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Gene Review

SLC13A3  -  solute carrier family 13 (sodium-dependent...

Homo sapiens

Synonyms: NADC3, Na(+)/dicarboxylate cotransporter 3, NaDC-3, SDCT2, Sodium-dependent high-affinity dicarboxylate transporter 2, ...
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High impact information on SLC13A3

  • SDCT2, unlike SDCT1, displayed a unique pH dependence for succinate transport (optimal pH 7.5-8.5) and showed a high affinity for dimethylsuccinate, two features characteristic of basolateral transport [1].
  • Using a PCR-based approach, we isolated a novel member of the sodium-dependent dicarboxylate/sulfate transporter called SDCT2 [1].
  • SDCT2 expressed in Xenopus oocytes mediated sodium-dependent transport of di- and tricarboxylates with substrate preference for succinate rather than citrate, but excluding monocarboxylates [1].
  • In situ hybridization revealed that SDCT2 is prominently expressed in kidney proximal tubule S3 segments and in perivenous hepatocytes, consistent with the sites of high-affinity dicarboxylate transport identified based on vesicle studies [1].
  • Our studies provide direct evidence of the localization of NaDC3 at the basolateral membrane of human renal proximal tubule cells and identify a di-hydrophobic amino acid motif VW as basolateral localization signal in the N-terminal cytoplasmic domain of NaDC3 [2].

Biological context of SLC13A3

  • The narrow substrate specificity prevents interaction of drugs with dicarboxylate-like structure with hNaDC-3 and ensures sufficient support of the proximal tubule cells with alpha-ketoglutarate for anion secretion via organic anion transporter 1 or 3 [3].
  • Point mutagenesis revealed that mutation of either of two hydrophobic amino acids V and W in this short sequence largely redirected NaDC3 to both apical and basolateral surfaces of LLC-PK, indicating that the two hydrophobic amino acids are critical for the basolateral targeting of NaDC3 [2].
  • Functional analysis of rat-human and human-rat NaDC3 chimeric transporters indicates that the catalytic domain of the transporter lies in the carboxy-terminal half of the protein [4].
  • The human NaDC3 gene is located on chromosome 20q12-13.1, as evidenced by fluorescent in situ hybridization [4].
  • The functional expression of NaDC3 in the brain was demonstrated by in situ hybridization and reverse transcription-polymerase chain reaction as well as by isolation of a full-length functional NaDC3 from a rat brain cDNA library [5].

Anatomical context of SLC13A3


Associations of SLC13A3 with chemical compounds

  • As opposed to the rat and flounder orthologs, hNaDC-3 was hardly inhibited by lithium concentrations up to 5 mM [3].
  • Then, EGFP-fused wild-type, NH2- and COOH-terminal deletion and point mutants of NaDC3, and chimera between NaDC3 and NaDC1, were generated and transfected into polarized renal cells lines, LLC-PK1 and MDCK [2].
  • These studies establish NaDC3 as the transporter responsible for the Na(+)-coupled transport of N-acetylaspartate in the brain [5].
  • Dimethylsuccinate also interacts with hNaDC3 [4].
  • Of these transporters, NaC3 (formerly known as Na+-coupled dicarboxylate transporter 3, NaDC3/SDCT2) and NaC2 (formerly known as Na+-coupled citrate transporter, NaCT) have been shown to be expressed in brain [7].

Analytical, diagnostic and therapeutic context of SLC13A3


  1. Molecular and functional analysis of SDCT2, a novel rat sodium-dependent dicarboxylate transporter. Chen, X., Tsukaguchi, H., Chen, X.Z., Berger, U.V., Hediger, M.A. J. Clin. Invest. (1999) [Pubmed]
  2. Identification of basolateral membrane targeting signal of human sodium-dependent dicarboxylate transporter 3. Bai, X., Chen, X., Feng, Z., Hou, K., Zhang, P., Fu, B., Shi, S. J. Cell. Physiol. (2006) [Pubmed]
  3. Substrate specificity of the human renal sodium dicarboxylate cotransporter, hNaDC-3, under voltage-clamp conditions. Burckhardt, B.C., Lorenz, J., Kobbe, C., Burckhardt, G. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  4. Structure, function, and genomic organization of human Na(+)-dependent high-affinity dicarboxylate transporter. Wang, H., Fei, Y.J., Kekuda, R., Yang-Feng, T.L., Devoe, L.D., Leibach, F.H., Prasad, P.D., Ganapathy, V. Am. J. Physiol., Cell Physiol. (2000) [Pubmed]
  5. Transport of N-acetylaspartate by the Na(+)-dependent high-affinity dicarboxylate transporter NaDC3 and its relevance to the expression of the transporter in the brain. Huang, W., Wang, H., Kekuda, R., Fei, Y.J., Friedrich, A., Wang, J., Conway, S.J., Cameron, R.S., Leibach, F.H., Ganapathy, V. J. Pharmacol. Exp. Ther. (2000) [Pubmed]
  6. Effects of human Na(+)/dicarboxylate cotransporter 3 on the replicative senescence of human embryonic lung diploid fibroblasts. Chen, X., Cao, D., Wang, J., Yuan, L., Feng, Z., Fu, B., Hong, Q., Zhang, X., Bai, X., Lu, Y., Ding, R. J. Gerontol. A Biol. Sci. Med. Sci. (2005) [Pubmed]
  7. Functional and molecular identification of sodium-coupled dicarboxylate transporters in rat primary cultured cerebrocortical astrocytes and neurons. Yodoya, E., Wada, M., Shimada, A., Katsukawa, H., Okada, N., Yamamoto, A., Ganapathy, V., Fujita, T. J. Neurochem. (2006) [Pubmed]
  8. Relationship between aging and renal high-affinity sodium-dependent dicarboxylate cotransporter-3 expression characterized with antifusion protein antibody. Wang, J., Chen, X., Zhu, H., Peng, L., Hong, Q. J. Gerontol. A Biol. Sci. Med. Sci. (2003) [Pubmed]
  9. Genomic cloning and restriction site mapping of a porcine adenovirus isolate: demonstration of genomic stability in porcine adenovirus. Kleiboeker, S.B., Seal, B.S., Mengeling, W.L. Arch. Virol. (1993) [Pubmed]
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