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   02-SEP-2026, entry version 210.
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:7557442, PubMed:7698742, 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=K(+)(in) + L-glutamate(out) + 3 Na(+)(out) + H(+)(out) =
CC         K(+)(out) + L-glutamate(in) + 3 Na(+)(in) + H(+)(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=K(+)(in) + L-aspartate(out) + 3 Na(+)(out) + H(+)(out) =
CC         K(+)(out) + L-aspartate(in) + 3 Na(+)(in) + H(+)(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) + K(+)(in) + 3 Na(+)(out) + H(+)(out) = D-
CC         aspartate(in) + K(+)(out) + 3 Na(+)(in) + H(+)(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:7557442, PubMed:7698742, PubMed:9180080, PubMed:9373176).
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:16880397,
CC       PubMed:9180080). Mice are born at the expected Mendelian rate, but gain
CC       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_001077514.4. [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; 41.
DR   FunCoup; P43006; 390.
DR   IntAct; P43006; 6.
DR   MINT; P43006; -.
DR   STRING; 10090.ENSMUSP00000079100; -.
DR   GlyConnect; P43006; 13 N-Linked glycans (2 sites).
DR   GlyCosmos; P43006; 2 sites, 13 glycans.
DR   GlyGen; P43006; 5 sites, 15 N-linked glycans (2 sites), 1 O-linked glycan (3 sites).
DR   iPTMnet; P43006; -.
DR   PhosphoSitePlus; P43006; -.
DR   SwissPalm; P43006; -.
DR   jPOST; P43006; -.
DR   PaxDb; 10090-ENSMUSP00000079100; -.
DR   PeptideAtlas; P43006; -.
DR   ProteomicsDB; 277747; -. [P43006-1]
DR   ProteomicsDB; 277748; -. [P43006-2]
DR   ProteomicsDB; 277749; -. [P43006-3]
DR   Antibodypedia; 2179; 335 antibodies from 36 providers.
DR   DNASU; 20511; -.
DR   Ensembl; ENSMUST00000005220.11; ENSMUSP00000005220.5; ENSMUSG00000005089.16. [P43006-3]
DR   Ensembl; ENSMUST00000080210.10; ENSMUSP00000079100.4; ENSMUSG00000005089.16. [P43006-1]
DR   Ensembl; ENSMUST00000111212.8; ENSMUSP00000106843.2; ENSMUSG00000005089.16. [P43006-2]
DR   GeneID; 20511; -.
DR   KEGG; mmu:20511; -.
DR   UCSC; uc008lid.2; mouse. [P43006-1]
DR   AGR; MGI:101931; -.
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; TWTKEID; -.
DR   OrthoDB; 5877963at2759; -.
DR   PhylomeDB; P43006; -.
DR   Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR   Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-MMU-9958863; SLC-mediated transport of amino acids.
DR   BioGRID-ORCS; 20511; 0 hits in 78 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P43006; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P43006; protein.
DR   Bgee; ENSMUSG00000005089; Expressed in lateral septal nucleus and 148 other cell types or tissues.
DR   ExpressionAtlas; P43006; baseline and differential.
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:GO_Central.
DR   GO; GO:0043198; C:dendritic shaft; ISO:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0098796; C:membrane protein complex; ISO:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IDA: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:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0031982; C:vesicle; 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:0033229; F:L-cysteine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR   GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:GO_Central.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IDA:MGI.
DR   GO; GO:0140009; P:L-aspartate import across plasma membrane; ISO:GO_Central.
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:0098656; P:monoatomic anion transmembrane transport; IDA: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; IDA:SynGO.
DR   GO; GO:0046326; P:positive regulation of D-glucose import across plasma membrane; 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   FunFam; 1.10.3860.10:FF:000002; Amino acid transporter; 1.
DR   Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR   InterPro; IPR050746; DAACS.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   PANTHER; PTHR11958:SF93; EXCITATORY AMINO ACID TRANSPORTER 2; 1.
DR   PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   SUPFAM; SSF118215; Proton glutamate symport protein; 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   COMPBIAS        1..11
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Basic and acidic residues"
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
FT                   Glt-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
//