Home  |  Contact
PROSITE documentation PDOC00591 [for PROSITE entry PS00714]

Sodium:dicarboxylate symporter family signatures





Description

It has been shown [1] that integral membrane proteins that mediate the intake of a wide variety of molecules with the concomitant uptake of sodium ions (sodium symporters) can be grouped, on the basis of sequence and functional similarities into a number of distinct families. One of these families [2] is known as the sodium:dicarboxylate symporter family (SDF) and currently consists of the following proteins:

  • Escherichia coli proton-glutamate symport protein (glutamate-aspartate carrier) (gene gltP). GltP is a sodium-independent carrier for glutamate and aspartate.
  • Bacillus proton/sodium-glutamate symport protein (gene gltT or gltP). GltT is a sodium-dependent carrier for glutamate and aspartate.
  • Rhizobium and Escherichia coli C4-dicarboxylate carrier (gene dctA), which is responsible for the transport of dicarboxylates such as succinate, fumarate, and malate. In Rhizobium this transport system plays an important role in the energy supply of the legume symbionts.
  • Three different mammalian sodium-dependent L-glutamate and aspartate high- affinity transporters (also known as excitatory amino acid transporters (EAAT)) [3,4,5]. These brain proteins are essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft.
  • EAAT-4, a mammalian chloride-dependent L-glutamate and aspartate high- affinity transporter [6].
  • Mammalian neutral amino acid transporter (SATT), a brain protein that plays a role in the transport of alanine, cysteine, serine and threonine [7].
  • Mammalian insulin-activated amino acid transporter (AAAT), an adipose tissue protein that transports serine and, to a lesser extent, alanine and glutamate [8].
  • Hypothetical protein ygjU from Escherichia coli and HI1545, the corresponding Haemophilus influenzae protein.

These transporters are proteins of from 420 to 573 amino acids which are highly hydrophobic and which probably contain about 10 transmembrane regions. As signature patterns, we selected two conserved regions. The first pattern is located in the N-terminal section and seems to include a hydrophilic region between two transmembrane regions. The second pattern is located in the C-terminal section.

Expert(s) to contact by email:

Hofmann K.

Last update:

December 2004 / Patterns and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

NA_DICARBOXYL_SYMP_2, PS00714; Sodium:dicarboxylate symporter family signature 2  (PATTERN)

NA_DICARBOXYL_SYMP_1, PS00713; Sodium:dicarboxylate symporter family signature 1  (PATTERN)


References

1AuthorsReizer J. Reizer A. Saier M.H. Jr.
TitleA functional superfamily of sodium/solute symporters.
SourceBiochim. Biophys. Acta 1197:133-166(1994).
PubMed ID8031825

2AuthorsStorck T. Schulte S. Hofmann K. Stoffel W.
TitleStructure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain.
SourceProc. Natl. Acad. Sci. U.S.A. 89:10955-10959(1992).
PubMed ID1279699

3AuthorsKanner B.I.
TitleGlutamate transporters from brain. A novel neurotransmitter transporter family.
SourceFEBS Lett. 325:95-99(1993).
PubMed ID8099882

4AuthorsKanai Y. Smith C.P. Hediger M.A.
TitleA new family of neurotransmitter transporters: the high-affinity glutamate transporters.
SourceFASEB J. 7:1450-1459(1993).
PubMed ID7903261

5AuthorsArriza J.L. Fairman W.A. Wadiche J.I. Murdoch G.H. Kavanaugh M.P. Amara S.G.
TitleFunctional comparisons of three glutamate transporter subtypes cloned from human motor cortex.
SourceJ. Neurosci. 14:5559-5569(1994).
PubMed ID7521911

6AuthorsFairman W.A. Vandenberg R.J. Arriza J.L. Kavanaugh M.P. Amara S.G.
TitleAn excitatory amino-acid transporter with properties of a ligand-gated chloride channel.
SourceNature 375:599-603(1995).
PubMed ID7791878
DOI10.1038/375599a0

7AuthorsArriza J.L. Kavanaugh M.P. Fairman W.A. Wu Y.N. Murdoch G.H. North R.A. Amara S.G.
TitleCloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family.
SourceJ. Biol. Chem. 268:15329-15332(1993).
PubMed ID8101838

8AuthorsLiao K. Lane M.D.
TitleExpression of a novel insulin-activated amino acid transporter gene during differentiation of 3T3-L1 preadipocytes into adipocytes.
SourceBiochem. Biophys. Res. Commun. 208:1008-1015(1995).
PubMed ID7702599



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)