EAA4_CAEEL
ID EAA4_CAEEL Reviewed; 499 AA.
AC Q22682;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative sodium-dependent excitatory amino acid transporter glt-4;
GN Name=glt-4; ORFNames=T22E5.2;
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 [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).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates the uptake of L-glutamate and also L-aspartate and D-
CC aspartate. Functions as a symporter that transports one amino acid
CC molecule together with two or three Na(+) ions and one proton, in
CC parallel with the counter-transport of one K(+) ion. Mediates Cl(-)
CC flux that is not coupled to amino acid transport; this avoids the
CC accumulation of negative charges due to aspartate and Na(+) symport.
CC {ECO:0000250|UniProtKB:O35921}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35921};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O35921}.
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 -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; FO081616; CCD72844.1; -; Genomic_DNA.
DR PIR; T16921; T16921.
DR RefSeq; NP_509075.3; NM_076674.5.
DR AlphaFoldDB; Q22682; -.
DR SMR; Q22682; -.
DR STRING; 6239.T22E5.2; -.
DR EPD; Q22682; -.
DR PaxDb; Q22682; -.
DR PeptideAtlas; Q22682; -.
DR EnsemblMetazoa; T22E5.2.1; T22E5.2.1; WBGene00001622.
DR GeneID; 188744; -.
DR KEGG; cel:CELE_T22E5.2; -.
DR UCSC; T22E5.2; c. elegans.
DR CTD; 188744; -.
DR WormBase; T22E5.2; CE38553; WBGene00001622; glt-4.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000167953; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; Q22682; -.
DR OMA; ATFRSHK; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; Q22682; -.
DR Reactome; R-CEL-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-CEL-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR PRO; PR:Q22682; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001622; Expressed in larva and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IBA:GO_Central.
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: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 3: Inferred from homology;
KW Amino-acid transport; Cell membrane; Chloride; Glycoprotein; Membrane;
KW Metal-binding; Potassium; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..499
FT /note="Putative sodium-dependent excitatory amino acid
FT transporter glt-4"
FT /id="PRO_0000202076"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..217
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 227..254
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 276..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 303..333
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 343..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 383..416
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 430..451
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 320..322
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 351
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 353
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 355
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 359
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 400..404
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 433
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 440
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 440
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 444
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 53935 MW; 80DE9293852FB499 CRC64;
MAKLSKENLL LLFTVLGVVV GIGLGFSLRD PSKAWSKRHL SYLRFPGDLF VQMLKMLILP
MIMSSIITSL ASLDSGTAGR LGMVSMIYYT LTTFFAVFLG IVLVSVIKPG KWTTTNIEDL
VGHVKTTPCV ATAVDTIIDL MKSCFPENLI EATFRSQKIC LKFFNGTTEI PPEIAMTMSP
EQRAQFTEVP EKIVSDGMNI LGLVVFSVAL GIVIGVIGED GKPMKNFFKS LEACSMKLIG
WVIIYSPVGI TFLIAAQIVG MKDPGQELHR LMGYVITVIL GLLIHAFVVI PLLCVVLARR
NPIKFVGGMA QALLTALATS SSSATLPLSI KCCEENNKVD PRVTRFVLPL GATINMDGTA
LYEAVAAIYI SQCYGNDLSL GEVVLVSLTA TLASIGAAGI PQAGIVTMIM VLIAIGLPTN
LFILIFPVDF MLDRLRTTVN VHGDSIATAV IERLCEDQLQ KGGHHLDTND QGYSMLSTNA
SPDPKRITIG NNCENSHML
