EAA1_BOVIN
ID EAA1_BOVIN Reviewed; 542 AA.
AC P46411; Q0VCK3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Excitatory amino acid transporter 1;
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 1;
DE Short=GLAST-1;
DE AltName: Full=Solute carrier family 1 member 3;
GN Name=SLC1A3; Synonyms=EAAT1, GLAST {ECO:0000303|PubMed:7723632}, GLAST1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=7723632; DOI=10.1016/0169-328x(94)00244-9;
RA Inoue K., Sakaitani M., Shimada S., Tohyama M.;
RT "Cloning and expression of a bovine glutamate transporter.";
RL Brain Res. Mol. Brain Res. 28:343-348(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:7723632). Functions as a symporter that transports one amino
CC acid molecule together with two or three Na(+) ions and one proton, in
CC parallel with the counter-transport of one K(+) ion (By similarity).
CC Plays a redundant role in the rapid removal of released glutamate from
CC the synaptic cleft, which is essential for terminating the postsynaptic
CC action of glutamate (By similarity). {ECO:0000250|UniProtKB:O57321,
CC ECO:0000250|UniProtKB:P56564, ECO:0000269|PubMed:7723632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-
CC aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29990;
CC Evidence={ECO:0000250|UniProtKB:P43003};
CC -!- SUBUNIT: Homotrimer (By similarity). {ECO:0000250|UniProtKB:P43003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7723632};
CC Multi-pass membrane protein.
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:P24942}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A3 subfamily. {ECO:0000305}.
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DR EMBL; D82056; BAA11527.1; -; mRNA.
DR EMBL; BC120125; AAI20126.1; -; mRNA.
DR RefSeq; NP_777025.1; NM_174600.2.
DR AlphaFoldDB; P46411; -.
DR SMR; P46411; -.
DR STRING; 9913.ENSBTAP00000024287; -.
DR PaxDb; P46411; -.
DR PRIDE; P46411; -.
DR Ensembl; ENSBTAT00000024287; ENSBTAP00000024287; ENSBTAG00000018245.
DR GeneID; 282354; -.
DR KEGG; bta:282354; -.
DR CTD; 6507; -.
DR VEuPathDB; HostDB:ENSBTAG00000018245; -.
DR VGNC; VGNC:34713; SLC1A3.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155464; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P46411; -.
DR OMA; GHGMNVD; -.
DR OrthoDB; 1184392at2759; -.
DR TreeFam; TF315206; -.
DR Reactome; R-BTA-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-BTA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-BTA-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000018245; Expressed in occipital lobe and 93 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; ISS:UniProtKB.
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:0031223; P:auditory behavior; IEA:Ensembl.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
DR GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0021545; P:cranial nerve development; IEA:Ensembl.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IGI:ARUK-UCL.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IDA:MGI.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IDA:MGI.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0070633; P:transepithelial transport; IGI:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; IGI:ARUK-UCL.
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 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Chloride; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Potassium; Reference proteome; Sodium;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="Excitatory amino acid transporter 1"
FT /id="PRO_0000202056"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 69..86
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 87..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 109..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 123..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 146..236
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 237..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 261..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 270..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 298..318
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 319..340
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 341..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 346..376
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 377..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 386..412
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 413..425
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT INTRAMEM 426..459
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 460..472
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TRANSMEM 473..494
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 495..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 363..365
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 394
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 396
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 398
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 402
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 443..447
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 476
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 483
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 483
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 487
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43003"
SQ SEQUENCE 542 AA; 59591 MW; F23810DB5DC016D2 CRC64;
MTKSNGEEAR LGGRMERFQQ GVRKRTLLAK KKVQNITKED VKSYLFRNAF VLLTVTAVIV
GTILGFTLRP YRMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG
MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMHREGK IVQVTAADAF LDLIRNMFPP
NLVEACFKQF KTNYEKRSFK VPIQPNETLV GAVINNVSEA METLTRITEE LVPVPGSVNG
VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP LGILFLIAGK
IVEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL
GTSSSSATLP ITFKCLEENN GVDKRVTRFV LPVGATINMD GTALYEALAA IFIAQVNNFE
LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT
TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLISQES EIEKSMDSET
KM
