{PDOC00591}
{PS00713; NA_DICARBOXYL_SYMP_1}
{PS00714; NA_DICARBOXYL_SYMP_2}
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* Sodium:dicarboxylate symporter family signatures *
****************************************************

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.

-Consensus pattern: P-x(0,1)-[GP]-[DES]-x-[LIVMF](2)-x-[LIVMA]-[LIVM]-[KREQS]-
                    [LIVMG]-[LIVM]-[LIVMF]-x-[PS]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for ygjU.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: P-x-G-x-[STA]-x-[NT]-[LIVMCP]-D-[GA]-[STANQF]-x-[LIVM]-
                    [FY]-x(2)-[LIVM]-x(2)-[LIVM]-[FY]-[LIV]-[SA]-[QH]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for ygjU.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Hofmann K.; kay.hofmann@memorec.com

-Last update: December 2004 / Patterns and text revised.

[ 1] Reizer J., Reizer A., Saier M.H. Jr.
     "A functional superfamily of sodium/solute symporters."
     Biochim. Biophys. Acta 1197:133-166(1994).
     PubMed=8031825
[ 2] Storck T., Schulte S., Hofmann K., Stoffel W.
     "Structure, expression, and functional analysis of a Na(+)-dependent
     glutamate/aspartate transporter from rat brain."
     Proc. Natl. Acad. Sci. U.S.A. 89:10955-10959(1992).
     PubMed=1279699
[ 3] Kanner B.I.
     "Glutamate transporters from brain. A novel neurotransmitter
     transporter family."
     FEBS Lett. 325:95-99(1993).
     PubMed=8099882
[ 4] Kanai Y., Smith C.P., Hediger M.A.
     "A new family of neurotransmitter transporters: the high-affinity
     glutamate transporters."
     FASEB J. 7:1450-1459(1993).
     PubMed=7903261
[ 5] Arriza J.L., Fairman W.A., Wadiche J.I., Murdoch G.H., Kavanaugh M.P.,
     Amara S.G.
     "Functional comparisons of three glutamate transporter subtypes cloned
     from human motor cortex."
     J. Neurosci. 14:5559-5569(1994).
     PubMed=7521911
[ 6] Fairman W.A., Vandenberg R.J., Arriza J.L., Kavanaugh M.P., Amara S.G.
     "An excitatory amino-acid transporter with properties of a
     ligand-gated chloride channel."
     Nature 375:599-603(1995).
     PubMed=7791878; DOI=10.1038/375599a0
[ 7] Arriza J.L., Kavanaugh M.P., Fairman W.A., Wu Y.N., Murdoch G.H.,
     North R.A., Amara S.G.
     "Cloning and expression of a human neutral amino acid transporter with
     structural similarity to the glutamate transporter gene family."
     J. Biol. Chem. 268:15329-15332(1993).
     PubMed=8101838
[ 8] Liao K., Lane M.D.
     "Expression of a novel insulin-activated amino acid transporter gene
     during differentiation of 3T3-L1 preadipocytes into adipocytes."
     Biochem. Biophys. Res. Commun. 208:1008-1015(1995).
     PubMed=7702599

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