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Database: UniProt
Entry: P51907
LinkDB: P51907
Original site: P51907 
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   27-MAR-2024, entry version 165.
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   GlyCosmos; P51907; 3 sites, No reported glycans.
DR   GlyGen; P51907; 3 sites.
DR   iPTMnet; P51907; -.
DR   PhosphoSitePlus; P51907; -.
DR   SwissPalm; P51907; -.
DR   PaxDb; 10116-ENSRNOP00000020272; -.
DR   ABCD; P51907; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000020272.8; ENSRNOP00000020272.5; ENSRNOG00000014816.8.
DR   Ensembl; ENSRNOT00055053196; ENSRNOP00055043964; ENSRNOG00055030650.
DR   Ensembl; ENSRNOT00060046386; ENSRNOP00060038549; ENSRNOG00060026771.
DR   Ensembl; ENSRNOT00065045510; ENSRNOP00065037313; ENSRNOG00065026368.
DR   GeneID; 25550; -.
DR   KEGG; rno:25550; -.
DR   UCSC; RGD:3696; rat.
DR   AGR; RGD:3696; -.
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   OrthoDB; 49426at2759; -.
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 cell types or tissues.
DR   Genevisible; P51907; RN.
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: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:0098794; C:postsynapse; ISO:RGD.
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:0098685; C:Schaffer collateral - CA1 synapse; 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: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:0005253; F:monoatomic anion channel 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: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: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:0090461; P:intracellular glutamate homeostasis; ISO:RGD.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; 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:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0098877; P:neurotransmitter receptor transport to plasma membrane; ISO:RGD.
DR   GO; GO:0010460; P:positive regulation of heart rate; ISO:RGD.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; 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; Sodium:dicarboxylate symporter; 1.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR   PANTHER; PTHR11958:SF110; EXCITATORY AMINO ACID TRANSPORTER 3; 1.
DR   PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   SUPFAM; SSF118215; Proton glutamate symport protein; 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
//
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