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SLC26A1 Membrane Protein Introduction

Introduction of SLC26A1

SLC26A1, also known as solute carrier family 26 (sulfate transporter) member 1, solute carrier family 26 (anion exchanger) member 1, sulfate/anion transporter SAT-1 protein, sulfate anion transporter AT1, SAT1, CAON, or EDM4, is a 75 kDa transmembrane protein with 701 amino acids length. In humans, it is encoded by the SLC26A1 gene which is localized at the chromosome 4p16.3. SLC26A1 is a founding member in the highly conserved SLC26A gene family, which codes for multifunctional anion channels and anion exchangers with a wide range of substrates and consists of 11 genes (SLC26A1 to SLC26A11) in mammals. SLC26A1 is predominantly expressed in the liver, brain, and pancreas, and works as an anion exchanger and transports, including sulfate, bicarbonate, chloride, and oxalate in an electroneutral manner.

Basic Information of SLC26A1
Protein Name Sulfate anion transporter 1
Gene Name SLC26A1
Aliases SAT-1, Solute carrier family 26 member 1
Organism Homo sapiens (Human)
UniProt ID Q9H2B4
Transmembrane Times 12
Length (aa) 701
Sequence MDESPEPLQQGRGPVPVRRQRPAPRGLREMLKARLWCSCSCSVLCVRALVQDLLPATRWLRQYRPREYLAGDVMSGLVIGIILVPQAIAYSLLAGLQPIYSLYTSFFANLIYFLMGTSRHVSVGIFSLLCLMVGQVVDRELQLAGFDPSQDGLQPGANSSTLNGSAAMLDCGRDCYAIRVATALTLMTGLYQVLMGVLRLGFVSAYLSQPLLDGFAMGASVTILTSQLKHLLGVRIPRHQGPGMVVLTWLSLLRGAGQANVCDVVTSTVCLAVLLAAKELSDRYRHRLRVPLPTELLVIVVATLVSHFGQLHKRFGSSVAGDIPTGFMPPQVPEPRLMQRVALDAVALALVAAAFSISLAEMFARSHGYSVRANQELLAVGCCNVLPAFLHCFATSAALAKSLVKTATGCRTQLSSVVSATVVLLVLLALAPLFHDLQRSVLACVIVVSLRGALRKVWDLPRLWRMSPADALVWAGTAATCMLVSTEAGLLAGVILSLLSLAGRTQRPRTALLARIGDTAFYEDATEFEGLVPEPGVRVFRFGGPLYYANKDFFLQSLYSLTGLDAGCMAARRKEGGSETGVGEGGPAQGEDLGPVSTRAALVPAAAGFHTVVIDCAPLLFLDAAGVSTLQDLRRDYGALGISLLLACCSPPVRDILSRGGFLGEGPGDTAEEEQLFLSVHDAVQTARARHRELEATDAHL

Function of SLC26A1 Membrane Protein

The human SLC26A1 is a 4,4'-diisothiocyanato-2,2'-stilbenedisulfonic acid (DIDS)-sensitive, electroneutral sodium-independent anion exchanger, responsible for transporting the sulfate, thiosulfate, bicarbonate, oxalate, and chloride. Human SLC26A1-mediated anion exchange is different from that of its rodent orthologs in its stimulation by alkaline pH, inhibition by acidic pH, and failure to transport glyoxylate. The transport of sulfate and oxalate modulated by SLC26A1 is highly dependent on the allosteric activation via extracellular chloride or non-substrate anions. Extracellular chloride motivates apparent Vmax of human SLC26A1-mediated sulfate uptake by allowing a two-log reduction in sensitivity to inhibition by extracellular protons, but not changing the transporter affinity for extracellular sulfate. Compared to SLC26A1-mediated sulfate transport, SLC26A1-related chloride transport is activated by acidic pH, which reveals decreased sensitivity to DIDS and exhibits a cation dependence for its DIDS-insensitive component. Furthermore, mutations in SLC26A1 result in multiple disorders, including hepatotoxicity, urolithiasis, distal renal tubular acidosis, and impaired gastric secretion, caused by the disruption of ion homeostasis.

Position of amino acid substitutions in the predicted secondary structure model of the human SLC26A1 protein.Fig.1 Position of amino acid substitutions in the predicted secondary structure model of the human SLC26A1 protein. (Dawson, 2013)

Application of SLC26A1 Membrane Protein in Literature

  1. Andharia N., et al. Electrophysiological properties of anion exchangers in the luminal membrane of guinea pig pancreatic duct cells. Pflugers Arch. 2018, 470(6): 897-907. PubMed ID: 29399744

    RT-PCR analysis in this work reveals that the main and interlobular ducts express all members of SLC26A family except for Slc26a5 and Slc26a8. SLC26A1, SLC26A4, SLC26A6, and SLC26A10 are observed to be localized at the luminal membrane of guinea pig pancreatic ducts by immunohistochemistry.

  2. Yin K., et al. Deletion of Slc26a1 and Slc26a7 Delays Enamel Mineralization in Mice. Front Physiol. 2018, 8: 307. PubMed ID: 28559854

    Some members of Slc26 gene family (Slc26a1, Slc26a3, Slc26a4, Slc26a6, and Slc26a7) are previously studied to be implicated in maturation-stage amelogenesis, particularly in a key process of pH regulation. The data here indicate that the involvement of SLC26A1 and SLC26A7 can function as pivotal ion transporters in pH regulatory networks during the enamel maturation.

  3. Rapp C., et al. Molecular analysis of human solute carrier SLC26 anion transporter disease-causing mutations using 3-dimensional homology modeling. Biochim Biophys Acta. 2017, 1859(12): 2420-2434. PubMed ID: 28941661

    The availability of the first crystal structure of a bacterial member (SLC26Dg) in the solute carrier SLC26 family of anion transporters has assisted authors to create three-dimensional models of all ten human members (SLC26A1-A11, A10 being a pseudogene) by a Phyre2 bioinformatic tool.

  4. Gee H.Y., et al. Mutations in SLC26A1 Cause Nephrolithiasis. Am J Hum Genet. 2016, 98(6): 1228-1234. PubMed ID: 27210743

    Analysis in this report reveals that the variant protein mimicking p.Thr185Met has defects in protein folding or trafficking. Furthermore, all the identified mutations in SLC26A1 may lead to a decreased transporter activity by measuring anion exchange activity of SLC26A1. The data identifies SLC26A1 mutations as causes of recessive Mendelian form of nephrolithiasis.

  5. Wu M., et al. Extracellular Cl(-) regulates human SO4 (2-)/anion exchanger SLC26A1 by altering pH sensitivity of anion transport. Pflugers Arch. 2016, 468(8): 1311-1332. PubMed ID: 27125215

    Genetic deficiency of SLC26A1 anion exchanger in mice is associated with hyposulfatemia and hyperoxaluria with nephrolithiasis. This study exhibits that rare SLC26A1 polymorphic variants from a patient with nephrolithiasis/calcinosis and a patient with renal Fanconi Syndrome have no loss-of-function phenotypes consistent with disease pathogenesis.

SLC26A1 Preparation Options

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Reference

  1. Dawson P A, et al. (2013). Human SLC26A1 gene variants: a pilot study. Scientific World Journal. 2013: 541710.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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