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Excitatory amino acid transporter 3 (Excitatory amino-acid carrier 1) (Neuronal and epithelial glutamate transporter) (Sodium-dependent glutamate/aspartate transporter 3) (Solute carrier family 1 member 1)

 EAA3_HUMAN              Reviewed;         524 AA.
P43005; O75587; Q5VZ24; Q8N199; Q9UEW2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
07-NOV-2018, entry version 169.
RecName: Full=Excitatory amino acid transporter 3;
AltName: Full=Excitatory amino-acid carrier 1;
AltName: Full=Neuronal and epithelial glutamate transporter;
AltName: Full=Sodium-dependent glutamate/aspartate transporter 3;
AltName: Full=Solute carrier family 1 member 1;
Name=SLC1A1; Synonyms=EAAC1, EAAT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=7859077; DOI=10.1016/0006-8993(94)90819-2;
Shashidharan P., Huntley G.W., Meyer T., Morrison J.H., Plaitakis A.;
"Neuron-specific human glutamate transporter: molecular cloning,
characterization and expression in human brain.";
Brain Res. 662:245-250(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=7914198;
Kanai Y., Stelzner M., Nussberger S., Khawaja S., Hebert S.C.,
Smith C.P., Hediger M.A.;
"The neuronal and epithelial human high affinity glutamate
transporter. Insights into structure and mechanism of transport.";
J. Biol. Chem. 269:20599-20606(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain cortex;
PubMed=7521911;
Arriza J.L., Fairman W.A., Wendy A., Wadiche J.I., Murdoch G.H.,
Kavanaugh M.P., Amara S.G.;
"Functional comparisons of three glutamate transporter subtypes cloned
from human motor cortex.";
J. Neurosci. 14:5559-5569(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11317217; DOI=10.1038/sj.mp.4000806;
Veenstra-VanderWeele J., Kim S.J., Gonen D., Hanna G.L.,
Leventhal B.L., Cook E.H. Jr.;
"Genomic organization of the SLC1A1/EAAC1 gene and mutation screening
in early-onset obsessive-compulsive disorder.";
Mol. Psychiatry 6:160-167(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
Yasuda-Kamatani Y.;
"A glutamate transporter related to EAAT3 from human brain.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 268-446.
TISSUE=Placenta;
Rome S., Mertani H.C., Lee K.O., Lobie P.E., Tome D.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8857541; DOI=10.1038/383634a0;
Zerangue N., Kavanaugh M.P.;
"Flux coupling in a neuronal glutamate transporter.";
Nature 383:634-637(1996).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=26690923; DOI=10.1007/s00232-015-9863-0;
Abousaab A., Warsi J., Elvira B., Lang F.;
"Caveolin-1 Sensitivity of Excitatory Amino Acid Transporters EAAT1,
EAAT2, EAAT3, and EAAT4.";
J. Membr. Biol. 249:239-249(2016).
[11]
INVOLVEMENT IN SCZD18.
PubMed=21982423; DOI=10.1016/j.biopsych.2011.08.009;
Melhem N., Middleton F., McFadden K., Klei L., Faraone S.V.,
Vinogradov S., Tiobech J., Yano V., Kuartei S., Roeder K., Byerley W.,
Devlin B., Myles-Worsley M.;
"Copy number variants for schizophrenia and related psychotic
disorders in Oceanic Palau: risk and transmission in extended
pedigrees.";
Biol. Psychiatry 70:1115-1121(2011).
[12]
INVOLVEMENT IN SCZD18.
PubMed=23341099; DOI=10.1002/ajmg.b.32125;
Myles-Worsley M., Tiobech J., Browning S.R., Korn J., Goodman S.,
Gentile K., Melhem N., Byerley W., Faraone S.V., Middleton F.A.;
"Deletion at the SLC1A1 glutamate transporter gene co-segregates with
schizophrenia and bipolar schizoaffective disorder in a 5-generation
family.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 162B:87-95(2013).
[13]
VARIANTS DCBXA ILE-395 DEL AND TRP-445, CHARACTERIZATION OF VARIANTS
DCBXA ILE-395 DEL AND TRP-445, INVOLVEMENT IN DCBXA, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=21123949; DOI=10.1172/JCI44474;
Bailey C.G., Ryan R.M., Thoeng A.D., Ng C., King K.,
Vanslambrouck J.M., Auray-Blais C., Vandenberg R.J., Broer S.,
Rasko J.E.;
"Loss-of-function mutations in the glutamate transporter SLC1A1 cause
human dicarboxylic aminoaciduria.";
J. Clin. Invest. 121:446-453(2011).
-!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter
that mediates the uptake of L-glutamate and also L-aspartate and
D-aspartate (PubMed:7914198, PubMed:7521911, PubMed:8857541,
PubMed:26690923, PubMed:21123949). Can also transport L-cysteine
(PubMed:21123949). Functions as a symporter that transports one
amino acid molecule together with two or three Na(+) ions and one
proton, in parallel with the counter-transport of one K(+) ion
(PubMed:7521911, PubMed:8857541, PubMed:26690923). Mediates Cl(-)
flux that is not coupled to amino acid transport; this avoids the
accumulation of negative charges due to aspartate and Na(+)
symport (PubMed:8857541, PubMed:26690923). Plays an important role
in L-glutamate and L-aspartate reabsorption in renal tubuli
(PubMed:21123949). Plays a redundant role in the rapid removal of
released glutamate from the synaptic cleft, which is essential for
terminating the postsynaptic action of glutamate (By similarity).
Negatively regulated by ARL6IP5 (By similarity).
{ECO:0000250|UniProtKB:P51906, ECO:0000250|UniProtKB:P51907,
ECO:0000269|PubMed:21123949, ECO:0000269|PubMed:26690923,
ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:7914198,
ECO:0000269|PubMed:8857541}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=268 uM for L-glutamate {ECO:0000269|PubMed:26690923};
-!- SUBUNIT: Homotrimer (Probable). Interacts with ARL6IP5 (By
similarity). {ECO:0000250|UniProtKB:P51906, ECO:0000305}.
-!- INTERACTION:
Q5T700:LDLRAD1; NbExp=3; IntAct=EBI-745376, EBI-10173166;
Q99942:RNF5; NbExp=5; IntAct=EBI-745376, EBI-348482;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21123949,
ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:7521911,
ECO:0000269|PubMed:7914198, ECO:0000269|PubMed:8857541}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P43003}. Apical cell
membrane {ECO:0000269|PubMed:21123949}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:P43003}.
-!- TISSUE SPECIFICITY: Expressed in all tissues tested including
liver, muscle, testis, ovary, retinoblastoma cell line, neurons
and brain (in which there was dense expression in substantia
nigra, red nucleus, hippocampus and in cerebral cortical layers).
{ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:7859077,
ECO:0000269|PubMed:7914198}.
-!- DOMAIN: Contains eight transmembrane regions plus two helical
hairpins that dip into the membrane. These helical hairpin
structures play an important role in the transport process. The
first enters the membrane from the cytoplasmic side, the second
one from the extracellular side. During the transport cycle, the
regions involved in amino acid transport, and especially the
helical hairpins, move vertically by about 15-18 Angstroms,
alternating between exposure to the aqueous phase and reinsertion
in the lipid bilayer. In contrast, the regions involved in
trimerization do not move. {ECO:0000250|UniProtKB:P43003}.
-!- PTM: Glycosylated.
-!- DISEASE: Dicarboxylic aminoaciduria (DCBXA) [MIM:222730]: An
autosomal recessive disorder characterized by abnormal excretion
of urinary glutamate and aspartate, resulting from the incomplete
reabsorption of anionic amino acids from the glomerular filtrate
in the kidney. It can be associated with mental retardation.
{ECO:0000269|PubMed:21123949}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Schizophrenia 18 (SCZD18) [MIM:615232]: A complex,
multifactorial psychotic disorder or group of disorders
characterized by disturbances in the form and content of thought
(e.g. delusions, hallucinations), in mood (e.g. inappropriate
affect), in sense of self and relationship to the external world
(e.g. loss of ego boundaries, withdrawal), and in behavior (e.g
bizarre or apparently purposeless behavior). Although it affects
emotions, it is distinguished from mood disorders in which such
disturbances are primary. Similarly, there may be mild impairment
of cognitive function, and it is distinguished from the dementias
in which disturbed cognitive function is considered primary. Some
patients manifest schizophrenic as well as bipolar disorder
symptoms and are often given the diagnosis of schizoaffective
disorder. {ECO:0000269|PubMed:21982423,
ECO:0000269|PubMed:23341099}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. A deletion at the chromosome 9p24.2 locus, including
SLC1A1, has been identified in patients with psychotic disorders
(PubMed:21982423). This 84 kb deletion is immediately upstream of
the SLC1A1 gene in a regulatory region that contains the full
native promoter sequence, extends through exon 1 of the SLC1A1
mRNA, co-segregates with disease in an extended 5-generation
pedigree and increases disease risk more than 18-fold for family
members (PubMed:23341099). {ECO:0000269|PubMed:21982423,
ECO:0000269|PubMed:23341099}.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A1 subfamily.
{ECO:0000305}.
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EMBL; U08989; AAA68628.1; -; mRNA.
EMBL; U06469; AAA53215.1; -; mRNA.
EMBL; U03506; AAA50430.1; -; mRNA.
EMBL; AF074911; AAC27511.3; -; Genomic_DNA.
EMBL; AF143773; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074903; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074904; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074905; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074906; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074907; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074908; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074909; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AF074910; AAC27511.3; JOINED; Genomic_DNA.
EMBL; AB008536; BAB83767.1; -; mRNA.
EMBL; AL162587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033040; AAH33040.1; -; mRNA.
EMBL; AF037982; AAC25029.1; -; mRNA.
CCDS; CCDS6452.1; -.
PIR; A54856; A54856.
PIR; I38433; I38433.
PIR; I38560; I38560.
RefSeq; NP_004161.4; NM_004170.5.
UniGene; Hs.444915; -.
ProteinModelPortal; P43005; -.
BioGrid; 112396; 42.
IntAct; P43005; 9.
STRING; 9606.ENSP00000262352; -.
BindingDB; P43005; -.
ChEMBL; CHEMBL2721; -.
DrugBank; DB00128; L-Aspartic Acid.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00230; Pregabalin.
GuidetoPHARMACOLOGY; 870; -.
TCDB; 2.A.23.2.3; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
iPTMnet; P43005; -.
PhosphoSitePlus; P43005; -.
BioMuta; SLC1A1; -.
DMDM; 1352332; -.
EPD; P43005; -.
MaxQB; P43005; -.
PaxDb; P43005; -.
PeptideAtlas; P43005; -.
PRIDE; P43005; -.
ProteomicsDB; 55571; -.
DNASU; 6505; -.
Ensembl; ENST00000262352; ENSP00000262352; ENSG00000106688.
GeneID; 6505; -.
KEGG; hsa:6505; -.
UCSC; uc003zij.3; human.
CTD; 6505; -.
DisGeNET; 6505; -.
EuPathDB; HostDB:ENSG00000106688.11; -.
GeneCards; SLC1A1; -.
HGNC; HGNC:10939; SLC1A1.
HPA; CAB015466; -.
HPA; HPA020086; -.
MalaCards; SLC1A1; -.
MIM; 133550; gene.
MIM; 222730; phenotype.
MIM; 615232; phenotype.
neXtProt; NX_P43005; -.
OpenTargets; ENSG00000106688; -.
Orphanet; 2195; Dicarboxylic aminoaciduria.
Orphanet; 166412; Hot water reflex epilepsy.
PharmGKB; PA35826; -.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; P43005; -.
KO; K05612; -.
OMA; YLYIAVI; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; P43005; -.
TreeFam; TF315206; -.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
Reactome; R-HSA-5619067; Defective SLC1A1 is implicated in schizophrenia 18 (SCZD18) and dicarboxylic aminoaciduria (DCBXA).
ChiTaRS; SLC1A1; human.
GeneWiki; SLC1A1; -.
GenomeRNAi; 6505; -.
PRO; PR:P43005; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106688; Expressed in 193 organ(s), highest expression level in caput epididymis.
CleanEx; HS_SLC1A1; -.
ExpressionAtlas; P43005; baseline and differential.
Genevisible; P43005; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
GO; GO:0015108; F:chloride transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0033229; F:cysteine transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:UniProtKB.
GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
GO; GO:0042883; P:cysteine transport; IDA:UniProtKB.
GO; GO:0070779; P:D-aspartate import across plasma membrane; IDA:UniProtKB.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0006811; P:ion transport; TAS:Reactome.
GO; GO:0140009; P:L-aspartate import across plasma membrane; IMP:UniProtKB.
GO; GO:0051938; P:L-glutamate import; IDA:UniProtKB.
GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:UniProtKB.
GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
Gene3D; 1.10.3860.10; -; 2.
InterPro; IPR001991; Na-dicarboxylate_symporter.
InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
InterPro; IPR036458; Na:dicarbo_symporter_sf.
Pfam; PF00375; SDF; 1.
SUPFAM; SSF118215; SSF118215; 1.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Chloride; Complete proteome;
Disease mutation; Glycoprotein; Membrane; Metal-binding;
Phosphoprotein; Polymorphism; Potassium; Reference proteome;
Schizophrenia; Sodium; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 524 Excitatory amino acid transporter 3.
/FTId=PRO_0000202065.
TOPO_DOM 1 18 Cytoplasmic. {ECO:0000305}.
TRANSMEM 19 38 Helical. {ECO:0000255}.
TOPO_DOM 39 61 Extracellular. {ECO:0000305}.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TOPO_DOM 83 93 Cytoplasmic. {ECO:0000305}.
TRANSMEM 94 114 Helical. {ECO:0000255}.
TOPO_DOM 115 205 Extracellular. {ECO:0000305}.
TRANSMEM 206 229 Helical; Name=4.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 230 238 Cytoplasmic. {ECO:0000305}.
TRANSMEM 239 266 Helical; Name=5.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 267 286 Extracellular. {ECO:0000305}.
TRANSMEM 287 308 Helical; Name=6.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 309 313 Cytoplasmic. {ECO:0000305}.
INTRAMEM 314 344 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 345 353 Cytoplasmic. {ECO:0000305}.
TRANSMEM 354 380 Helical; Name=7.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 381 393 Extracellular. {ECO:0000305}.
INTRAMEM 394 427 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 428 440 Extracellular. {ECO:0000305}.
TRANSMEM 441 462 Helical; Name=8.
{ECO:0000250|UniProtKB:P43003}.
TOPO_DOM 463 524 Cytoplasmic. {ECO:0000305}.
REGION 331 333 Aspartate binding.
{ECO:0000250|UniProtKB:P43003}.
REGION 411 415 Aspartate binding.
{ECO:0000250|UniProtKB:P43003}.
METAL 362 362 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 364 364 Sodium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P43003}.
METAL 366 366 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
METAL 451 451 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 455 455 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
BINDING 370 370 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
BINDING 444 444 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
BINDING 451 451 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000250|UniProtKB:P51906}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000250|UniProtKB:P51906}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 27 27 A -> G (in dbSNP:rs2229885).
/FTId=VAR_023309.
VARIANT 50 50 F -> Y (in dbSNP:rs2228621).
/FTId=VAR_023308.
VARIANT 395 395 Missing (in DCBXA; inhibits L-glutamate
and L-cysteine transport activities).
{ECO:0000269|PubMed:21123949}.
/FTId=VAR_071953.
VARIANT 445 445 R -> W (in DCBXA; reduces L-glutamate and
L-cysteine transport activities; reduces
cell membrane expression;
dbSNP:rs587777696).
{ECO:0000269|PubMed:21123949}.
/FTId=VAR_071954.
CONFLICT 10 10 E -> PS (in Ref. 3; AAA50430).
{ECO:0000305}.
CONFLICT 92 92 L -> V (in Ref. 7; AAH33040).
{ECO:0000305}.
CONFLICT 94 94 A -> V (in Ref. 1; AAA68628 and 4;
AAC27511). {ECO:0000305}.
CONFLICT 96 96 V -> L (in Ref. 2; AAA53215).
{ECO:0000305}.
CONFLICT 170 170 K -> N (in Ref. 2; AAA53215).
{ECO:0000305}.
CONFLICT 172 172 P -> A (in Ref. 2; AAA53215).
{ECO:0000305}.
CONFLICT 260 260 L -> H (in Ref. 2; AAA53215).
{ECO:0000305}.
CONFLICT 280 280 R -> A (in Ref. 1; AAA68628).
{ECO:0000305}.
CONFLICT 376 376 V -> G (in Ref. 8; AAC25029).
{ECO:0000305}.
SEQUENCE 524 AA; 57100 MW; FC6244ADC9EA228F CRC64;
MGKPARKGCE WKRFLKNNWV LLSTVAAVVL GITTGVLVRE HSNLSTLEKF YFAFPGEILM
RMLKLIILPL IISSMITGVA ALDSNVSGKI GLRAVVYYFC TTLIAVILGI VLVVSIKPGV
TQKVGEIART GSTPEVSTVD AMLDLIRNMF PENLVQACFQ QYKTKREEVK PPSDPEMNMT
EESFTAVMTT AISKNKTKEY KIVGMYSDGI NVLGLIVFCL VFGLVIGKMG EKGQILVDFF
NALSDATMKI VQIIMCYMPL GILFLIAGKI IEVEDWEIFR KLGLYMATVL TGLAIHSIVI
LPLIYFIVVR KNPFRFAMGM AQALLTALMI SSSSATLPVT FRCAEENNQV DKRITRFVLP
VGATINMDGT ALYEAVAAVF IAQLNDLDLG IGQIITISIT ATSASIGAAG VPQAGLVTMV
IVLSAVGLPA EDVTLIIAVD WLLDRFRTMV NVLGDAFGTG IVEKLSKKEL EQMDVSSEVN
IVNPFALEST ILDNEDSDTK KSYVNGGFAV DKSDTISFTQ TSQF


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