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2.A.23.2.1
Glutamate/aspartate:Na+ symporter, GLAST or EAAT1, Structural rearrangements have been probed by Leighton et al., 2006). EAAT1 interacts directly with the Na+, K+-ATPase (TC #3.A.3.1) (Rose et al., 2009). CEAT1 couples glutamate uptake to the symport of 3 Na+ and 1 H+ followed by the antiport of 1 K+. It can function as an uncoupled anion, water and/or urea channel (Vandenberg et al., 2011). Large collective motions regulate the functional properties of EAAT1 trimers (Jiang et al., 2011).  The reentrant helical hairpin loop, HP1, functions during the transport cycle as the proposed internal gate.  HP1 is packed against transmembrane domain, TMS 2 and TMS5 in its closed state, and two residues located in TM2 and HP2 of EAAT1 are in close proximity (Zhang et al. 2014).  In EAAT1, R388 is a critical element for the structural coupling between the substrate translocation and the gating mechanisms of the EAAT-associated anion channel, and conversion to E or D creates a constitutively open anion channel (Torres-Salazar et al. 2015).

Accession Number:P24942
Protein Name:EAA1 aka EAAT1 aka SLC1A3
Length:543
Molecular Weight:59697.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate glutamate, aspartate, Na+, H+, K+

Cross database links:

Genevestigator: P24942
eggNOG: roNOG12449
RefSeq: NP_062098.1   
Entrez Gene ID: 29483   
Pfam: PF00375   
KEGG: rno:29483   

Gene Ontology

GO:0016323 C:basolateral plasma membrane
GO:0043197 C:dendritic spine
GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0005743 C:mitochondrial inner membrane
GO:0045202 C:synapse
GO:0005314 F:high-affinity glutamate transmembrane trans...
GO:0017153 F:sodium:dicarboxylate symporter activity
GO:0006835 P:dicarboxylic acid transport
GO:0043490 P:malate-aspartate shuttle
GO:0006836 P:neurotransmitter transport
GO:0010035 P:response to inorganic substance

References (5)

[1] “Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain.”  Storck T.et.al.   1279699
[2] “Expression cloning of a rat glutamate transporter.”  Tanaka K.et.al.   8387171
[3] “The open reading frame of the Na(+)-dependent glutamate transporter GLAST-1 is expressed in bone and a splice variant of this molecule is expressed in bone and brain.”  Huggett J.et.al.   11086157
[4] “UDP galactose:ceramide galactosyltransferase and glutamate/aspartate transporter. Copurification, separation and characterization of the two glycoproteins.”  Schulte S.et.al.   8521863
[5] “Identification of a glutamate/aspartate transporter in the rat cochlea.”  Li H.S.et.al.   7527019

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTKSNGEEPR MGSRMERFQQ GVRKRTLLAK KKVQNITKED VKSYLFRNAF VLLTVSAVIV 
61:	GTILGFALRP YKMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG 
121:	MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMYREGK IVQVTAADAF LDLIRNMFPP 
181:	NLVEACFKQF KTSYEKRSFK VPIQANETLL GAVINNVSEA METLTRIREE MVPVPGSVNG 
241:	VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP LGILFLIAGK 
301:	ILEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL 
361:	GTSSSSATLP ITFKCLEENN GVDKRITRFV LPVGATINMD GTALYEALAA IFIAQVNNFD 
421:	LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT 
481:	TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLIAQDN EPEKPVADSE 
541:	TKM