EAA2_MOUSE
ID EAA2_MOUSE Reviewed; 572 AA.
AC P43006; O35877; O54686; O54687;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Excitatory amino acid transporter 2;
DE AltName: Full=GLT-1 {ECO:0000303|PubMed:9180080, ECO:0000303|PubMed:9373176};
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 2;
DE AltName: Full=Solute carrier family 1 member 2;
GN Name=Slc1a2; Synonyms=Eaat2, Glt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7698742; DOI=10.1006/geno.1994.1609;
RA Kirschner M.A., Copeland N.G., Gilbert D.J., Jenkins N.A., Amara S.G.;
RT "Mouse excitatory amino acid transporter EAAT2: isolation,
RT characterization, and proximity to neuroexcitability loci on mouse
RT chromosome 2.";
RL Genomics 24:218-224(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=JCL:ICR; TISSUE=Cerebellum;
RX PubMed=7766664; DOI=10.1016/0304-4165(95)00062-g;
RA Mukainaka Y., Tanaka K., Hagiwara T., Wada K.;
RT "Molecular cloning of two glutamate transporter subtypes from mouse
RT brain.";
RL Biochim. Biophys. Acta 1244:233-237(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7557442; DOI=10.1016/0378-1119(95)00293-f;
RA Sutherland M.L., Delaney T.A., Noebels J.L.;
RT "Molecular characterization of a high-affinity mouse glutamate
RT transporter.";
RL Gene 162:271-274(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Peng J.-B., Guo L.-H.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=JCL:ICR; TISSUE=Brain, and Liver;
RX PubMed=9373176; DOI=10.1016/s0014-5793(97)01232-5;
RA Utsunomiya-Tate N., Endou H., Kanai Y.;
RT "Tissue specific variants of glutamate transporter GLT-1.";
RL FEBS Lett. 416:312-316(1997).
RN [6]
RP PROTEIN SEQUENCE OF 66-87; 159-173 AND 478-525, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9180080; DOI=10.1126/science.276.5319.1699;
RA Tanaka K., Watase K., Manabe T., Yamada K., Watanabe M., Takahashi K.,
RA Iwama H., Nishikawa T., Ichihara N., Kikuchi T., Okuyama S., Kawashima N.,
RA Hori S., Takimoto M., Wada K.;
RT "Epilepsy and exacerbation of brain injury in mice lacking the glutamate
RT transporter GLT-1.";
RL Science 276:1699-1702(1997).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16880397; DOI=10.1073/pnas.0509144103;
RA Matsugami T.R., Tanemura K., Mieda M., Nakatomi R., Yamada K., Kondo T.,
RA Ogawa M., Obata K., Watanabe M., Hashikawa T., Tanaka K.;
RT "Indispensability of the glutamate transporters GLAST and GLT1 to brain
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12161-12166(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-505; SER-520;
RP SER-530; SER-532; SER-542; SER-558 AND SER-562, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP PALMITOYLATION AT CYS-38, AND MUTAGENESIS OF CYS-38.
RX PubMed=20685337; DOI=10.1016/j.nbd.2010.05.027;
RA Huang K., Kang M.H., Askew C., Kang R., Sanders S.S., Wan J., Davis N.G.,
RA Hayden M.R.;
RT "Palmitoylation and function of glial glutamate transporter-1 is reduced in
RT the YAC128 mouse model of Huntington disease.";
RL Neurobiol. Dis. 40:207-215(2010).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates the uptake of L-glutamate and also L-aspartate and D-aspartate
CC (PubMed:7698742, PubMed:7557442, PubMed:9373176). Functions as a
CC symporter that transports one amino acid molecule together with two or
CC three Na(+) ions and one proton, in parallel with the counter-transport
CC of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid
CC transport; this avoids the accumulation of negative charges due to
CC aspartate and Na(+) symport (By similarity). Essential for the rapid
CC removal of released glutamate from the synaptic cleft, and for
CC terminating the postsynaptic action of glutamate (PubMed:9180080).
CC {ECO:0000250|UniProtKB:P43004, ECO:0000269|PubMed:7557442,
CC ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080,
CC ECO:0000269|PubMed:9373176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000305|PubMed:7698742};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000250|UniProtKB:P43004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-
CC aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29990;
CC Evidence={ECO:0000250|UniProtKB:P43004};
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with AJUBA (By
CC similarity). {ECO:0000250|UniProtKB:P31596,
CC ECO:0000250|UniProtKB:P43004}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7557442,
CC ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9373176}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P43004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Glt-1;
CC IsoId=P43006-1; Sequence=Displayed;
CC Name=Glt-1A;
CC IsoId=P43006-2; Sequence=VSP_006264;
CC Name=Glt-1B;
CC IsoId=P43006-3; Sequence=VSP_006264, VSP_006265;
CC -!- TISSUE SPECIFICITY: Detected in brain (PubMed:9180080). Detected in
CC embryonic forebrain, especially in globus pallidus, perirhinal cortex,
CC lateral hypothalamus, hippocampus, and on fimbria and axonal pathways
CC connecting the neocortex, basal ganglia and thalamus (at protein level)
CC (PubMed:16880397). Isoform GLT1 is expressed in the brain
CC (PubMed:7698742, PubMed:7557442, PubMed:9373176, PubMed:9180080).
CC Isoforms GLT-1A and GLT-1B are expressed in the liver (PubMed:9373176).
CC {ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:7557442,
CC ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080,
CC ECO:0000269|PubMed:9373176}.
CC -!- DOMAIN: Contains eight transmembrane regions plus two helical hairpins
CC that dip into the membrane. These helical hairpin structures play an
CC important role in the transport process. The first enters the membrane
CC from the cytoplasmic side, the second one from the extracellular side.
CC During the transport cycle, the regions involved in amino acid
CC transport, and especially the helical hairpins, move vertically by
CC about 15-18 Angstroms, alternating between exposure to the aqueous
CC phase and reinsertion in the lipid bilayer. In contrast, the regions
CC involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P43004}.
CC -!- PTM: Palmitoylation at Cys-38 is not required for correct subcellular
CC localization, but is important for glutamate uptake activity.
CC {ECO:0000269|PubMed:20685337}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at birth (PubMed:9180080,
CC PubMed:16880397). Mice are born at the expected Mendelian rate, but
CC gain weight more slowly, especially after the first 30 days after birth
CC (PubMed:9180080). Only half of them are still alive 60 days after birth
CC (PubMed:9180080). Death is due to spontaneous epileptic seizures
CC (PubMed:9180080). Besides, mutant mice display neuronal degeneration in
CC the hippocampus CA1 field, probably due to impaired glutamate removal
CC from the synaptic cleft (PubMed:9180080). Glutamate uptake by
CC synaptosomes from mutant mouse brain cortex is reduced by 94%
CC (PubMed:9180080). Mice deficient in both Slc1a2 and Slc1a3 die at about
CC 17 dpc; they display defects in the brain structure that affects the
CC brain cortex, hippocampus and olfactory bulb, due to impaired radial
CC migration of neurons into the cortical plate and disorganization of the
CC radial glial cell arrangement (PubMed:16880397).
CC {ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:9180080}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A2 subfamily. {ECO:0000305}.
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DR EMBL; U11763; AAA77673.1; -; mRNA.
DR EMBL; D43796; BAA07854.1; -; mRNA.
DR EMBL; U24699; AAA91643.1; -; mRNA.
DR EMBL; U75372; AAB71737.1; -; mRNA.
DR EMBL; U75373; AAB71738.1; -; mRNA.
DR EMBL; AB007810; BAA23770.1; -; mRNA.
DR EMBL; AB007811; BAA23771.1; -; mRNA.
DR EMBL; AB007812; BAA23772.1; -; mRNA.
DR CCDS; CCDS16469.1; -. [P43006-3]
DR CCDS; CCDS38188.1; -. [P43006-1]
DR CCDS; CCDS38189.1; -. [P43006-2]
DR PIR; A55676; A55676.
DR PIR; JC4262; JC4262.
DR RefSeq; NP_001070982.1; NM_001077514.3. [P43006-1]
DR RefSeq; NP_001070983.1; NM_001077515.2. [P43006-2]
DR RefSeq; NP_035523.1; NM_011393.2. [P43006-3]
DR AlphaFoldDB; P43006; -.
DR SMR; P43006; -.
DR BioGRID; 203290; 11.
DR IntAct; P43006; 6.
DR MINT; P43006; -.
DR STRING; 10090.ENSMUSP00000079100; -.
DR GlyConnect; 2306; 13 N-Linked glycans (2 sites).
DR GlyGen; P43006; 2 sites, 13 N-linked glycans (2 sites).
DR iPTMnet; P43006; -.
DR PhosphoSitePlus; P43006; -.
DR SwissPalm; P43006; -.
DR jPOST; P43006; -.
DR MaxQB; P43006; -.
DR PaxDb; P43006; -.
DR PeptideAtlas; P43006; -.
DR PRIDE; P43006; -.
DR ProteomicsDB; 277747; -. [P43006-1]
DR ProteomicsDB; 277748; -. [P43006-2]
DR ProteomicsDB; 277749; -. [P43006-3]
DR Antibodypedia; 2179; 312 antibodies from 33 providers.
DR DNASU; 20511; -.
DR Ensembl; ENSMUST00000005220; ENSMUSP00000005220; ENSMUSG00000005089. [P43006-3]
DR Ensembl; ENSMUST00000080210; ENSMUSP00000079100; ENSMUSG00000005089. [P43006-1]
DR Ensembl; ENSMUST00000111212; ENSMUSP00000106843; ENSMUSG00000005089. [P43006-2]
DR GeneID; 20511; -.
DR KEGG; mmu:20511; -.
DR UCSC; uc008lid.2; mouse. [P43006-1]
DR CTD; 6506; -.
DR MGI; MGI:101931; Slc1a2.
DR VEuPathDB; HostDB:ENSMUSG00000005089; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155379; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P43006; -.
DR OMA; YLYIAVI; -.
DR PhylomeDB; P43006; -.
DR TreeFam; TF315206; -.
DR Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR BioGRID-ORCS; 20511; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Slc1a2; mouse.
DR PRO; PR:P43006; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P43006; protein.
DR Bgee; ENSMUSG00000005089; Expressed in lateral septal nucleus and 147 other tissues.
DR ExpressionAtlas; P43006; baseline and differential.
DR Genevisible; P43006; MM.
DR GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0098796; C:membrane protein complex; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0008509; F:anion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0033229; F:cysteine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:MGI.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0098656; P:anion transmembrane transport; IDA:MGI.
DR GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:MGI.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:MGI.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IEA:Ensembl.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IBA:GO_Central.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0098810; P:neurotransmitter reuptake; IMP:SynGO.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IMP:MGI.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR GO; GO:0007632; P:visual behavior; IMP:MGI.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Chloride;
KW Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Potassium; Reference proteome;
KW Sodium; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..572
FT /note="Excitatory amino acid transporter 2"
FT /id="PRO_0000202062"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..258
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 268..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 317..338
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 344..374
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 384..410
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 424..457
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 471..492
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361..363
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 392
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 394
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 396
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 400
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 441..445
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 474
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 481
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 481
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 485
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31596"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31596"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31596"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 38
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:20685337"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..6
FT /note="MASTEG -> MVS (in isoform Glt-1A and isoform Glt-
FT 1B)"
FT /evidence="ECO:0000305"
FT /id="VSP_006264"
FT VAR_SEQ 551..572
FT /note="TLAANGKSADCSVEEEPWKREK -> PFPFLDIETCI (in isoform
FT Glt-1B)"
FT /evidence="ECO:0000305"
FT /id="VSP_006265"
FT MUTAGEN 38
FT /note="C->S: Severely impairs glutamate uptake activity."
FT /evidence="ECO:0000269|PubMed:20685337"
FT CONFLICT 26
FT /note="D -> E (in Ref. 3; AAA91643)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="G -> R (in Ref. 3; AAA91643)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="A -> V (in Ref. 3; AAA91643)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="T -> I (in Ref. 4; AAB71737)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="K -> L (in Ref. 4; AAB71737)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="K -> EFD (in Ref. 3; AAA91643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 62030 MW; 13C7C30DED40CA81 CRC64;
MASTEGANNM PKQVEVRMHD SHLSSDEPKH RNLGMRMCDK LGKNLLLSLT VFGVILGAVC
GGLLRLASPI HPDVVMLIAF PGDILMRMLK MLILPLIISS LITGLSGLDA KASGRLGTRA
MVYYMSTTII AAVLGVILVL AIHPGNPKLK KQLGPGKKND EVSSLDAFLD LIRNLFPENL
VQACFQQIQT VTKKVLVAPP SEEANTTKAV ISMLNETMNE APEETKIVIK KGLEFKDGMN
VLGLIGFFIA FGIAMGKMGE QAKLMVEFFN ILNEIVMKLV IMIMWYSPLG IACLICGKII
AIKDLEVVAR QLGMYMITVI VGLIIHGGIF LPLIYFVVTR KNPFSFFAGI FQAWITALGT
ASSAGTLPVT FRCLEDNLGI DKRVTRFVLP VGATINMDGT ALYEAVAAIF IAQMNGVILD
GGQIVTVSLT ATLASIGAAS IPSAGLVTML LILTAVGLPT EDISLLVAVD WLLDRMRTSV
NVVGDSFGAG IVYHLSKSEL DTIDSQHRMQ EDIEMTKTQS IYDDKNHRES NSNQCVYAAH
NSVVIDECKV TLAANGKSAD CSVEEEPWKR EK
