Biology:SLC26A6
 Generic protein structure example |
Solute carrier family 26 member 6 is a protein that in humans is encoded by the SLC26A6 gene.[1][2][3] It is an anion-exchanger expressed in the apical membrane of the kidney proximal tubule, the apical membranes of the duct cells in the pancreas, and the villi of the duodenum.[4]
This gene belongs to the solute carrier 26 family, whose members encode anion transporter proteins. This particular family member encodes a protein involved in transporting chloride, oxalate, sulfate and bicarbonate. Several alternatively spliced transcript variants of this gene, encoding distinct isoforms, have been described, but the full-length nature of some of these variants has not been determined.[3]
Associated diseases
Diseases associated with SLC26A6 include sialolithiasis and urolithiasis.[5]
See also
References
- ↑ "Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger". Genomics 70 (1): 102–112. November 2000. doi:10.1006/geno.2000.6355. PMID 11087667.
- ↑ "Cloning and characterization of SLC26A6, a novel member of the solute carrier 26 gene family". Genomics 72 (1): 43–50. February 2001. doi:10.1006/geno.2000.6445. PMID 11247665.
- ↑ 3.0 3.1 "Entrez Gene: SLC26A6 solute carrier family 26, member 6". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=65010.
- ↑ "Renal and intestinal transport defects in Slc26a6-null mice". American Journal of Physiology. Cell Physiology. 4 288 (4): C957–C965. April 2005. doi:10.1152/ajpcell.00505.2004. PMID 15574486.
- ↑ "SLC26A6 Gene - GeneCards | S26A6 Protein | S26A6 Antibody". https://www.genecards.org/cgi-bin/carddisp.pl?gene=SLC26A6.
Further reading
- "Physiological roles and regulation of mammalian sulfate transporters". Physiological Reviews 81 (4): 1499–1533. October 2001. doi:10.1152/physrev.2001.81.4.1499. PMID 11581495.
- "Dominance of intrinsic genetic factors in shaping the human immunoglobulin Vlambda repertoire". Journal of Molecular Biology 294 (2): 457–465. November 1999. doi:10.1006/jmbi.1999.3243. PMID 10610771.
- "Molecular characterization of the murine Slc26a6 anion exchanger: functional comparison with Slc26a1". American Journal of Physiology. Renal Physiology 283 (4): F826–F838. October 2002. doi:10.1152/ajprenal.00079.2002. PMID 12217875.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–16903. December 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
]* "Functional comparison of mouse slc26a6 anion exchanger with human SLC26A6 polypeptide variants: differences in anion selectivity, regulation, and electrogenicity". The Journal of Biological Chemistry 280 (9): 8564–8580. March 2005. doi:10.1074/jbc.M411703200. PMID 15548529.
- "SLC26A6 and SLC26A7 anion exchangers have a distinct distribution in human kidney". Nephron. Experimental Nephrology 101 (2): e50–e58. 2006. doi:10.1159/000086345. PMID 15956810.
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. January 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "Coupling modes and stoichiometry of Cl-/HCO3- exchange by slc26a3 and slc26a6". The Journal of General Physiology 127 (5): 511–524. May 2006. doi:10.1085/jgp.200509392. PMID 16606687.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–648. November 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "Anion exchangers in flux: functional differences between human and mouse SLC26A6 polypeptides". Epithelial Anion Transport in Health and Disease: The Role of the SLC26 Transporters Family. Novartis Foundation Symposia. 273. 2007. pp. 107–19; discussion 119–25, 261–4. doi:10.1002/0470029579.ch8. ISBN 9780470016244.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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