Summary: Organic solute transporter subunit beta protein
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OSTbeta Edit Wikipedia article
|Solute carrier family 51, beta subunit|
|RNA expression pattern|
OST-beta together with OST-alpha is able to transport estrone sulfate, taurocholate, digoxin, and prostaglandin E2 across cell membranes. The Ost-alpha / Ost-beta heterodimer, but not the individual subunits, stimulates sodium-independent bile acid uptake. The heterodimer furthermore is essential for intestinal bile acid transport.
OST-alpha and OST-alpha have high expression in the testis, colon, liver, small intestine, kidney, ovary, and adrenal gland.
- "Entrez Gene: OSTbeta organic solute transporter beta".
- Seward DJ, Koh AS, Boyer JL, Ballatori N (July 2003). "Functional complementation between a novel mammalian polygenic transport complex and an evolutionarily ancient organic solute transporter, OSTalpha-OSTbeta". J. Biol. Chem. 278 (30): 27473–82. doi:10.1074/jbc.M301106200. PMID 12719432.
- Dawson PA, Hubbert M, Haywood J, Craddock AL, Zerangue N, Christian WV, Ballatori N (February 2005). "The Heteromeric Organic Solute Transporter α-β, Ostα-Ostβ, Is an Ileal Basolateral Bile Acid Transporter". J. Biol. Chem. 280 (8): 6960–8. doi:10.1074/jbc.M412752200. PMC 1224727. PMID 15563450.
- Rao A, Haywood J, Craddock AL, Belinsky MG, Kruh GD, Dawson PA (March 2008). "The organic solute transporter α-β, Ostα-Ostβ, is essential for intestinal bile acid transport and homeostasis". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3891–6. doi:10.1073/pnas.0712328105. PMC 2268840. PMID 18292224.
- Sun AQ, Balasubramaniyan N, Xu K et al. (2007). "Protein-protein interactions and membrane localization of the human organic solute transporter". Am. J. Physiol. Gastrointest. Liver Physiol. 292 (6): G1586–93. doi:10.1152/ajpgi.00457.2006. PMID 17332473.
- Boyer JL, Trauner M, Mennone A et al. (2006). "Upregulation of a basolateral FXR-dependent bile acid efflux transporter OSTalpha-OSTbeta in cholestasis in humans and rodents". Am. J. Physiol. Gastrointest. Liver Physiol. 290 (6): G1124–30. doi:10.1152/ajpgi.00539.2005. PMID 16423920.
- Ballatori N, Christian WV, Lee JY et al. (2005). "OSTalpha-OSTbeta: a major basolateral bile acid and steroid transporter in human intestinal, renal, and biliary epithelia". Hepatology 42 (6): 1270–9. doi:10.1002/hep.20961. PMID 16317684.
- Landrier JF, Eloranta JJ, Vavricka SR, Kullak-Ublick GA (2006). "The nuclear receptor for bile acids, FXR, transactivates human organic solute transporter-alpha and -beta genes". Am. J. Physiol. Gastrointest. Liver Physiol. 290 (3): G476–85. doi:10.1152/ajpgi.00430.2005. PMID 16269519.
- Lee H, Zhang Y, Lee FY et al. (2006). "FXR regulates organic solute transporters alpha and beta in the adrenal gland, kidney, and intestine". J. Lipid Res. 47 (1): 201–14. doi:10.1194/jlr.M500417-JLR200. PMID 16251721.
- Dawson PA, Hubbert M, Haywood J et al. (2005). "The Heteromeric Organic Solute Transporter α-β, Ostα-Ostβ, Is an Ileal Basolateral Bile Acid Transporter". J. Biol. Chem. 280 (8): 6960–8. doi:10.1074/jbc.M412752200. PMC 1224727. PMID 15563450.
- Seward DJ, Koh AS, Boyer JL, Ballatori N (2003). "Functional complementation between a novel mammalian polygenic transport complex and an evolutionarily ancient organic solute transporter, OSTalpha-OSTbeta". J. Biol. Chem. 278 (30): 27473–82. doi:10.1074/jbc.M301106200. PMID 12719432.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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Organic solute transporter subunit beta protein Provide feedback
No Pfam abstract.
Hwang JH, Parton A, Czechanski A, Ballatori N, Barnes D;, Comp Biochem Physiol C Toxicol Pharmacol. 2008;148:39-47.: Arachidonic acid-induced expression of the organic solute and steroid transporter-beta (Ost-beta) in a cartilaginous fish cell line. PUBMED:18407792 EPMC:18407792
Dawson PA, Hubbert M, Haywood J, Craddock AL, Zerangue N, Christian WV, Ballatori N;, J Biol Chem. 2005;280:6960-6968.: The heteromeric organic solute transporter alpha-beta, Ostalpha-Ostbeta, is an ileal basolateral bile acid transporter. PUBMED:15563450 EPMC:15563450
Frankenberg T, Rao A, Chen F, Haywood J, Shneider BL, Dawson PA;, Am J Physiol Gastrointest Liver Physiol. 2006;290:G912-G922.: Regulation of the mouse organic solute transporter alpha-beta, Ostalpha-Ostbeta, by bile acids. PUBMED:16357058 EPMC:16357058
Internal database links
|SCOOP:||TMEM156 DUF4725 DUF4834 Cadherin_C_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR029387
Organic solute transporter subunit beta (OSTbeta, also known as SLC51B) is an essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood [PUBMED:16317684].
OSTbeta is a single-TM domain polypeptide that forms a transporter complex with Ost-alpha protein, which is a 7-transmembrane (TM) domain containing protein. This heterodimerisation is required for the delivery of the complex to the plasma membrane. The OSTalpha-OSTbeta complex serves as a multispecific transporter that may participate in cellular uptake of bile acids, some endogenous and exogenous steroids, and eicosanoids. It functions via a facilitated diffusion mechanism. Interestingly, this transporter also transports dehydroepiandrosterone sulfate (DHEAS) and pregnenolone sulfate (PREGS), which are major excitatory neurosteroids. This suggests a possible function for OSTalpha-OSTbeta complex in the brain [PUBMED:23506901].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||plasma membrane (GO:0005886)|
|Molecular function||protein heterodimerization activity (GO:0046982)|
|transporter activity (GO:0005215)|
|Biological process||bile acid and bile salt transport (GO:0015721)|
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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family:
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Number in seed:||19|
|Number in full:||52|
|Average length of the domain:||122.00 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||74.14 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
|Download:||download the raw HMM for this family|
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How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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