Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Excitatory amino acid transporter 1 (Sodium-dependent glutamate/aspartate transporter 1) (GLAST-1) (Solute carrier family 1 member 3)

 EAA1_HUMAN              Reviewed;         542 AA.
P43003; B2R5T3; Q4JCQ8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=Excitatory amino acid transporter 1 {ECO:0000303|PubMed:16042756, ECO:0000303|PubMed:8647279};
AltName: Full=Sodium-dependent glutamate/aspartate transporter 1 {ECO:0000303|PubMed:8647279};
Short=GLAST-1 {ECO:0000303|PubMed:8647279};
AltName: Full=Solute carrier family 1 member 3;
Name=SLC1A3;
Synonyms=EAAT1 {ECO:0000303|PubMed:16042756,
ECO:0000303|PubMed:8647279}, GLAST,
GLAST1 {ECO:0000303|PubMed:8647279};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Cerebellum;
PubMed=8218410; DOI=10.1016/0167-4781(93)90057-K;
Shashidharan P., Plaitakis A.;
"Cloning and characterization of a glutamate transporter cDNA from
human cerebellum.";
Biochim. Biophys. Acta 1216:161-164(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain cortex;
PubMed=7521911;
Arriza J.L., Fairman W.A., Wendy 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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8123008; DOI=10.1006/bbrc.1994.1210;
Kawakami H., Tanaka K., Nakayama T., Inoue K., Nakamura S.;
"Cloning and expression of a human glutamate transporter.";
Biochem. Biophys. Res. Commun. 199:171-176(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8647279; DOI=10.1016/0014-5793(96)00424-3;
Stoffel W., Sasse J., Dueker M., Mueller R., Hofmann K.O., Fink T.,
Lichter P.;
"Human high affinity, Na(+)-dependent L-glutamate/L-aspartate
transporter GLAST-1 (EAAT-1): gene structure and localization to
chromosome 5p11-p12.";
FEBS Lett. 386:189-193(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=16042756; DOI=10.1111/j.1471-4159.2005.03370.x;
Vallejo-Illarramendi A., Domercq M., Matute C.;
"A novel alternative splicing form of excitatory amino acid
transporter 1 is a negative regulator of glutamate uptake.";
J. Neurochem. 95:341-348(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-363 AND
ARG-477.
PubMed=20477940; DOI=10.1111/j.1471-4159.2010.06796.x;
Ryan R.M., Kortt N.C., Sirivanta T., Vandenberg R.J.;
"The position of an arginine residue influences substrate affinity and
K+ coupling in the human glutamate transporter, EAAT1.";
J. Neurochem. 114:565-575(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=26690923; DOI=10.1007/s00232-015-9863-0;
Abousaab A., Warsi J., Elvira B., Lang F.;
"Caveolin-1 Sensitivity of Excitatory Amino Acid Transporters EAAT1,
EAAT2, EAAT3, and EAAT4.";
J. Membr. Biol. 249:239-249(2016).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-523.
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).
[15]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-148 AND 243-542 IN
COMPLEXES WITH SODIUM; ASPARTATE AND ALLOSTERIC INHIBITOR, FUNCTION,
TOPOLOGY, SUBUNIT, AND DOMAIN.
PubMed=28424515; DOI=10.1038/nature22064;
Canul-Tec J.C., Assal R., Cirri E., Legrand P., Brier S.,
Chamot-Rooke J., Reyes N.;
"Structure and allosteric inhibition of excitatory amino acid
transporter 1.";
Nature 544:446-451(2017).
[16]
VARIANT EA6 ARG-290.
PubMed=16116111; DOI=10.1212/01.WNL.0000172638.58172.5a;
Jen J.C., Wan J., Palos T.P., Howard B.D., Baloh R.W.;
"Mutation in the glutamate transporter EAAT1 causes episodic ataxia,
hemiplegia, and seizures.";
Neurology 65:529-534(2005).
-!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter
that mediates the uptake of L-glutamate and also L-aspartate and
D-aspartate (PubMed:7521911, PubMed:8123008, PubMed:20477940,
PubMed:26690923, PubMed:28032905, PubMed:28424515). 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 (PubMed:20477940). Mediates
Cl(-) flux that is not coupled to amino acid transport; this
avoids the accumulation of negative charges due to aspartate and
Na(+) symport (PubMed:20477940). 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
(By similarity). {ECO:0000250|UniProtKB:P56564,
ECO:0000269|PubMed:20477940, ECO:0000269|PubMed:26690923,
ECO:0000269|PubMed:28032905, ECO:0000269|PubMed:28424515,
ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:8123008}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=525 uM for L-glutamate {ECO:0000269|PubMed:26690923};
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:28424515}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20477940,
ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:28032905,
ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:8123008}; Multi-
pass membrane protein {ECO:0000269|PubMed:28424515}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43003-1; Sequence=Displayed;
Name=2; Synonyms=EAAT1ex9skip;
IsoId=P43003-2; Sequence=VSP_043913;
Note=Expressed throughout the CNS, both in gray matter and
axonal tracts, at levels ranging between 10% and 20% of isoform
1. Localizes to ER, has no functional glutamate uptake activity,
and exerts a dominant negative effect isoform 1.;
-!- TISSUE SPECIFICITY: Detected in brain (PubMed:8218410,
PubMed:7521911, PubMed:8123008). Detected at very much lower
levels in heart, lung, placenta and skeletal muscle
(PubMed:7521911, PubMed:8123008). Highly expressed in cerebellum,
but also found in frontal cortex, hippocampus and basal ganglia
(PubMed:7521911). {ECO:0000269|PubMed:7521911,
ECO:0000269|PubMed:8123008, ECO:0000269|PubMed:8218410}.
-!- 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:0000305|PubMed:28424515}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P24942}.
-!- DISEASE: Episodic ataxia 6 (EA6) [MIM:612656]: A disorder
characterized by episodic ataxia, seizures, migraine and
alternating hemiplegia. {ECO:0000269|PubMed:16116111}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A3 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L19158; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U03504; AAA50428.1; -; mRNA.
EMBL; D26443; BAA05462.1; -; mRNA.
EMBL; Z31713; CAA83507.1; -; Genomic_DNA.
EMBL; Z31703; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31704; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31705; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31706; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31707; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31708; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31709; CAA83507.1; JOINED; Genomic_DNA.
EMBL; Z31710; CAA83507.1; JOINED; Genomic_DNA.
EMBL; AY954110; AAY28724.1; -; mRNA.
EMBL; AK312304; BAG35230.1; -; mRNA.
EMBL; AC008957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471119; EAW55945.1; -; Genomic_DNA.
CCDS; CCDS3919.1; -. [P43003-1]
CCDS; CCDS54844.1; -. [P43003-2]
PIR; S38353; S38353.
RefSeq; NP_001160167.1; NM_001166695.2. [P43003-2]
RefSeq; NP_001276869.1; NM_001289940.1.
RefSeq; NP_004163.3; NM_004172.4. [P43003-1]
RefSeq; XP_005248399.1; XM_005248342.2. [P43003-1]
UniGene; Hs.481918; -.
PDB; 5LLM; X-ray; 3.25 A; A=1-148, A=243-542.
PDB; 5LLU; X-ray; 3.32 A; A=1-148, A=243-542.
PDB; 5LM4; X-ray; 3.10 A; A=1-148, A=243-542.
PDB; 5MJU; X-ray; 3.71 A; A=1-148, A=243-542.
PDBsum; 5LLM; -.
PDBsum; 5LLU; -.
PDBsum; 5LM4; -.
PDBsum; 5MJU; -.
ProteinModelPortal; P43003; -.
SMR; P43003; -.
BioGrid; 112398; 7.
IntAct; P43003; 3.
MINT; MINT-5004226; -.
STRING; 9606.ENSP00000265113; -.
BindingDB; P43003; -.
ChEMBL; CHEMBL3085; -.
DrugBank; DB00142; L-Glutamic Acid.
GuidetoPHARMACOLOGY; 868; -.
TCDB; 2.A.23.2.6; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
iPTMnet; P43003; -.
PhosphoSitePlus; P43003; -.
SwissPalm; P43003; -.
BioMuta; SLC1A3; -.
DMDM; 1169458; -.
MaxQB; P43003; -.
PaxDb; P43003; -.
PeptideAtlas; P43003; -.
PRIDE; P43003; -.
Ensembl; ENST00000265113; ENSP00000265113; ENSG00000079215. [P43003-1]
Ensembl; ENST00000381918; ENSP00000371343; ENSG00000079215. [P43003-2]
GeneID; 6507; -.
KEGG; hsa:6507; -.
UCSC; uc003jkj.4; human. [P43003-1]
CTD; 6507; -.
DisGeNET; 6507; -.
EuPathDB; HostDB:ENSG00000079215.13; -.
GeneCards; SLC1A3; -.
HGNC; HGNC:10941; SLC1A3.
HPA; CAB002573; -.
HPA; HPA037467; -.
HPA; HPA037468; -.
MalaCards; SLC1A3; -.
MIM; 600111; gene.
MIM; 612656; phenotype.
neXtProt; NX_P43003; -.
OpenTargets; ENSG00000079215; -.
Orphanet; 2131; Alternating hemiplegia of childhood.
Orphanet; 209967; Episodic ataxia type 6.
PharmGKB; PA35828; -.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; P43003; -.
KO; K05614; -.
OMA; TFAFSSR; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; P43003; -.
TreeFam; TF315206; -.
Reactome; R-HSA-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
Reactome; R-HSA-5619062; Defective SLC1A3 causes episodic ataxia 6 (EA6).
ChiTaRS; SLC1A3; human.
GeneWiki; Glutamate_aspartate_transporter; -.
GenomeRNAi; 6507; -.
PRO; PR:P43003; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000079215; -.
CleanEx; HS_SLC1A3; -.
ExpressionAtlas; P43003; baseline and differential.
Genevisible; P43003; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:UniProtKB.
GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031223; P:auditory behavior; IEA:Ensembl.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
GO; GO:0021545; P:cranial nerve development; IEA:Ensembl.
GO; GO:0070779; P:D-aspartate import; IDA:UniProtKB.
GO; GO:0140016; P:D-aspartate import across plasma membrane; IMP:UniProtKB.
GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
GO; GO:0006537; P:glutamate biosynthetic process; IEA:Ensembl.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0006811; P:ion transport; TAS:Reactome.
GO; GO:0140009; P:L-aspartate import across plasma membrane; IDA:UniProtKB.
GO; GO:0051938; P:L-glutamate import; IDA:UniProtKB.
GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:UniProtKB.
GO; GO:0089711; P:L-glutamate transmembrane transport; IDA:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0001504; P:neurotransmitter uptake; TAS:ProtInc.
GO; GO:0050806; P:positive regulation of synaptic transmission; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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;
3D-structure; Alternative splicing; Amino-acid transport;
Cell membrane; Chloride; Complete proteome; Disease mutation;
Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Potassium; Reference proteome; Sodium; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 542 Excitatory amino acid transporter 1.
/FTId=PRO_0000202057.
TOPO_DOM 1 47 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 48 68 Helical; Name=1.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 69 86 Extracellular.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 87 108 Helical; Name=2.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 109 122 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 123 145 Helical; Name=3.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 146 236 Extracellular.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 237 260 Helical; Name=4.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 261 269 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 270 297 Helical; Name=5.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 298 318 Extracellular.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 319 340 Helical; Name=6.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 341 345 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
INTRAMEM 346 376 Discontinuously helical.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 377 385 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 386 412 Helical; Name=7.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 413 425 Extracellular.
{ECO:0000305|PubMed:28424515}.
INTRAMEM 426 459 Discontinuously helical.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 460 472 Extracellular.
{ECO:0000305|PubMed:28424515}.
TRANSMEM 473 494 Helical; Name=8.
{ECO:0000305|PubMed:28424515}.
TOPO_DOM 495 542 Cytoplasmic.
{ECO:0000305|PubMed:28424515}.
REGION 363 365 Aspartate binding. {ECO:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
REGION 443 447 Aspartate binding. {ECO:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
METAL 394 394 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 396 396 Sodium 2; via carbonyl oxygen.
{ECO:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
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:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
BINDING 476 476 Aspartate. {ECO:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
BINDING 483 483 Aspartate. {ECO:0000244|PDB:5LM4,
ECO:0000269|PubMed:28424515}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 430 475 SITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIA
VDWFL -> R (in isoform 2).
{ECO:0000303|PubMed:16042756}.
/FTId=VSP_043913.
VARIANT 219 219 E -> D (in dbSNP:rs2032892).
/FTId=VAR_011877.
VARIANT 290 290 P -> R (in EA6; dbSNP:rs137852619).
{ECO:0000269|PubMed:16116111}.
/FTId=VAR_031733.
MUTAGEN 363 363 S->R: Loss of electrogenic glutamate
transport. Strongly decreased L-aspartate
and L-glutamate uptake combined with
strongly increased permeability ot other
ions; when associated with M-477.
{ECO:0000269|PubMed:20477940}.
MUTAGEN 477 477 R->M: Strongly decreased L-aspartate and
L-glutamate uptake combined with strongly
increased permeability ot other ions;
when associated with R-363.
{ECO:0000269|PubMed:20477940}.
MUTAGEN 523 523 Y->F: No effect on activity.
{ECO:0000269|PubMed:28032905}.
CONFLICT 366 366 S -> CT (in Ref. 1). {ECO:0000305}.
HELIX 41 45 {ECO:0000244|PDB:5LM4}.
HELIX 76 81 {ECO:0000244|PDB:5LM4}.
HELIX 83 95 {ECO:0000244|PDB:5LM4}.
HELIX 102 104 {ECO:0000244|PDB:5LM4}.
HELIX 106 109 {ECO:0000244|PDB:5LM4}.
HELIX 114 117 {ECO:0000244|PDB:5LM4}.
HELIX 121 136 {ECO:0000244|PDB:5LM4}.
HELIX 262 265 {ECO:0000244|PDB:5LM4}.
HELIX 274 277 {ECO:0000244|PDB:5LM4}.
HELIX 283 300 {ECO:0000244|PDB:5LM4}.
HELIX 316 328 {ECO:0000244|PDB:5LM4}.
HELIX 332 335 {ECO:0000244|PDB:5LM4}.
HELIX 347 351 {ECO:0000244|PDB:5LM4}.
HELIX 353 362 {ECO:0000244|PDB:5LM4}.
TURN 365 367 {ECO:0000244|PDB:5LM4}.
HELIX 369 377 {ECO:0000244|PDB:5LM4}.
TURN 378 380 {ECO:0000244|PDB:5LM4}.
HELIX 387 396 {ECO:0000244|PDB:5LM4}.
HELIX 400 407 {ECO:0000244|PDB:5LM4}.
HELIX 411 414 {ECO:0000244|PDB:5LM4}.
HELIX 424 439 {ECO:0000244|PDB:5LM4}.
HELIX 446 449 {ECO:0000244|PDB:5LM4}.
HELIX 451 456 {ECO:0000244|PDB:5LM4}.
HELIX 462 464 {ECO:0000244|PDB:5LM4}.
HELIX 465 473 {ECO:0000244|PDB:5LM4}.
HELIX 475 487 {ECO:0000244|PDB:5LM4}.
HELIX 493 497 {ECO:0000244|PDB:5LM4}.
HELIX 499 504 {ECO:0000244|PDB:5LM4}.
SEQUENCE 542 AA; 59572 MW; 6E9F62D35A3A5A29 CRC64;
MTKSNGEEPK MGGRMERFQQ GVRKRTLLAK KKVQNITKED VKSYLFRNAF VLLTVTAVIV
GTILGFTLRP YRMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG
MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMHREGK IVRVTAADAF LDLIRNMFPP
NLVEACFKQF KTNYEKRSFK VPIQANETLV GAVINNVSEA METLTRITEE LVPVPGSVNG
VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP VGILFLIAGK
IVEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL
GTSSSSATLP ITFKCLEENN GVDKRVTRFV LPVGATINMD GTALYEALAA IFIAQVNNFE
LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT
TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLIAQDN ETEKPIDSET
KM


Related products :

Catalog number Product name Quantity
EIAAB12295 Eaat1,Excitatory amino acid transporter 1,GLAST-1,Glial glutamate transporter,Rat,Rattus norvegicus,Slc1a3,Sodium-dependent glutamate_aspartate transporter 1,Solute carrier family 1 member 3
EIAAB12296 Bos taurus,Bovine,EAAT1,Excitatory amino acid transporter 1,GLAST,GLAST1,GLAST-1,SLC1A3,Sodium-dependent glutamate_aspartate transporter 1,Solute carrier family 1 member 3
EIAAB12293 EAAT1,Excitatory amino acid transporter 1,GLAST,GLAST1,GLAST-1,Homo sapiens,Human,SLC1A3,Sodium-dependent glutamate_aspartate transporter 1,Solute carrier family 1 member 3
EIAAB12307 Eaat4,Excitatory amino acid transporter 4,High-affinity neuronal glutamate transporter,Mouse,Mus musculus,Slc1a6,Sodium-dependent glutamate_aspartate transporter,Solute carrier family 1 member 6
EIAAB12308 Eaat4,Excitatory amino acid transporter 4,High-affinity neuronal glutamate transporter,Rat,Rattus norvegicus,Slc1a6,Sodium-dependent glutamate_aspartate transporter,Solute carrier family 1 member 6
EIAAB12301 Eaac1,Eaat3,Excitatory amino acid transporter 3,Excitatory amino-acid carrier 1,Rat,Rattus norvegicus,Slc1a1,Sodium-dependent glutamate_aspartate transporter 3,Solute carrier family 1 member 1
EIAAB12300 Eaac1,Eaat3,Excitatory amino acid transporter 3,Excitatory amino-acid carrier 1,Mouse,Mus musculus,Slc1a1,Sodium-dependent glutamate_aspartate transporter 3,Solute carrier family 1 member 1
EIAAB12302 EAAC1,EAAT3,Excitatory amino acid transporter 3,Excitatory amino-acid carrier 1,Oryctolagus cuniculus,Rabbit,SLC1A1,Sodium-dependent glutamate_aspartate transporter 3,Solute carrier family 1 member 1
EIAAB12305 EAAT4,Excitatory amino acid transporter 4,Homo sapiens,Human,SLC1A6,Sodium-dependent glutamate_aspartate transporter,Solute carrier family 1 member 6
EIAAB12298 Eaat2,Excitatory amino acid transporter 2,Glt1,GLT-1,Mouse,Mus musculus,Slc1a2,Sodium-dependent glutamate_aspartate transporter 2,Solute carrier family 1 member 2
EIAAB12297 EAAT2,Excitatory amino acid transporter 2,GLT1,Glutamate_aspartate transporter II,Homo sapiens,Human,SLC1A2,Sodium-dependent glutamate_aspartate transporter 2,Solute carrier family 1 member 2
EIAAB12299 Eaat2,Excitatory amino acid transporter 2,Glt1,GLT-1,GLUT-R,Rat,Rattus norvegicus,Slc1a2,Sodium-dependent glutamate_aspartate transporter 2,Solute carrier family 1 member 2
EIAAB12304 EAAC1,EAAT3,Excitatory amino acid transporter 3,Excitatory amino-acid carrier 1,Homo sapiens,Human,Neuronal and epithelial glutamate transporter,SLC1A1,Sodium-dependent glutamate_aspartate transporter
EIAAB12309 EAAT5,Excitatory amino acid transporter 5,Homo sapiens,Human,Retinal glutamate transporter,SLC1A7,Solute carrier family 1 member 7
EIAAB12294 Eaat1,Excitatory amino acid transporter 1,GLAST-1,Glial high affinity glutamate transporter,Gmt1,High-affinity neuronal glutamate transporter,Mouse,Mus musculus,Slc1a3,Sodium-dependent glutamate_aspar
EIAAB12306 Canis familiaris,Canis lupus familiaris,Dog,EAAT4,Excitatory amino acid transporter 4,SLC1A6,Sodium-dependent glutamate_aspartate transporter,Solute carrier family 1 member 6
EIAAB12303 Bos taurus,Bovine,EAAC1,EAAT3,Excitatory amino acid transporter 3,Excitatory amino-acid carrier 1,Renal high affinity glutamate transporter EAAC1,SLC1A1,Sodium-dependent glutamate_aspartate transporte
EIAAB37146 Homo sapiens,Human,SLC6A18,Sodium- and chloride-dependent transporter XTRP2,Sodium-dependent neutral amino acid transporter B(0)AT3,Solute carrier family 6 member 18,System B(0) neutral amino acid tra
EIAAB37148 Mouse,Mus musculus,Slc6a18,Sodium- and chloride-dependent transporter XTRP2,Sodium-dependent neutral amino acid transporter B(0)AT3,Solute carrier family 6 member 18,System B(0) neutral amino acid tra
EIAAB37136 Amino acid transporter ATB0+,Homo sapiens,Human,SLC6A14,Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+),Solute carrier family 6 member 14
EIAAB37138 Ntt73,Rat,Rattus norvegicus,Slc6a15,sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Transpor
EIAAB37140 B0AT2,Bos taurus,Bovine,NTT73,SLC6A15,Sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Transp
EIAAB37137 B0at2,Mouse,Mus musculus,Ntt73,Slc6a15,Sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Trans
EIAAB37150 B0at1,Rat,Rattus norvegicus,Slc6a19,Sodium-dependent neutral amino acid transporter B(0)AT1,Solute carrier family 6 member 19,System B(0) neutral amino acid transporter AT1
EIAAB37151 B0at1,Mouse,Mus musculus,Slc6a19,Sodium-dependent neutral amino acid transporter B(0)AT1,Solute carrier family 6 member 19,System B(0) neutral amino acid transporter AT1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur