EAA1_CAEEL
ID EAA1_CAEEL Reviewed; 503 AA.
AC Q10901; P90798; Q17920;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Excitatory amino acid transporter;
DE AltName: Full=Sodium-dependent glutamate/ aspartate transporter;
GN Name=glt-1; ORFNames=C12D12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Bristol N2;
RX PubMed=8885221; DOI=10.1016/0166-6851(96)02667-9;
RA Radice A.D., Lustigman S.;
RT "Cloning and characterization of cDNAs encoding putative glutamate
RT transporters from Caenorhabditis elegans and Onchocerca volvulus.";
RL Mol. Biochem. Parasitol. 80:41-53(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8920929; DOI=10.1006/bbrc.1996.1676;
RA Kawano T., Takuwa K., Nakajima T.;
RT "Molecular cloning of a cDNA for the glutamate transporter of the nematode
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 228:415-420(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=9178573; DOI=10.1271/bbb.61.927;
RA Kawano T., Takuwa K., Nakajima T.;
RT "Structure and activity of a new form of the glutamate transporter of the
RT nematode Caenorhabditis elegans.";
RL Biosci. Biotechnol. Biochem. 61:927-929(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177 AND ASN-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
CC -!- FUNCTION: Transports L-glutamate and also L- and D-aspartate. Essential
CC for terminating the postsynaptic action of glutamate by rapidly
CC removing released glutamate from the synaptic cleft. Acts as a symport
CC by cotransporting sodium (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=Glt-2;
CC IsoId=Q10901-1; Sequence=Displayed;
CC Name=b; Synonyms=Glt-1;
CC IsoId=Q10901-2; Sequence=VSP_006267;
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; U35250; AAB41909.1; -; mRNA.
DR EMBL; U35250; AAB41910.1; -; mRNA.
DR EMBL; D86740; BAA13164.1; -; mRNA.
DR EMBL; D86741; BAA21840.1; -; mRNA.
DR EMBL; FO080514; CCD64307.1; -; Genomic_DNA.
DR EMBL; FO080514; CCD64308.1; -; Genomic_DNA.
DR PIR; JC5078; JC5078.
DR RefSeq; NP_001024393.1; NM_001029222.3. [Q10901-1]
DR RefSeq; NP_001024394.1; NM_001029223.2. [Q10901-2]
DR AlphaFoldDB; Q10901; -.
DR SMR; Q10901; -.
DR BioGRID; 45579; 7.
DR STRING; 6239.C12D12.2a; -.
DR TCDB; 2.A.23.2.10; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR iPTMnet; Q10901; -.
DR EPD; Q10901; -.
DR PaxDb; Q10901; -.
DR PeptideAtlas; Q10901; -.
DR EnsemblMetazoa; C12D12.2a.1; C12D12.2a.1; WBGene00001620. [Q10901-1]
DR EnsemblMetazoa; C12D12.2b.1; C12D12.2b.1; WBGene00001620. [Q10901-2]
DR GeneID; 180641; -.
DR KEGG; cel:CELE_C12D12.2; -.
DR UCSC; C12D12.2b.3; c. elegans. [Q10901-1]
DR CTD; 180641; -.
DR WormBase; C12D12.2a; CE29083; WBGene00001620; glt-1. [Q10901-1]
DR WormBase; C12D12.2b; CE29084; WBGene00001620; glt-1. [Q10901-2]
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000167643; -.
DR HOGENOM; CLU_019375_3_0_1; -.
DR InParanoid; Q10901; -.
DR OMA; YLMRFAP; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; Q10901; -.
DR Reactome; R-CEL-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR PRO; PR:Q10901; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001620; Expressed in larva and 4 other tissues.
DR GO; GO:0042995; C:cell projection; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central.
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; Glycoprotein; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..503
FT /note="Excitatory amino acid transporter"
FT /id="PRO_0000202074"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:8885221"
FT /id="VSP_006267"
FT CONFLICT 68
FT /note="L -> P (in Ref. 1; AAB41909/AAB41910)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..273
FT /note="ADTA -> ENTT (in Ref. 1; AAB41909/AAB41910)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> G (in Ref. 1; AAB41909/AAB41910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 54676 MW; 3014BFF28E41E798 CRC64;
MPPDTRINKE IMVSWIRKNL LLVLTVSSVV LGALCGFLLR GLQLSPQNIM YISFPGELLM
HMLKMMILPL IMSSLISGLA QLDARQSGKL GSLAVTYYMF TTAVAVVTGI FLVLVIHPGD
PTIKKEIGTG TEGKTVSTVD TLLDLLRNMF PENVVQATFQ QVQTKYIKVR PKVVKNNDSA
TLAALNNGSL DYVKASVEYT SGMNVLGVIV FCIAIGISLS QLGQEAHVMV QFFVIMDKVI
MKLVMTVMWY SPFGIFCLIM GKILEIHDLA DTARMLAMYM VTVLSGLAIH SLISLPLIFF
VTTKKNPYVF MRGLFQAWIT ALGTASSSAT LPITFNCLEE NLGVDRRVTR FVLPVGATIN
MDGTALYEAV AAIFIAQING VHLSFGQVVT VSLTATLASI GAASVPSAGL VTMLLVLTAV
GLPVKDVSLI VAVDWLLDRI RTSINVLGDA MGAGIVYHYS KADLDAHDRL AATTRSHSIA
MNDEKRQLAV YNSLPTDDEK HTH
