFI GSFTYLFKFI
EQQFGRTASQ ANFLLGIITI PTMATAMFLG GYIVKKFKLT SVGIAKFVFF TSSVAYAFQF
LYFPLLCENK PFAGLTLTYD GMNPVDSHID VPLSYCNSDC SCDKNQWEPI CGENGVTYIS
PCLAGCKSFR GDKKPNNTEF YDCSCISNSG NNSAHLGECP RYKCKTNYYF YIILQVTVSF
FTAMGSPSLI LILMKSVQPE LKSLAMGFHS LIIRALGGIL APIYYGAFID RTCIKWSVTS
CGKRGACRLY NSRLFGFSYL GLNLALKTPP LFLYVVLIYF TKRKYKRNDN KTLENGRQFT
DEGNPDSVNK NGYYCVPYDE QSNETPL
