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Excitatory amino acid transporter 1 (Glial high affinity glutamate transporter) (High-affinity neuronal glutamate transporter) (GluT-1) (Sodium-dependent glutamate/aspartate transporter 1) (GLAST-1) (Solute carrier family 1 member 3)

 EAA1_MOUSE              Reviewed;         543 AA.
P56564; Q99P53;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
05-MAR-2002, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Excitatory amino acid transporter 1;
AltName: Full=Glial high affinity glutamate transporter;
AltName: Full=High-affinity neuronal glutamate transporter;
Short=GluT-1 {ECO:0000303|PubMed:7903437};
AltName: Full=Sodium-dependent glutamate/aspartate transporter 1;
Short=GLAST-1;
AltName: Full=Solute carrier family 1 member 3;
Name=Slc1a3; Synonyms=Eaat1, Gmt1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=7903437; DOI=10.1016/0304-3940(93)90829-A;
Tanaka K.;
"Cloning and expression of a glutamate transporter from mouse brain.";
Neurosci. Lett. 159:183-186(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Neural stem cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 80-114; 161-175; 189-196; 269-280 AND 480-499, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15363892; DOI=10.1016/j.molbrainres.2004.06.026;
Stoffel W., Koerner R., Wachtmann D., Keller B.U.;
"Functional analysis of glutamate transporters in excitatory synaptic
transmission of GLAST1 and GLAST1/EAAC1 deficient mice.";
Brain Res. Mol. Brain Res. 128:170-181(2004).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15390100; DOI=10.1002/glia.20097;
Sarthy V.P., Pignataro L., Pannicke T., Weick M., Reichenbach A.,
Harada T., Tanaka K., Marc R.;
"Glutamate transport by retinal Muller cells in glutamate/aspartate
transporter-knockout mice.";
Glia 49:184-196(2005).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=16880397; DOI=10.1073/pnas.0509144103;
Matsugami T.R., Tanemura K., Mieda M., Nakatomi R., Yamada K.,
Kondo T., Ogawa M., Obata K., Watanabe M., Hashikawa T., Tanaka K.;
"Indispensability of the glutamate transporters GLAST and GLT1 to
brain development.";
Proc. Natl. Acad. Sci. U.S.A. 103:12161-12166(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206; ASN-215 AND ASN-216.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=28032905; DOI=10.1002/1873-3468.12549;
Krycer J.R., Fazakerley D.J., Cater R.J., C Thomas K., Naghiloo S.,
Burchfield J.G., Humphrey S.J., Vandenberg R.J., Ryan R.M.,
James D.E.;
"The amino acid transporter, SLC1A3, is plasma membrane-localised in
adipocytes and its activity is insensitive to insulin.";
FEBS Lett. 591:322-330(2017).
-!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter
that mediates the uptake of L-glutamate and also L-aspartate and
D-aspartate (PubMed:7903437, PubMed:28032905). Functions as a
symporter that transports one amino acid molecule together with
two or three Na(+) ions and one proton, in parallel with the
counter-transport of one K(+) ion (By similarity). Plays a
redundant role in the rapid removal of released glutamate from the
synaptic cleft, which is essential for terminating the
postsynaptic action of glutamate (PubMed:15363892,
PubMed:15390100,PubMed:16880397). {ECO:0000250|UniProtKB:O57321,
ECO:0000269|PubMed:15363892, ECO:0000269|PubMed:15390100,
ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:28032905,
ECO:0000269|PubMed:7903437}.
-!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P43003}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28032905,
ECO:0000269|PubMed:7903437}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Detected in brain, in Bergmann glia arborising
into the molecular layer of the cerebellum (at protein level)
(PubMed:15363892). Localized in brain and is highly enriched in
the Purkinje cell layer in cerebellum. Intermediate level in lung,
low level in spleen, skeletal muscle and testis.
{ECO:0000269|PubMed:7903437}.
-!- DOMAIN: Contains eight transmembrane regions plus two helical
hairpins that dip into the membrane. These helical hairpin
structures play an important role in the transport process. The
first enters the membrane from the cytoplasmic side, the second
one from the extracellular side. During the transport cycle, the
regions involved in amino acid transport, and especially the
helical hairpins, move vertically by about 15-18 Angstroms,
alternating between exposure to the aqueous phase and reinsertion
in the lipid bilayer. In contrast, the regions involved in
trimerization do not move. {ECO:0000250|UniProtKB:P43003}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:19656770}.
-!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:15363892,
PubMed:15390100). Mutant mice display normal locomotion, motor
coordination and learning, and globally normal glutamate uptake in
brain vesicle preparations (PubMed:15363892). The decay time of
glutamate receptor mediated excitatory postsynaptic currents
(EPSCs) in cerebellar Purkinje is slightly increased
(PubMed:15363892). The decreased rate of glutamate uptake in
retina Mueller cells from mutant mice suggests that Slc1a3
accounts for about half of the glutamate uptake activity in wild-
type cells (PubMed:15390100). Mice deficient in both Slc1a2 and
Slc1a3 die at about 17 dpc (PubMed:16880397).
{ECO:0000269|PubMed:15363892, ECO:0000269|PubMed:15390100,
ECO:0000269|PubMed:16880397}.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A3 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF330257; AAK01708.1; -; mRNA.
EMBL; BC058711; AAH58711.1; -; mRNA.
EMBL; BC066154; AAH66154.1; -; mRNA.
CCDS; CCDS27373.1; -.
RefSeq; NP_683740.1; NM_148938.3.
UniGene; Mm.204834; -.
ProteinModelPortal; P56564; -.
BioGrid; 203291; 5.
IntAct; P56564; 2.
MINT; MINT-4996875; -.
STRING; 10090.ENSMUSP00000005493; -.
iPTMnet; P56564; -.
PhosphoSitePlus; P56564; -.
SwissPalm; P56564; -.
PaxDb; P56564; -.
PeptideAtlas; P56564; -.
PRIDE; P56564; -.
Ensembl; ENSMUST00000005493; ENSMUSP00000005493; ENSMUSG00000005360.
GeneID; 20512; -.
KEGG; mmu:20512; -.
UCSC; uc007vex.1; mouse.
CTD; 6507; -.
MGI; MGI:99917; Slc1a3.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; P56564; -.
KO; K05614; -.
OMA; TFAFSSR; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; P56564; -.
TreeFam; TF315206; -.
Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
PRO; PR:P56564; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000005360; -.
ExpressionAtlas; P56564; baseline and differential.
Genevisible; P56564; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0016597; F:amino acid binding; IDA:MGI.
GO; GO:0016595; F:glutamate binding; IDA:MGI.
GO; GO:0015501; F:glutamate:sodium symporter activity; ISS:UniProtKB.
GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IDA:MGI.
GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031223; P:auditory behavior; IMP:MGI.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
GO; GO:0021545; P:cranial nerve development; IMP:MGI.
GO; GO:0070779; P:D-aspartate import; IMP:UniProtKB.
GO; GO:0140016; P:D-aspartate import across plasma membrane; ISS:UniProtKB.
GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:MGI.
GO; GO:0006537; P:glutamate biosynthetic process; IMP:MGI.
GO; GO:0006536; P:glutamate metabolic process; IMP:MGI.
GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:UniProtKB.
GO; GO:0051938; P:L-glutamate import; IMP:MGI.
GO; GO:0098712; P:L-glutamate import across plasma membrane; ISS:UniProtKB.
GO; GO:0089711; P:L-glutamate transmembrane transport; ISO:MGI.
GO; GO:0015813; P:L-glutamate transport; IDA:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0043200; P:response to amino acid; ISO:MGI.
GO; GO:0046677; P:response to antibiotic; IMP:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
GO; GO:0009416; P:response to light stimulus; IMP:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
Gene3D; 1.10.3860.10; -; 1.
InterPro; IPR036458; Na-dicarbo_symporter_sf.
InterPro; IPR001991; Na-dicarboxylate_symporter.
InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
Pfam; PF00375; SDF; 1.
PRINTS; PR00173; EDTRNSPORT.
SUPFAM; SSF118215; SSF118215; 2.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Chloride; Complete proteome;
Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
Phosphoprotein; Potassium; Reference proteome; Sodium; Symport;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 543 Excitatory amino acid transporter 1.
/FTId=PRO_0000202058.
TOPO_DOM 1 47 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 48 68 Helical; Name=1.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 69 86 Extracellular.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 87 108 Helical; Name=2.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 109 122 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 123 145 Helical; Name=3.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 146 236 Extracellular.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 237 260 Helical; Name=4.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 261 269 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 270 297 Helical; Name=5.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 298 318 Extracellular.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 319 340 Helical; Name=6.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 341 345 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
INTRAMEM 346 376 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 377 385 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 386 412 Helical; Name=7.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 413 425 Extracellular.
{ECO:0000250|UniProtKB:P43003}.
INTRAMEM 426 459 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 460 472 Extracellular.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 473 494 Helical; Name=8.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 495 543 Cytoplasmic.
{ECO:0000250|UniProtKB:P43003}.
REGION 363 365 Aspartate binding.
{ECO:0000250|UniProtKB:O59010}.
REGION 443 447 Aspartate binding.
{ECO:0000250|UniProtKB:P43003}.
COMPBIAS 363 366 Poly-Ser.
METAL 394 394 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 396 396 Sodium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 398 398 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
METAL 483 483 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 487 487 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
BINDING 402 402 Aspartate.
{ECO:0000250|UniProtKB:O59010}.
BINDING 476 476 Aspartate.
{ECO:0000250|UniProtKB:O59010}.
BINDING 483 483 Aspartate.
{ECO:0000250|UniProtKB:O59010}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
SEQUENCE 543 AA; 59622 MW; E0B24CBA1D5B086D CRC64;
MTKSNGEEPR MGGRMERLQQ GVRKRTLLAK KKVQSLTKED VKSYLFRNAF VLLTVTAVIV
GTILGFALRP YKMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG
MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMYREGK IVQVTAADAF LDLIRNMFPP
NLVEACFKQF KTSYEKRSFK VPIQSNETLL GAVINNVSEA METLTRIREE MVPVPGSVNG
VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP LGILFLIAGK
IVEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL
GTSSSSATLP ITFKCLEENN GVDKRITRFV LPVGATINMD GTALYEALAA IFIAQVNNFD
LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT
TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLIAQDN EPEKPVADSE
TKM


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