EAA3_MOUSE
ID EAA3_MOUSE Reviewed; 523 AA.
AC P51906; O35869; O35875; Q6P1F7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Excitatory amino acid transporter 3;
DE AltName: Full=Excitatory amino-acid carrier 1 {ECO:0000303|PubMed:9233792};
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 3;
DE AltName: Full=Solute carrier family 1 member 1;
GN Name=Slc1a1; Synonyms=Eaac1 {ECO:0000303|PubMed:9233792}, Eaat3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=JCL:ICR; TISSUE=Cerebellum;
RX PubMed=7766664; DOI=10.1016/0304-4165(95)00062-g;
RA Mukainaka Y., Tanaka K., Hagiwara T., Wada K.;
RT "Molecular cloning of two glutamate transporter subtypes from mouse
RT brain.";
RL Biochim. Biophys. Acta 1244:233-237(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain;
RA Peng J.-B., Guo L.-H.;
RT "Molecular cloning of a mouse glutamate transporter.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9233792; DOI=10.1093/emboj/16.13.3822;
RA Peghini P., Janzen J., Stoffel W.;
RT "Glutamate transporter EAAC-1-deficient mice develop dicarboxylic
RT aminoaciduria and behavioral abnormalities but no neurodegeneration.";
RL EMBO J. 16:3822-3832(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARL6IP5.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12119102; DOI=10.1016/s0378-1119(02)00669-8;
RA Butchbach M.E.R., Lai L., Lin C.-L.G.;
RT "Molecular cloning, gene structure, expression profile and functional
RT characterization of the mouse glutamate transporter (EAAT3) interacting
RT protein GTRAP3-18.";
RL Gene 292:81-90(2002).
RN [7]
RP INTERACTION WITH ARL6IP5, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18684713; DOI=10.1074/jbc.m801570200;
RA Akiduki S., Ikemoto M.J.;
RT "Modulation of the neural glutamate transporter EAAC1 by the addicsin-
RT interacting protein ARL6IP1.";
RL J. Biol. Chem. 283:31323-31332(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, INTERACTION WITH SORCS2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=30840898; DOI=10.1016/j.celrep.2019.02.027;
RA Malik A.R., Szydlowska K., Nizinska K., Asaro A., van Vliet E.A., Popp O.,
RA Dittmar G., Fritsche-Guenther R., Kirwan J.A., Nykjaer A., Lukasiuk K.,
RA Aronica E., Willnow T.E.;
RT "SorCS2 Controls Functional Expression of Amino Acid Transporter EAAT3 and
RT Protects Neurons from Oxidative Stress and Epilepsy-Induced Pathology.";
RL Cell Rep. 26:2792-2804(2019).
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:12119102, PubMed:18684713). Can also transport L-cysteine
CC (PubMed:30840898). 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. 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 (By
CC similarity). Plays an important role in L-glutamate and L-aspartate
CC reabsorption in renal tubuli (PubMed:9233792). Plays a redundant role
CC in the rapid removal of released glutamate from the synaptic cleft,
CC which is essential for terminating the postsynaptic action of glutamate
CC (PubMed:9233792). Contributes to glutathione biosynthesis and
CC protection against oxidative stress via its role in L-glutamate and L-
CC cysteine transport (PubMed:30840898). Negatively regulated by ARL6IP5
CC (PubMed:12119102). {ECO:0000250|UniProtKB:P43005,
CC ECO:0000269|PubMed:12119102, ECO:0000269|PubMed:18684713,
CC ECO:0000269|PubMed:30840898, ECO:0000269|PubMed:9233792}.
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:P43005};
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:P43005};
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:P43005};
CC -!- SUBUNIT: Homotrimer (Probable). Interacts with ARL6IP5
CC (PubMed:12119102, PubMed:18684713). Interacts with RTN2 (via N-
CC terminus); the interaction promotes cell surface expression of SLC1A1
CC (By similarity). Interacts with SORCS2; this interaction is important
CC for normal expression at the cell membrane (PubMed:30840898).
CC {ECO:0000250|UniProtKB:P51907, ECO:0000269|PubMed:12119102,
CC ECO:0000269|PubMed:18684713, ECO:0000269|PubMed:30840898, ECO:0000305}.
CC -!- INTERACTION:
CC P51906; P53702: Hccs; NbExp=5; IntAct=EBI-8580001, EBI-8579982;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12119102,
CC ECO:0000269|PubMed:18684713, ECO:0000269|PubMed:30840898,
CC ECO:0000269|PubMed:9233792}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P43003}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P43005}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P43003}. Synapse, synaptosome
CC {ECO:0000269|PubMed:30840898}. Early endosome membrane
CC {ECO:0000269|PubMed:30840898}. Late endosome membrane
CC {ECO:0000269|PubMed:30840898}. Recycling endosome membrane
CC {ECO:0000269|PubMed:30840898}.
CC -!- TISSUE SPECIFICITY: Detected on neurons in the brain cortex, dentate
CC gyrus and hippocampus CA2 region (at protein level) (PubMed:30840898).
CC Expressed in whole brain, brain cortex, hippocampus, cerebellum, lung,
CC kidney, small intestine and skeletal muscle.
CC {ECO:0000269|PubMed:30840898, ECO:0000269|PubMed:7766664,
CC ECO:0000269|PubMed:9233792}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype at birth. Mice are born at
CC the expected Mendelian rate, are viable and fertile, and do not develop
CC any neurological symptoms with increasing age. They show decreased
CC spontaneous locomotor activity. Besides, urinary excretion of glutamate
CC and aspartate are strongly increased, but glutamate and aspartate serum
CC levels are normal. {ECO:0000269|PubMed:9233792}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A1 subfamily. {ECO:0000305}.
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DR EMBL; D43797; BAA07855.1; -; mRNA.
DR EMBL; U73521; AAB80694.1; -; mRNA.
DR EMBL; U75217; AAB71742.1; -; Genomic_DNA.
DR EMBL; CH466534; EDL41660.1; -; Genomic_DNA.
DR EMBL; BC065099; AAH65099.1; -; mRNA.
DR CCDS; CCDS29727.1; -.
DR PIR; S55677; S55677.
DR RefSeq; NP_033225.1; NM_009199.2.
DR AlphaFoldDB; P51906; -.
DR SMR; P51906; -.
DR BioGRID; 203289; 1.
DR IntAct; P51906; 1.
DR MINT; P51906; -.
DR STRING; 10090.ENSMUSP00000025875; -.
DR GlyGen; P51906; 3 sites.
DR iPTMnet; P51906; -.
DR PhosphoSitePlus; P51906; -.
DR jPOST; P51906; -.
DR MaxQB; P51906; -.
DR PaxDb; P51906; -.
DR PeptideAtlas; P51906; -.
DR PRIDE; P51906; -.
DR ProteomicsDB; 277794; -.
DR ABCD; P51906; 1 sequenced antibody.
DR Antibodypedia; 3650; 376 antibodies from 37 providers.
DR DNASU; 20510; -.
DR Ensembl; ENSMUST00000025875; ENSMUSP00000025875; ENSMUSG00000024935.
DR GeneID; 20510; -.
DR KEGG; mmu:20510; -.
DR UCSC; uc008hcl.1; mouse.
DR CTD; 6505; -.
DR MGI; MGI:105083; Slc1a1.
DR VEuPathDB; HostDB:ENSMUSG00000024935; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155397; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P51906; -.
DR OMA; YFCTTII; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; P51906; -.
DR TreeFam; TF315206; -.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR BioGRID-ORCS; 20510; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Slc1a1; mouse.
DR PRO; PR:P51906; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P51906; protein.
DR Bgee; ENSMUSG00000024935; Expressed in pigmented layer of retina and 171 other tissues.
DR Genevisible; P51906; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0150002; C:distal dendrite; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0097386; C:glial cell projection; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0099544; C:perisynaptic space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:MGI.
DR GO; GO:0005253; F:anion channel activity; IDA:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0033229; F:cysteine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0140010; F:D-aspartate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:MGI.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0032148; P:activation of protein kinase B activity; IMP:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0071242; P:cellular response to ammonium ion; IDA:MGI.
DR GO; GO:1903926; P:cellular response to bisphenol A; IDA:MGI.
DR GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
DR GO; GO:0071288; P:cellular response to mercury ion; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:1990708; P:conditioned place preference; IMP:MGI.
DR GO; GO:1903712; P:cysteine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0042883; P:cysteine transport; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:MGI.
DR GO; GO:0070777; P:D-aspartate transport; ISO:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0090461; P:glutamate homeostasis; IMP:MGI.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IMP:MGI.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:MGI.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; ISO:MGI.
DR GO; GO:0051938; P:L-glutamate import; ISO:MGI.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:MGI.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0070997; P:neuron death; IMP:MGI.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; IMP:ARUK-UCL.
DR GO; GO:0098877; P:neurotransmitter receptor transport to plasma membrane; IMP:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; IMP:CACAO.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0090313; P:regulation of protein targeting to membrane; IMP:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0072347; P:response to anesthetic; IMP:MGI.
DR GO; GO:0048678; P:response to axon injury; IDA:MGI.
DR GO; GO:0036293; P:response to decreased oxygen levels; IMP:MGI.
DR GO; GO:0043278; P:response to morphine; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0010842; P:retina layer formation; IMP:MGI.
DR GO; GO:0060013; P:righting reflex; IMP:MGI.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IMP:MGI.
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 Amino-acid transport; Cell membrane; Chloride; Endosome; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Potassium; Reference proteome;
KW Sodium; Symport; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..523
FT /note="Excitatory amino acid transporter 3"
FT /id="PRO_0000202066"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..61
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..204
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..228
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 229..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..265
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 266..285
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 286..307
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 308..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 313..343
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 344..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..379
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 380..392
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 393..426
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 427..439
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 440..461
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 462..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 102
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 330
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 332
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 361
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 363
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 365
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 367
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 369
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 404
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 405
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 407
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 410
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 446
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 447
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 450
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 450
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT BINDING 454
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P43005"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 121
FT /note="T -> A (in Ref. 2; AAB71742)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="M -> I (in Ref. 1; BAA07855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 56694 MW; 46F35480465E5A82 CRC64;
MGKPTSSGCD WRRFLRNHWL LLSTVAAVVL GIVLGVVVRG HSELSNLDKF YFAFPGEILM
RMLKLVILPL IVSSMITGVA ALDSNVSGKI GLRAVVYYFS TTVIAVILGI VLVVSIKPGV
TQKVNDINRT GKTPEVSTMD AMLDLIRNMF PENLVQACFQ QYKTKREEVK PVGDPGGNAT
EVSVTTAMTT MSENKTKEYK IVGLYSDGIN VLGLIIFCLV FGLVIGKMGE KGQILVDFFN
ALSDATMKIV QIIMCYMPIG ILFLIAGKII EVEDWEIFRK LGLYMATVLS GLAIHSLIVL
PLLYFIVVRK NPFRFALGMA QALLTALMIS SSSATLPVTF RCAEEKNQVD KRITRFVLPV
GATINMDGTA LYEAVAAVFI AQLNGLDLSI GQIVTISITA TAASIGAAGV PQAGLVTMVI
VLSAVGLPAE DVTLIIAVDW LLDRFRTMVN VLGDAFGTGI VEKLSKKELE QMDVSSEVNI
VNPFALEPTT LDNEDSDTKK SYVNGGFAVD KSDTISFTQT SQF
