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Excitatory amino acid transporter 2 (GLT-1) (Sodium-dependent glutamate/aspartate transporter 2) (Solute carrier family 1 member 2)

 EAA2_MOUSE              Reviewed;         572 AA.
P43006; O35877; O54686; O54687;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Excitatory amino acid transporter 2;
AltName: Full=GLT-1 {ECO:0000303|PubMed:9180080, ECO:0000303|PubMed:9373176};
AltName: Full=Sodium-dependent glutamate/aspartate transporter 2;
AltName: Full=Solute carrier family 1 member 2;
Name=Slc1a2; Synonyms=Eaat2, Glt1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=7698742; DOI=10.1006/geno.1994.1609;
Kirschner M.A., Copeland N.G., Gilbert D.J., Jenkins N.A., Amara S.G.;
"Mouse excitatory amino acid transporter EAAT2: isolation,
characterization, and proximity to neuroexcitability loci on mouse
chromosome 2.";
Genomics 24:218-224(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=JCL:ICR; TISSUE=Cerebellum;
PubMed=7766664; DOI=10.1016/0304-4165(95)00062-G;
Mukainaka Y., Tanaka K., Hagiwara T., Wada K.;
"Molecular cloning of two glutamate transporter subtypes from mouse
brain.";
Biochim. Biophys. Acta 1244:233-237(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=7557442; DOI=10.1016/0378-1119(95)00293-F;
Sutherland M.L., Delaney T.A., Noebels J.L.;
"Molecular characterization of a high-affinity mouse glutamate
transporter.";
Gene 162:271-274(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Peng J.-B., Guo L.-H.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
SPECIFICITY.
STRAIN=JCL:ICR; TISSUE=Brain, and Liver;
PubMed=9373176; DOI=10.1016/S0014-5793(97)01232-5;
Utsunomiya-Tate N., Endou H., Kanai Y.;
"Tissue specific variants of glutamate transporter GLT-1.";
FEBS Lett. 416:312-316(1997).
[6]
PROTEIN SEQUENCE OF 66-87; 159-173 AND 478-525, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=9180080;
Tanaka K., Watase K., Manabe T., Yamada K., Watanabe M., Takahashi K.,
Iwama H., Nishikawa T., Ichihara N., Kikuchi T., Okuyama S.,
Kawashima N., Hori S., Takimoto M., Wada K.;
"Epilepsy and exacerbation of brain injury in mice lacking the
glutamate transporter GLT-1.";
Science 276:1699-1702(1997).
[8]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=16880397; DOI=10.1073/pnas.0509144103;
Matsugami T.R., Tanemura K., Mieda M., Nakatomi R., Yamada K.,
Kondo T., Ogawa M., Obata K., Watanabe M., Hashikawa T., Tanaka K.;
"Indispensability of the glutamate transporters GLAST and GLT1 to
brain development.";
Proc. Natl. Acad. Sci. U.S.A. 103:12161-12166(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-505; SER-520;
SER-530; SER-532; SER-542; SER-558 AND SER-562, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
PALMITOYLATION AT CYS-38, AND MUTAGENESIS OF CYS-38.
PubMed=20685337; DOI=10.1016/j.nbd.2010.05.027;
Huang K., Kang M.H., Askew C., Kang R., Sanders S.S., Wan J.,
Davis N.G., Hayden M.R.;
"Palmitoylation and function of glial glutamate transporter-1 is
reduced in the YAC128 mouse model of Huntington disease.";
Neurobiol. Dis. 40:207-215(2010).
-!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter
that mediates the uptake of L-glutamate and also L-aspartate and
D-aspartate (PubMed:7698742, PubMed:7557442, PubMed:9373176).
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. Mediates Cl(-) flux
that is not coupled to amino acid transport; this avoids the
accumulation of negative charges due to aspartate and Na(+)
symport (By similarity). Essential for the rapid removal of
released glutamate from the synaptic cleft, and for terminating
the postsynaptic action of glutamate (PubMed:9180080).
{ECO:0000250|UniProtKB:P43004, ECO:0000269|PubMed:7557442,
ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080,
ECO:0000269|PubMed:9373176}.
-!- SUBUNIT: Homotrimer (By similarity). Interacts with AJUBA (By
similarity). {ECO:0000250|UniProtKB:P31596,
ECO:0000250|UniProtKB:P43004}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7557442,
ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9373176}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P43004}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Glt-1;
IsoId=P43006-1; Sequence=Displayed;
Name=Glt-1A;
IsoId=P43006-2; Sequence=VSP_006264;
Name=Glt-1B;
IsoId=P43006-3; Sequence=VSP_006264, VSP_006265;
-!- TISSUE SPECIFICITY: Detected in brain (PubMed:9180080). Detected
in embryonic forebrain, especially in globus pallidus, perirhinal
cortex, lateral hypothalamus, hippocampus, and on fimbria and
axonal pathways connecting the neocortex, basal ganglia and
thalamus (at protein level) (PubMed:16880397). Isoform GLT1 is
expressed in the brain (PubMed:7698742, PubMed:7557442,
PubMed:9373176, PubMed:9180080). Isoforms GLT-1A and GLT-1B are
expressed in the liver (PubMed:9373176).
{ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:7557442,
ECO:0000269|PubMed:7698742, ECO:0000269|PubMed:9180080,
ECO:0000269|PubMed:9373176}.
-!- 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. {ECO:0000250|UniProtKB:P43004}.
-!- PTM: Palmitoylation at Cys-38 is not required for correct
subcellular localization, but is important for glutamate uptake
activity. {ECO:0000269|PubMed:20685337}.
-!- DISRUPTION PHENOTYPE: No visible phenotype at birth
(PubMed:9180080, PubMed:16880397). Mice are born at the expected
Mendelian rate, but gain weight more slowly, especially after the
first 30 days after birth (PubMed:9180080). Only half of them are
still alive 60 days after birth (PubMed:9180080). Death is due to
spontaneous epileptic seizures (PubMed:9180080). Besides, mutant
mice display neuronal degeneration in the hippocampus CA1 field,
probably due to impaired glutamate removal from the synaptic cleft
(PubMed:9180080). Glutamate uptake by synaptosomes from mutant
mouse brain cortex is reduced by 94% (PubMed:9180080). Mice
deficient in both Slc1a2 and Slc1a3 die at about 17 dpc; they
display defects in the brain structure that affects the brain
cortex, hippocampus and olfactory bulb, due to impaired radial
migration of neurons into the cortical plate and disorganization
of the radial glial cell arrangement (PubMed:16880397).
{ECO:0000269|PubMed:16880397, ECO:0000269|PubMed:9180080}.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. SLC1A2 subfamily.
{ECO:0000305}.
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EMBL; U11763; AAA77673.1; -; mRNA.
EMBL; D43796; BAA07854.1; -; mRNA.
EMBL; U24699; AAA91643.1; -; mRNA.
EMBL; U75372; AAB71737.1; -; mRNA.
EMBL; U75373; AAB71738.1; -; mRNA.
EMBL; AB007810; BAA23770.1; -; mRNA.
EMBL; AB007811; BAA23771.1; -; mRNA.
EMBL; AB007812; BAA23772.1; -; mRNA.
CCDS; CCDS16469.1; -. [P43006-3]
CCDS; CCDS38188.1; -. [P43006-1]
CCDS; CCDS38189.1; -. [P43006-2]
PIR; A55676; A55676.
PIR; JC4262; JC4262.
RefSeq; NP_001070982.1; NM_001077514.3. [P43006-1]
RefSeq; NP_001070983.1; NM_001077515.2. [P43006-2]
RefSeq; NP_035523.1; NM_011393.2. [P43006-3]
UniGene; Mm.267547; -.
UniGene; Mm.371582; -.
UniGene; Mm.453107; -.
UniGene; Mm.453110; -.
ProteinModelPortal; P43006; -.
BioGrid; 203290; 7.
IntAct; P43006; 8.
MINT; MINT-4093909; -.
STRING; 10090.ENSMUSP00000079100; -.
iPTMnet; P43006; -.
PhosphoSitePlus; P43006; -.
SwissPalm; P43006; -.
PaxDb; P43006; -.
PeptideAtlas; P43006; -.
PRIDE; P43006; -.
Ensembl; ENSMUST00000005220; ENSMUSP00000005220; ENSMUSG00000005089. [P43006-3]
Ensembl; ENSMUST00000080210; ENSMUSP00000079100; ENSMUSG00000005089. [P43006-1]
Ensembl; ENSMUST00000111212; ENSMUSP00000106843; ENSMUSG00000005089. [P43006-2]
GeneID; 20511; -.
KEGG; mmu:20511; -.
UCSC; uc008lid.2; mouse. [P43006-1]
CTD; 6506; -.
MGI; MGI:101931; Slc1a2.
eggNOG; KOG3787; Eukaryota.
eggNOG; COG1301; LUCA.
GeneTree; ENSGT00760000119117; -.
HOGENOM; HOG000208776; -.
HOVERGEN; HBG000080; -.
InParanoid; P43006; -.
KO; K05613; -.
OMA; VDWFMGI; -.
OrthoDB; EOG091G0UCE; -.
PhylomeDB; P43006; -.
TreeFam; TF315206; -.
Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-MMU-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
ChiTaRS; Slc1a2; mouse.
PRO; PR:P43006; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000005089; -.
ExpressionAtlas; P43006; baseline and differential.
Genevisible; P43006; MM.
GO; GO:0030673; C:axolemma; IDA:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0008509; F:anion transmembrane transporter activity; IDA:MGI.
GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:MGI.
GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030534; P:adult behavior; IMP:MGI.
GO; GO:0098656; P:anion transmembrane transport; IDA:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
GO; GO:0070779; P:D-aspartate import; ISO:MGI.
GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:UniProtKB.
GO; GO:0089711; P:L-glutamate transmembrane transport; IDA:MGI.
GO; GO:0015813; P:L-glutamate transport; IDA:MGI.
GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
GO; GO:0043200; P:response to amino acid; IMP:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0009416; P:response to light stimulus; IMP:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0021537; P:telencephalon development; IMP:MGI.
GO; GO:0007632; P:visual behavior; IMP:MGI.
Gene3D; 1.10.3860.10; -; 1.
InterPro; IPR036458; Na-dicarbo_symporter_sf.
InterPro; IPR001991; Na-dicarboxylate_symporter.
InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
Pfam; PF00375; SDF; 1.
PRINTS; PR00173; EDTRNSPORT.
SUPFAM; SSF118215; SSF118215; 2.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
1: Evidence at protein level;
Alternative splicing; Amino-acid transport; Cell membrane; Chloride;
Complete proteome; Direct protein sequencing; Glycoprotein;
Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
Potassium; Reference proteome; Sodium; Symport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 572 Excitatory amino acid transporter 2.
/FTId=PRO_0000202062.
TOPO_DOM 1 44 Cytoplasmic. {ECO:0000255}.
TRANSMEM 45 64 Helical. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TRANSMEM 121 142 Helical. {ECO:0000255}.
TRANSMEM 235 258 Helical; Name=4.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 268 295 Helical; Name=5.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 317 338 Helical; Name=6.
{ECO:0000250|UniProtKB:P43003}.
INTRAMEM 344 374 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 384 410 Helical; Name=7.
{ECO:0000250|UniProtKB:P43003}.
INTRAMEM 424 457 Discontinuously helical.
{ECO:0000250|UniProtKB:P43003}.
TRANSMEM 471 492 Helical; Name=8.
{ECO:0000250|UniProtKB:P43003}.
REGION 361 363 Aspartate binding.
{ECO:0000250|UniProtKB:P43003}.
REGION 441 445 Aspartate binding.
{ECO:0000250|UniProtKB:P43003}.
METAL 392 392 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 394 394 Sodium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P43003}.
METAL 396 396 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
METAL 481 481 Sodium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O59010}.
METAL 485 485 Sodium 1. {ECO:0000250|UniProtKB:O59010}.
BINDING 400 400 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
BINDING 474 474 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
BINDING 481 481 Aspartate.
{ECO:0000250|UniProtKB:P43003}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P31596}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:P31596}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:P31596}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 537 537 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 542 542 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 38 38 S-palmitoyl cysteine.
{ECO:0000269|PubMed:20685337}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 6 MASTEG -> MVS (in isoform Glt-1A and
isoform Glt-1B). {ECO:0000305}.
/FTId=VSP_006264.
VAR_SEQ 551 572 TLAANGKSADCSVEEEPWKREK -> PFPFLDIETCI (in
isoform Glt-1B). {ECO:0000305}.
/FTId=VSP_006265.
MUTAGEN 38 38 C->S: Severely impairs glutamate uptake
activity. {ECO:0000269|PubMed:20685337}.
CONFLICT 26 26 D -> E (in Ref. 3; AAA91643).
{ECO:0000305}.
CONFLICT 62 62 G -> R (in Ref. 3; AAA91643).
{ECO:0000305}.
CONFLICT 112 112 A -> V (in Ref. 3; AAA91643).
{ECO:0000305}.
CONFLICT 454 454 T -> I (in Ref. 4; AAB71737).
{ECO:0000305}.
CONFLICT 525 525 K -> L (in Ref. 4; AAB71737).
{ECO:0000305}.
CONFLICT 572 572 K -> EFD (in Ref. 3; AAA91643).
{ECO:0000305}.
SEQUENCE 572 AA; 62030 MW; 13C7C30DED40CA81 CRC64;
MASTEGANNM PKQVEVRMHD SHLSSDEPKH RNLGMRMCDK LGKNLLLSLT VFGVILGAVC
GGLLRLASPI HPDVVMLIAF PGDILMRMLK MLILPLIISS LITGLSGLDA KASGRLGTRA
MVYYMSTTII AAVLGVILVL AIHPGNPKLK KQLGPGKKND EVSSLDAFLD LIRNLFPENL
VQACFQQIQT VTKKVLVAPP SEEANTTKAV ISMLNETMNE APEETKIVIK KGLEFKDGMN
VLGLIGFFIA FGIAMGKMGE QAKLMVEFFN ILNEIVMKLV IMIMWYSPLG IACLICGKII
AIKDLEVVAR QLGMYMITVI VGLIIHGGIF LPLIYFVVTR KNPFSFFAGI FQAWITALGT
ASSAGTLPVT FRCLEDNLGI DKRVTRFVLP VGATINMDGT ALYEAVAAIF IAQMNGVILD
GGQIVTVSLT ATLASIGAAS IPSAGLVTML LILTAVGLPT EDISLLVAVD WLLDRMRTSV
NVVGDSFGAG IVYHLSKSEL DTIDSQHRMQ EDIEMTKTQS IYDDKNHRES NSNQCVYAAH
NSVVIDECKV TLAANGKSAD CSVEEEPWKR EK


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EIAAB37148 Mouse,Mus musculus,Slc6a18,Sodium- and chloride-dependent transporter XTRP2,Sodium-dependent neutral amino acid transporter B(0)AT3,Solute carrier family 6 member 18,System B(0) neutral amino acid tra
EIAAB37136 Amino acid transporter ATB0+,Homo sapiens,Human,SLC6A14,Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+),Solute carrier family 6 member 14
EIAAB37138 Ntt73,Rat,Rattus norvegicus,Slc6a15,sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Transpor
EIAAB37137 B0at2,Mouse,Mus musculus,Ntt73,Slc6a15,Sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Trans
EIAAB37140 B0AT2,Bos taurus,Bovine,NTT73,SLC6A15,Sodium- and chloride-dependent neurotransmitter transporter NTT73,Sodium-dependent neutral amino acid transporter B(0)AT2,Solute carrier family 6 member 15,Transp
EIAAB37151 B0at1,Mouse,Mus musculus,Slc6a19,Sodium-dependent neutral amino acid transporter B(0)AT1,Solute carrier family 6 member 19,System B(0) neutral amino acid transporter AT1
EIAAB37150 B0at1,Rat,Rattus norvegicus,Slc6a19,Sodium-dependent neutral amino acid transporter B(0)AT1,Solute carrier family 6 member 19,System B(0) neutral amino acid transporter AT1
EIAAB37149 B0AT1,Homo sapiens,Human,SLC6A19,Sodium-dependent neutral amino acid transporter B(0)AT1,Solute carrier family 6 member 19,System B(0) neutral amino acid transporter AT1


 

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