EAA3_RAT
ID EAA3_RAT Reviewed; 523 AA.
AC P51907; O88389; Q63727; Q9JJP8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Excitatory amino acid transporter 3;
DE AltName: Full=Excitatory amino-acid carrier 1 {ECO:0000303|PubMed:8772431, ECO:0000303|PubMed:9011753};
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 3;
DE AltName: Full=Solute carrier family 1 member 1;
GN Name=Slc1a1;
GN Synonyms=Eaac1 {ECO:0000303|PubMed:8772431, ECO:0000303|PubMed:9011753},
GN Eaat3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=9011753; DOI=10.1016/0169-328x(95)00279-2;
RA Bjoras M., Gjesdal O., Erickson J.D., Torp R., Levy L.M., Ottersen O.P.,
RA Degree M., Storm-Mathisen J., Seeberg E., Danbolt N.C.;
RT "Cloning and expression of a neuronal rat brain glutamate transporter.";
RL Brain Res. Mol. Brain Res. 36:163-168(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8747153; DOI=10.1097/00001756-199511270-00020;
RA Kanai Y., Bhide P.G., Difiglia M., Hediger M.A.;
RT "Neuronal high-affinity glutamate transport in the rat central nervous
RT system.";
RL NeuroReport 6:2357-2362(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8613726; DOI=10.1523/jneurosci.15-12-07872.1995;
RA Kiryu S., Yao G.L., Morita N., Kato H., Kiyama H.;
RT "Nerve injury enhances rat neuronal glutamate transporter expression:
RT identification by differential display PCR.";
RL J. Neurosci. 15:7872-7878(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=8772431; DOI=10.1152/ajpcell.1996.270.1.c67;
RA Velaz-Faircloth M., McGraw T.S., Malandro M.S., Fremeau R.T. Jr.,
RA Kilberg M.S., Anderson K.J.;
RT "Characterization and distribution of the neuronal glutamate transporter
RT EAAC1 in rat brain.";
RL Am. J. Physiol. 270:C67-C75(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-368.
RX PubMed=8738164; DOI=10.1016/0169-328x(95)00331-l;
RA Palos T.P., Ramachandran B., Boado R., Howard B.D.;
RT "Rat C6 and human astrocytic tumor cells express a neuronal type of
RT glutamate transporter.";
RL Brain Res. Mol. Brain Res. 37:297-303(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-445.
RC TISSUE=Intestine;
RA Rome S., Mertani H.C., Lee K.O., Tome D.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND INTERACTION WITH ARL6IP5.
RX PubMed=11242046; DOI=10.1038/35065084;
RA Lin C.-L.G., Orlov I., Ruggiero A.M., Dykes-Hoberg M., Lee A., Jackson M.,
RA Rothstein J.D.;
RT "Modulation of the neuronal glutamate transporter EAAC1 by the interacting
RT protein GTRAP3-18.";
RL Nature 410:84-88(2001).
RN [9]
RP INTERACTION WITH RTN2, AND SUBCELLULAR LOCATION.
RX PubMed=19720795; DOI=10.2337/db09-0756;
RA Ikemoto T., Hosoya T., Takata K., Aoyama H., Hiramatsu T., Onoe H.,
RA Suzuki M., Endo M.;
RT "Functional role of neuroendocrine-specific protein-like 1 in membrane
RT translocation of GLUT4.";
RL Diabetes 58:2802-2812(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:9011753, PubMed:11242046). Can also transport L-cysteine.
CC Functions as a symporter that transports one amino acid molecule
CC together with two or three Na(+) ions and one proton, in parallel with
CC the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not
CC coupled to amino acid transport; this avoids the accumulation of
CC negative charges due to aspartate and Na(+) symport. Plays an important
CC role in L-glutamate and L-aspartate reabsorption in renal tubuli (By
CC similarity). Plays a redundant role in the rapid removal of released
CC glutamate from the synaptic cleft, which is essential for terminating
CC the postsynaptic action of glutamate (By similarity). Contributes to
CC glutathione biosynthesis and protection against oxidative stress via
CC its role in L-glutamate and L-cysteine transport (By similarity).
CC Negatively regulated by ARL6IP5 (PubMed:11242046).
CC {ECO:0000250|UniProtKB:P43005, ECO:0000250|UniProtKB:P51906,
CC ECO:0000269|PubMed:11242046}.
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/PRAF3
CC (PubMed:11242046). Interacts with RTN2 (via N-terminus); the
CC interaction promotes cell surface expression of SLC1A1
CC (PubMed:19720795). Interacts with SORCS2; this interaction is important
CC for normal expression at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P51906, ECO:0000269|PubMed:11242046,
CC ECO:0000269|PubMed:19720795, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11242046,
CC ECO:0000269|PubMed:19720795, ECO:0000269|PubMed:9011753}; Multi-pass
CC membrane protein {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:0000250|UniProtKB:P51906}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P51906}. Late endosome membrane
CC {ECO:0000250|UniProtKB:P51906}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P51906}.
CC -!- TISSUE SPECIFICITY: Expressed to a high extent in brain and kidney, and
CC to a lower extent in heart, lung and skeletal muscle.
CC {ECO:0000269|PubMed:8772431, ECO:0000269|PubMed:9011753}.
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. SLC1A1 subfamily. {ECO:0000305}.
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DR EMBL; X94255; CAA63937.1; -; mRNA.
DR EMBL; U39555; AAB09773.1; -; mRNA.
DR EMBL; D63772; BAA09849.1; -; mRNA.
DR EMBL; L35558; AAB51161.1; -; mRNA.
DR EMBL; BC061743; AAH61743.1; -; mRNA.
DR EMBL; U21104; AAF34319.1; -; mRNA.
DR EMBL; AF038571; AAC25030.1; -; mRNA.
DR RefSeq; NP_037164.3; NM_013032.3.
DR AlphaFoldDB; P51907; -.
DR SMR; P51907; -.
DR BioGRID; 247581; 3.
DR MINT; P51907; -.
DR STRING; 10116.ENSRNOP00000020272; -.
DR BindingDB; P51907; -.
DR ChEMBL; CHEMBL3113; -.
DR GuidetoPHARMACOLOGY; 870; -.
DR GlyGen; P51907; 3 sites.
DR iPTMnet; P51907; -.
DR PhosphoSitePlus; P51907; -.
DR SwissPalm; P51907; -.
DR PaxDb; P51907; -.
DR PRIDE; P51907; -.
DR ABCD; P51907; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000020272; ENSRNOP00000020272; ENSRNOG00000014816.
DR GeneID; 25550; -.
DR KEGG; rno:25550; -.
DR UCSC; RGD:3696; rat.
DR CTD; 6505; -.
DR RGD; 3696; Slc1a1.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155397; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P51907; -.
DR OMA; YFCTTII; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; P51907; -.
DR TreeFam; TF315206; -.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR PRO; PR:P51907; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014816; Expressed in kidney and 15 other tissues.
DR Genevisible; P51907; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:ARUK-UCL.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0032279; C:asymmetric synapse; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; IDA:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
DR GO; GO:0150002; C:distal dendrite; IDA:ARUK-UCL.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; IDA:ARUK-UCL.
DR GO; GO:0099544; C:perisynaptic space; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:ARUK-UCL.
DR GO; GO:1990635; C:proximal dendrite; IDA:ARUK-UCL.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043083; C:synaptic cleft; IDA:ARUK-UCL.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0005253; F:anion channel activity; ISO:RGD.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0033229; F:cysteine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0140010; F:D-aspartate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:RGD.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:RGD.
DR GO; GO:1903926; P:cellular response to bisphenol A; ISO:RGD.
DR GO; GO:0071314; P:cellular response to cocaine; ISO:RGD.
DR GO; GO:0071288; P:cellular response to mercury ion; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:1990708; P:conditioned place preference; ISO:RGD.
DR GO; GO:1903712; P:cysteine transmembrane transport; ISO:RGD.
DR GO; GO:0042883; P:cysteine transport; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:RGD.
DR GO; GO:0070777; P:D-aspartate transport; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0090461; P:glutamate homeostasis; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0006750; P:glutathione biosynthetic process; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; ISO:RGD.
DR GO; GO:0051938; P:L-glutamate import; ISO:RGD.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:RGD.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0061744; P:motor behavior; ISO:RGD.
DR GO; GO:0097049; P:motor neuron apoptotic process; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0070997; P:neuron death; ISO:RGD.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; ISO:RGD.
DR GO; GO:0098877; P:neurotransmitter receptor transport to plasma membrane; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0090313; P:regulation of protein targeting to membrane; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0072347; P:response to anesthetic; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; ISO:RGD.
DR GO; GO:0036293; P:response to decreased oxygen levels; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0010842; P:retina layer formation; ISO:RGD.
DR GO; GO:0060013; P:righting reflex; ISO:RGD.
DR GO; GO:0006801; P:superoxide metabolic process; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0071577; P:zinc ion transmembrane transport; ISO:RGD.
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_0000202067"
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:0000250|UniProtKB:P51906"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51906"
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 68
FT /note="L -> M (in Ref. 3; BAA09849)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="R -> C (in Ref. 3; BAA09849)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..151
FT /note="MFP -> ILG (in Ref. 2; AAB09773)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Q -> E (in Ref. 6; AAB51161)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="G -> C (in Ref. 6; AAB51161)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="C -> F (in Ref. 6; AAB51161)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="R -> C (in Ref. 7; AAC25030)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="R -> T (in Ref. 6; AAB51161)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> V (in Ref. 3; BAA09849)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="A -> P (in Ref. 4; AAF34319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 56772 MW; D6783244E37640E4 CRC64;
MGKPTSSGCD WRRFLRNHWL LLSTVAAVVL GIVVGVLVRG HSELSNLDKF YFAFPGEILM
RMLKLVILPL IISSMITGVA ALDSNVSGKI GLRAVVYYFS TTVIAVILGI VLVVSIKPGV
TQKVNEINRT GKTPEVSTVD AMLDLIRNMF PENLVQACFQ QYKTKREEVK PASDPGGNQT
EVSVTTAMTT MSENKTKEYK IVGLYSDGIN VLGLIIFCLV FGLVIGKMGE KGQILVDFFN
ALSDATMKIV QIIMCYMPIG ILFLIAGKII EVEDWEIFRK LGLYMATVLS GLAIHSLVVL
PLIYFIVVRK NPFRFALGMA QALLTALMIS SSSATLPVTF RCAEEKNHVD KRITRFVLPV
GATINMDGTA LYEAVAAVFI AQLNGMDLSI GQIITISITA TAASIGAAGV PQAGLVTMVI
VLSAVGLPAE DVTLIIAVDW LLDRFRTMVN VLGDAFGTGI VEKLSKKELE QVDVSSEVNI
VNPFALEPTI LDNEDSDTKK SYVNGGFSVD KSDTISFTQT SQF
