OSTB_MOUSE
ID OSTB_MOUSE Reviewed; 128 AA.
AC Q80WK2; Q14BU3; Q3V4C1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Organic solute transporter subunit beta {ECO:0000303|PubMed:22535958};
DE Short=OST-beta {ECO:0000303|PubMed:17650074};
DE AltName: Full=Solute carrier family 51 subunit beta;
GN Name=Slc51b; Synonyms=Ostb;
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].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=12719432; DOI=10.1074/jbc.m301106200;
RA Seward D.J., Koh A.S., Boyer J.L., Ballatori N.;
RT "Functional complementation between a novel mammalian polygenic transport
RT complex and an evolutionarily ancient organic solute transporter, OSTalpha-
RT OSTbeta.";
RL J. Biol. Chem. 278:27473-27482(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15563450; DOI=10.1074/jbc.m412752200;
RA Dawson P.A., Hubbert M., Haywood J., Craddock A.L., Zerangue N.,
RA Christian W.V., Ballatori N.;
RT "The heteromeric organic solute transporter alpha-beta, Ostalpha-Ostbeta,
RT is an ileal basolateral bile acid transporter.";
RL J. Biol. Chem. 280:6960-6968(2005).
RN [5]
RP FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=16317684; DOI=10.1002/hep.20961;
RA Ballatori N., Christian W.V., Lee J.Y., Dawson P.A., Soroka C.J.,
RA Boyer J.L., Madejczyk M.S., Li N.;
RT "OSTalpha-OSTbeta: a major basolateral bile acid and steroid transporter in
RT human intestinal, renal, and biliary epithelia.";
RL Hepatology 42:1270-1279(2005).
RN [6]
RP INDUCTION BY NR1H4.
RX PubMed=16357058; DOI=10.1152/ajpgi.00479.2005;
RA Frankenberg T., Rao A., Chen F., Haywood J., Shneider B.L., Dawson P.A.;
RT "Regulation of the mouse organic solute transporter alpha-beta, Ostalpha-
RT Ostbeta, by bile acids.";
RL Am. J. Physiol. 290:G912-G922(2006).
RN [7]
RP INDUCTION.
RX PubMed=16628672; DOI=10.1002/hep.21158;
RA Mennone A., Soroka C.J., Cai S.Y., Harry K., Adachi M., Hagey L.,
RA Schuetz J.D., Boyer J.L.;
RT "Mrp4-/- mice have an impaired cytoprotective response in obstructive
RT cholestasis.";
RL Hepatology 43:1013-1021(2006).
RN [8]
RP IDENTIFICATION OF THE OST-ALPHA/OST-BETA COMPLEX, SUBCELLULAR LOCATION,
RP TOPOLOGY, INTERACTION WITH SLC51A, FUNCTION, AND TRANSPORT ACTIVITY.
RX PubMed=17650074; DOI=10.1042/bj20070716;
RA Li N., Cui Z., Fang F., Lee J.Y., Ballatori N.;
RT "Heterodimerization, trafficking and membrane topology of the two proteins,
RT Ost alpha and Ost beta, that constitute the organic solute and steroid
RT transporter.";
RL Biochem. J. 407:363-372(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, 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).
RN [10]
RP FUNCTION OF THE OST-ALPHA/OST-BETA COMPLEX IN BILE TRANSPORT, SUBCELLULAR
RP LOCATION, TOPOLOGY, MUTAGENESIS OF 29-GLU-ASP-30; 34-TRP-ASN-35;
RP 54-ARG-ARG-55 AND ARG-61, AND TRANSPORT ACTIVITY.
RX PubMed=22535958; DOI=10.1074/jbc.m112.352245;
RA Christian W.V., Li N., Hinkle P.M., Ballatori N.;
RT "beta-Subunit of the Ostalpha-Ostbeta organic solute transporter is
RT required not only for heterodimerization and trafficking but also for
RT function.";
RL J. Biol. Chem. 287:21233-21243(2012).
CC -!- FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a
CC heterodimer that acts as the intestinal basolateral transporter
CC responsible for bile acid export from enterocytes into portal blood
CC (PubMed:15563450, PubMed:16317684, PubMed:17650074, PubMed:22535958).
CC The Ost-alpha/Ost-beta complex efficiently transports the major species
CC of bile acids (taurocholate) (PubMed:16317684, PubMed:17650074,
CC PubMed:22535958). Taurine conjugates are transported more efficiently
CC across the basolateral membrane than glycine-conjugated bile acids
CC (PubMed:16317684). Can also transport steroids such as estrone 3-
CC sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role
CC in the enterohepatic circulation of sterols (By similarity). Able to
CC transport eicosanoids such as prostaglandin E2 (By similarity).
CC Modulates SLC51A glycosylation, membrane trafficking and stability
CC activities (PubMed:15563450). {ECO:0000250|UniProtKB:Q86UW1,
CC ECO:0000250|UniProtKB:Q90YM5, ECO:0000269|PubMed:15563450,
CC ECO:0000269|PubMed:16317684, ECO:0000269|PubMed:17650074,
CC ECO:0000269|PubMed:22535958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:16317684,
CC ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in);
CC Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in);
CC Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851,
CC ChEBI:CHEBI:29746; Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in);
CC Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in);
CC Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurodeoxycholate(out) = taurodeoxycholate(in);
CC Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycodeoxycholate(out) = glycodeoxycholate(in);
CC Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982;
CC Evidence={ECO:0000269|PubMed:16317684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000250|UniProtKB:Q90YM5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC Evidence={ECO:0000250|UniProtKB:Q86UW2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone
CC 3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905;
CC Evidence={ECO:0000250|UniProtKB:Q86UW2};
CC -!- SUBUNIT: Interacts with SLC51A. The Ost-alpha/Ost-beta complex is a
CC heterodimer composed of alpha (SLC51A) and beta (SLC51B) subunit;
CC induces the transport of SLC51A from the reticulum endoplasmic to the
CC plasma membrane. {ECO:0000269|PubMed:17650074}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15563450,
CC ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}; Single-pass
CC membrane protein {ECO:0000269|PubMed:15563450,
CC ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}. Note=Mainly
CC restricted to the lateral and basal membranes of ileal enterocytes.
CC -!- TISSUE SPECIFICITY: Present at high level in ileum. In ileum, it is
CC restricted to the apical domain on the mature villus enterocytes with
CC little detectable expression in the goblet cells or crypt enterocytes
CC (at protein level). Expressed in kidney but not in heart, brain, liver,
CC spleen, embryo, lung, thymus, ovary nor testis.
CC {ECO:0000269|PubMed:15563450}.
CC -!- INDUCTION: Positively regulated via the bile acid-activated nuclear
CC receptor farnesoid X receptor (NR1H4/FXR).
CC {ECO:0000269|PubMed:16357058, ECO:0000269|PubMed:16628672}.
CC -!- DOMAIN: The transmembrane domain (TM) is the major site of interaction
CC with SLC51A. The extracellular-membrane interface is absolutely
CC required for transport activity. The intracellular-membrane interface
CC is necessary for establishing the correct membrane orientation that is
CC essential for the heterodimer Ost-alpha/Ost-beta complex formation and
CC transport activity at the cell membrane surface.
CC -!- SIMILARITY: Belongs to the OST-beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE20418.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY279396; AAP23994.1; -; mRNA.
DR EMBL; AK002463; BAE20415.1; -; mRNA.
DR EMBL; AK004188; BAE20418.1; ALT_SEQ; mRNA.
DR EMBL; BC115606; AAI15607.1; -; mRNA.
DR EMBL; BC115607; AAI15608.1; -; mRNA.
DR CCDS; CCDS23291.1; -.
DR RefSeq; NP_849264.1; NM_178933.2.
DR AlphaFoldDB; Q80WK2; -.
DR SMR; Q80WK2; -.
DR STRING; 10090.ENSMUSP00000064494; -.
DR iPTMnet; Q80WK2; -.
DR PhosphoSitePlus; Q80WK2; -.
DR MaxQB; Q80WK2; -.
DR PaxDb; Q80WK2; -.
DR PeptideAtlas; Q80WK2; -.
DR PRIDE; Q80WK2; -.
DR ProteomicsDB; 295480; -.
DR Antibodypedia; 1475; 69 antibodies from 12 providers.
DR DNASU; 330962; -.
DR Ensembl; ENSMUST00000065894; ENSMUSP00000064494; ENSMUSG00000053862.
DR GeneID; 330962; -.
DR KEGG; mmu:330962; -.
DR UCSC; uc009qdg.1; mouse.
DR CTD; 123264; -.
DR MGI; MGI:3582052; Slc51b.
DR VEuPathDB; HostDB:ENSMUSG00000053862; -.
DR eggNOG; ENOG502S380; Eukaryota.
DR GeneTree; ENSGT00390000010409; -.
DR HOGENOM; CLU_158049_0_0_1; -.
DR InParanoid; Q80WK2; -.
DR OMA; EMLWVFR; -.
DR OrthoDB; 940161at2759; -.
DR PhylomeDB; Q80WK2; -.
DR TreeFam; TF337010; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR BioGRID-ORCS; 330962; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slc51b; mouse.
DR PRO; PR:Q80WK2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80WK2; protein.
DR Bgee; ENSMUSG00000053862; Expressed in jejunum and 55 other tissues.
DR Genevisible; Q80WK2; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IPI:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:UniProtKB.
DR GO; GO:0032782; P:bile acid secretion; ISO:MGI.
DR GO; GO:0071702; P:organic substance transport; IPI:MGI.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0060050; P:positive regulation of protein glycosylation; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR InterPro; IPR029387; OSTbeta.
DR Pfam; PF15048; OSTbeta; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..128
FT /note="Organic solute transporter subunit beta"
FT /id="PRO_0000331555"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 29..30
FT /note="ED->AA: Does not inhibit transport activity. Does
FT not inhibit colocalization with SLC51A at the plasma
FT membrane. Does not decrease glycosylation of SLC51A."
FT /evidence="ECO:0000269|PubMed:22535958"
FT MUTAGEN 34..35
FT /note="WN->AA: Inhibits transport activity. Inhibits weakly
FT colocalization with SLC51A at the plasma membrane.
FT Decreases glycosylation of SLC51A."
FT /evidence="ECO:0000269|PubMed:22535958"
FT MUTAGEN 34..35
FT /note="WN->FQ: Does not inhibit transport activity. Does
FT not inhibit colocalization with SLC51A at the plasma
FT membrane. Does not decrease glycosylation of SLC51A."
FT /evidence="ECO:0000269|PubMed:22535958"
FT MUTAGEN 54..55
FT /note="RR->AA: Inhibits transport activity. Inhibits
FT localization at the plasma membrane and membrane
FT orientation. Decreases glycosylation of SLC51A."
FT /evidence="ECO:0000269|PubMed:22535958"
FT MUTAGEN 61
FT /note="R->G: Does not inhibit transport activity. Does not
FT inhibit colocalization with SLC51A at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:22535958"
FT CONFLICT 70
FT /note="K -> Q (in Ref. 3; AAI15607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14684 MW; ADE8D76D128B68B9 CRC64;
MDHSAEKAAA NAEVPQELLE EMLWYFRAED AAPWNYSILV LAVLVVMTSM FLLRRSILAN
RNRKKQPQDK ETPEDLHLDD SIMKENNSQV FLRETLISEK PDLAPGEPEL KEKDSSLVFL
PDPQETES
