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Glutamate transporter homolog (Glt(Ph)) (Sodium-aspartate symporter Glt(Ph)) (Sodium-dependent aspartate transporter)

 GLT_PYRHO               Reviewed;         425 AA.
O59010;
05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Glutamate transporter homolog {ECO:0000303|PubMed:15483603};
Short=Glt(Ph) {ECO:0000303|PubMed:15483603};
AltName: Full=Sodium-aspartate symporter Glt(Ph) {ECO:0000303|PubMed:28137870};
AltName: Full=Sodium-dependent aspartate transporter {ECO:0000303|PubMed:17230192, ECO:0000303|PubMed:19380583};
OrderedLocusNames=PH1295 {ECO:0000312|EMBL:BAA30399.1};
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
NBRC 100139 / OT-3).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=70601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
{ECO:0000312|Proteomes:UP000000752};
PubMed=9679194; DOI=10.1093/dnares/5.2.55;
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
Masuchi Y., Shizuya H., Kikuchi H.;
"Complete sequence and gene organization of the genome of a hyper-
thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
DNA Res. 5:55-76(1998).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-65.
PubMed=17435767; DOI=10.1038/nsmb1230;
Ryan R.M., Mindell J.A.;
"The uncoupled chloride conductance of a bacterial glutamate
transporter homolog.";
Nat. Struct. Mol. Biol. 14:365-371(2007).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19380583; DOI=10.1074/jbc.M109.005926;
Ryan R.M., Compton E.L., Mindell J.A.;
"Functional characterization of a Na+-dependent aspartate transporter
from Pyrococcus horikoshii.";
J. Biol. Chem. 284:17540-17548(2009).
[4]
ELECTRON MICROSCOPY, DOMAIN, SUBUNIT, SUBCELLULAR LOCATION, AND
TOPOLOGY.
PubMed=28137870; DOI=10.1073/pnas.1616413114;
Ruan Y., Miyagi A., Wang X., Chami M., Boudker O., Scheuring S.;
"Direct visualization of glutamate transporter elevator mechanism by
high-speed AFM.";
Proc. Natl. Acad. Sci. U.S.A. 114:1584-1588(2017).
[5] {ECO:0000244|PDB:1XFH}
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-417, SUBUNIT, SUBCELLULAR
LOCATION, AND TOPOLOGY.
PubMed=15483603; DOI=10.1038/nature03018;
Yernool D., Boudker O., Jin Y., Gouaux E.;
"Structure of a glutamate transporter homologue from Pyrococcus
horikoshii.";
Nature 431:811-818(2004).
[6] {ECO:0000244|PDB:2NWL, ECO:0000244|PDB:2NWW, ECO:0000244|PDB:2NWX}
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1-417 IN COMPLEXES WITH
ASPARTATE; INHIBITOR AND SODIUM, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, TOPOLOGY, AND MUTAGENESIS OF ASP-405.
PubMed=17230192; DOI=10.1038/nature05455;
Boudker O., Ryan R.M., Yernool D., Shimamoto K., Gouaux E.;
"Coupling substrate and ion binding to extracellular gate of a sodium-
dependent aspartate transporter.";
Nature 445:387-393(2007).
[7] {ECO:0000244|PDB:3KBC}
X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS), SUBUNIT, TOPOLOGY, AND DOMAIN.
PubMed=19924125; DOI=10.1038/nature08616;
Reyes N., Ginter C., Boudker O.;
"Transport mechanism of a bacterial homologue of glutamate
transporters.";
Nature 462:880-885(2009).
[8] {ECO:0000244|PDB:3V8F, ECO:0000244|PDB:3V8G}
X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 1-417, SUBUNIT, AND
TOPOLOGY.
PubMed=22343718; DOI=10.1038/nsmb.2233;
Verdon G., Boudker O.;
"Crystal structure of an asymmetric trimer of a bacterial glutamate
transporter homolog.";
Nat. Struct. Mol. Biol. 19:355-357(2012).
[9] {ECO:0000244|PDB:4IZM}
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 1-417, SUBUNIT, TOPOLOGY,
AND DOMAIN.
PubMed=23563139; DOI=10.1038/nsmb.2548;
Reyes N., Oh S., Boudker O.;
"Binding thermodynamics of a glutamate transporter homolog.";
Nat. Struct. Mol. Biol. 20:634-640(2013).
[10] {ECO:0000244|PDB:4OYE, ECO:0000244|PDB:4OYF, ECO:0000244|PDB:4P19}
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-417, SUBUNIT, TOPOLOGY,
DOMAIN, AND MUTAGENESIS OF MET-311 AND ARG-397.
PubMed=24842876; DOI=10.7554/eLife.02283;
Verdon G., Oh S., Serio R.N., Boudker O.;
"Coupled ion binding and structural transitions along the transport
cycle of glutamate transporters.";
Elife 3:E02283-E02283(2014).
[11] {ECO:0000244|PDB:4X2S}
X-RAY CRYSTALLOGRAPHY (4.21 ANGSTROMS) OF 1-417, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ARG-276 AND
MET-395.
DOI=10.1038/nature14158;
Akyuz N., Georgieva E., Zhou Z., Stolzenberg S., Cuendet M.,
Khelashvili G., Altman R.B., Terry D.S., Freed J.H., Weinstein H.,
Boudker O., Blanchard S.C.;
"Transport domain motions in a glutamate transporter homologue
determine turnover rate.";
Nature 0:0-0(2015).
-!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter
that mediates aspartate uptake (PubMed:17435767, PubMed:19380583,
PubMed:17230192, Ref.11). Has only very low glutamate transport
activity (PubMed:19380583, PubMed:17230192). Functions as a
symporter that transports one amino acid molecule together with
two or three Na(+) ions, resulting in electrogenic transport
(PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances
the affinity for aspartate (PubMed:19380583, Ref.11). 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:17435767). In contrast to mammalian
homologs, transport does not depend on pH or K(+) ions
(PubMed:19380583). {ECO:0000269|PubMed:17230192,
ECO:0000269|PubMed:17435767, ECO:0000269|PubMed:19380583,
ECO:0000269|Ref.11}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=120 nM for L-aspartate transport
{ECO:0000269|PubMed:19380583};
Vmax=3.7 nmol/min/mg enzyme {ECO:0000269|PubMed:19380583};
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15483603,
ECO:0000269|PubMed:17230192, ECO:0000269|PubMed:19924125,
ECO:0000269|PubMed:22343718, ECO:0000269|PubMed:23563139,
ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870,
ECO:0000269|Ref.11}.
-!- INTERACTION:
Self; NbExp=27; IntAct=EBI-15815831, EBI-15815831;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15483603,
ECO:0000305|PubMed:17230192, ECO:0000305|PubMed:17435767,
ECO:0000305|PubMed:19380583, ECO:0000305|PubMed:28137870,
ECO:0000305|Ref.11}; Multi-pass membrane protein
{ECO:0000269|PubMed:15483603, ECO:0000269|PubMed:17230192,
ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:22343718,
ECO:0000269|PubMed:23563139, ECO:0000269|PubMed:24842876,
ECO:0000269|PubMed:28137870, ECO:0000269|Ref.11}.
-!- 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, regions involved in
trimerization do not move. {ECO:0000269|PubMed:15483603,
ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:23563139,
ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870,
ECO:0000269|Ref.11}.
-!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation
symporter (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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EMBL; BA000001; BAA30399.1; -; Genomic_DNA.
PIR; E71075; E71075.
PDB; 1XFH; X-ray; 3.50 A; A/B/C=1-417.
PDB; 2NWL; X-ray; 2.96 A; A/B/C=1-417.
PDB; 2NWW; X-ray; 3.20 A; A/B/C=1-417.
PDB; 2NWX; X-ray; 3.29 A; A/B/C=1-417.
PDB; 3KBC; X-ray; 3.51 A; A/B/C=1-425.
PDB; 3V8F; X-ray; 3.80 A; A/B/C=1-417.
PDB; 3V8G; X-ray; 4.66 A; A/B/C/D/E/F=1-417.
PDB; 4IZM; X-ray; 4.50 A; A/B/C=1-417.
PDB; 4OYE; X-ray; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L=8-416.
PDB; 4OYF; X-ray; 3.41 A; A/B/C/D/E/F=1-419.
PDB; 4P19; X-ray; 3.25 A; A/B/C=1-417.
PDB; 4P1A; X-ray; 3.75 A; A/B/C=1-417.
PDB; 4P3J; X-ray; 3.50 A; A/B/C=1-417.
PDB; 4P6H; X-ray; 4.08 A; A/B/C=1-417.
PDB; 4X2S; X-ray; 4.21 A; A/B/C=1-417.
PDB; 5CFY; X-ray; 3.50 A; A/B/C/D/E/F=1-425.
PDBsum; 1XFH; -.
PDBsum; 2NWL; -.
PDBsum; 2NWW; -.
PDBsum; 2NWX; -.
PDBsum; 3KBC; -.
PDBsum; 3V8F; -.
PDBsum; 3V8G; -.
PDBsum; 4IZM; -.
PDBsum; 4OYE; -.
PDBsum; 4OYF; -.
PDBsum; 4P19; -.
PDBsum; 4P1A; -.
PDBsum; 4P3J; -.
PDBsum; 4P6H; -.
PDBsum; 4X2S; -.
PDBsum; 5CFY; -.
ProteinModelPortal; O59010; -.
SMR; O59010; -.
DIP; DIP-59313N; -.
STRING; 70601.PH1295; -.
TCDB; 2.A.23.1.5; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
EnsemblBacteria; BAA30399; BAA30399; BAA30399.
KEGG; pho:PH1295; -.
eggNOG; arCOG04335; Archaea.
eggNOG; COG1301; LUCA.
HOGENOM; HOG000208778; -.
OMA; VMGISEM; -.
OrthoDB; POG093Z02C3; -.
BioCyc; PHOR70601:GJWR-1291-MONOMER; -.
EvolutionaryTrace; O59010; -.
Proteomes; UP000000752; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005283; F:sodium:amino acid symporter activity; IDA:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
GO; GO:0140009; P:L-aspartate import across plasma membrane; IMP:UniProtKB.
GO; GO:0089712; P:L-aspartate transmembrane transport; IDA:UniProtKB.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
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; 1.
PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
1: Evidence at protein level;
3D-structure; Amino-acid transport; Cell membrane; Chloride;
Complete proteome; Membrane; Metal-binding; Sodium; Symport;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 425 Glutamate transporter homolog.
/FTId=PRO_0000440893.
TOPO_DOM 1 11 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 12 30 Helical; Name=1.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 31 41 Extracellular.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 42 62 Helical; Name=2.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 63 80 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 81 103 Helical; Name=3.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 104 121 Extracellular.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 122 160 Discontinuously helical; Name=4.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 161 196 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 197 218 Helical; Name=5.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 219 230 Extracellular.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 231 251 Helical; Name=6.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 252 260 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
INTRAMEM 261 289 Discontinuously helical.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 290 297 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 298 320 Discontinuously helical; Name=7.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 321 337 Extracellular.
{ECO:0000269|PubMed:15483603}.
INTRAMEM 338 372 Discontinuously helical.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 373 391 Extracellular.
{ECO:0000269|PubMed:15483603}.
TRANSMEM 392 412 Helical; Name=8.
{ECO:0000269|PubMed:15483603}.
TOPO_DOM 413 425 Cytoplasmic.
{ECO:0000269|PubMed:15483603}.
REGION 276 278 Aspartate binding. {ECO:0000244|PDB:2NWL,
ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:3KBC,
ECO:0000269|PubMed:17230192}.
METAL 306 306 Sodium 1; via carbonyl oxygen.
{ECO:0000244|PDB:2NWX,
ECO:0000305|PubMed:17230192}.
METAL 308 308 Sodium 2; via carbonyl oxygen.
{ECO:0000244|PDB:2NWX,
ECO:0000305|PubMed:17230192}.
METAL 310 310 Sodium 1. {ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:4X2S,
ECO:0000305|PubMed:17230192}.
METAL 352 352 Sodium 2; via carbonyl oxygen.
{ECO:0000244|PDB:2NWX,
ECO:0000305|PubMed:17230192}.
METAL 401 401 Sodium 1; via carbonyl oxygen.
{ECO:0000244|PDB:2NWX,
ECO:0000305|PubMed:17230192}.
METAL 405 405 Sodium 1. {ECO:0000244|PDB:2NWX,
ECO:0000305|PubMed:17230192}.
BINDING 314 314 Aspartate. {ECO:0000244|PDB:2NWL,
ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:3KBC,
ECO:0000269|PubMed:17230192}.
BINDING 355 355 Aspartate; via carbonyl oxygen.
{ECO:0000244|PDB:2NWL,
ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:3KBC,
ECO:0000269|PubMed:17230192}.
BINDING 394 394 Aspartate. {ECO:0000244|PDB:2NWL,
ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:3KBC,
ECO:0000269|PubMed:17230192}.
BINDING 401 401 Aspartate. {ECO:0000244|PDB:2NWL,
ECO:0000244|PDB:2NWX,
ECO:0000244|PDB:3KBC,
ECO:0000269|PubMed:17230192}.
MUTAGEN 65 65 S->V: Strongly decreased chloride
conductance.
{ECO:0000269|PubMed:17435767}.
MUTAGEN 276 276 R->S: Increased rate of aspartate
transport; when associated with R-395.
{ECO:0000269|Ref.11}.
MUTAGEN 311 311 M->A: Decreased dependence of aspartate
binding on Na(+) concentration.
{ECO:0000269|PubMed:24842876}.
MUTAGEN 395 395 M->R: Increased rate of aspartate
transport; when associated with S-276.
{ECO:0000269|Ref.11}.
MUTAGEN 397 397 R->A: Strongly decreased affinity for
aspartate. {ECO:0000269|PubMed:24842876}.
MUTAGEN 405 405 D->N: Strongly decreased affinity for
aspartate. {ECO:0000269|PubMed:17230192}.
HELIX 15 32 {ECO:0000244|PDB:2NWL}.
TURN 33 35 {ECO:0000244|PDB:2NWL}.
HELIX 36 42 {ECO:0000244|PDB:2NWL}.
HELIX 44 69 {ECO:0000244|PDB:2NWL}.
TURN 74 77 {ECO:0000244|PDB:2NWL}.
HELIX 78 106 {ECO:0000244|PDB:2NWL}.
TURN 109 112 {ECO:0000244|PDB:4P19}.
STRAND 118 120 {ECO:0000244|PDB:4P19}.
HELIX 131 134 {ECO:0000244|PDB:2NWL}.
HELIX 135 137 {ECO:0000244|PDB:2NWL}.
HELIX 142 147 {ECO:0000244|PDB:2NWL}.
HELIX 151 169 {ECO:0000244|PDB:2NWL}.
HELIX 174 201 {ECO:0000244|PDB:2NWL}.
HELIX 205 217 {ECO:0000244|PDB:2NWL}.
TURN 218 220 {ECO:0000244|PDB:2NWL}.
HELIX 221 223 {ECO:0000244|PDB:2NWL}.
HELIX 227 245 {ECO:0000244|PDB:2NWL}.
HELIX 247 253 {ECO:0000244|PDB:2NWL}.
HELIX 258 275 {ECO:0000244|PDB:2NWL}.
HELIX 278 290 {ECO:0000244|PDB:2NWL}.
TURN 291 293 {ECO:0000244|PDB:2NWL}.
HELIX 296 306 {ECO:0000244|PDB:2NWL}.
STRAND 307 309 {ECO:0000244|PDB:2NWW}.
HELIX 312 329 {ECO:0000244|PDB:2NWL}.
TURN 333 338 {ECO:0000244|PDB:1XFH}.
HELIX 339 351 {ECO:0000244|PDB:2NWL}.
STRAND 354 357 {ECO:0000244|PDB:2NWL}.
HELIX 358 370 {ECO:0000244|PDB:2NWL}.
HELIX 379 387 {ECO:0000244|PDB:2NWL}.
HELIX 390 415 {ECO:0000244|PDB:2NWL}.
SEQUENCE 425 AA; 44807 MW; 2F32EC45B0212FF5 CRC64;
MGLYRKYIEY PVLQKILIGL ILGAIVGLIL GHYGYADAVK TYVKPFGDLF VRLLKMLVMP
IVFASLVVGA ASISPARLGR VGVKIVVYYL LTSAFAVTLG IIMARLFNPG AGIHLAVGGQ
QFQPKQAPPL VKILLDIVPT NPFGALANGQ VLPTIFFAII LGIAITYLMN SENEKVRKSA
ETLLDAINGL AEAMYKIVNG VMQYAPIGVF ALIAYVMAEQ GVKVVGELAK VTAAVYVGLT
LQILLVYFVL LKIYGIDPIS FIKKAKDAML TAFVTRSSSG TLPVTMRVAK EMGISEGIYS
FTLPLGATIN MDGTALYQGV CTFFIANALG SHLTVGQQLT IVLTAVLASI GTAGVPGAGA
IMLAMVLESV GLPLTDPNVA AAYAMILGID AILDMGRTMV NVTGDLTGTA IVAKTEGELE
KGVIA


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EIAAB37133 Gabt2,Gabt3,Gat2,GAT-2,Gat3,GAT-3,Gat-3,Mouse,Mus musculus,Slc6a13,Sodium- and chloride-dependent GABA transporter 2,Sodium- and chloride-dependent GABA transporter 3,Solute carrier family 6 member 13
EIAAB37125 Gabt3,Gabt4,Gat3,GAT-3,Gat4,GAT-4,Gat-4,Mouse,Mus musculus,Slc6a11,Sodium- and chloride-dependent GABA transporter 3,Sodium- and chloride-dependent GABA transporter 4,Solute carrier family 6 member 11
EIAAB37145 Homo sapiens,Human,NTT4,SLC6A17,Sodium-dependent neurotransmitter transporter NTT4,Sodium-dependent neutral amino acid transporter SLC6A17,Solute carrier family 6 member 17
EIAAB37144 Ntt4,Rat,Rattus norvegicus,Rxt1,Slc6a17,Sodium-dependent neurotransmitter transporter NTT4,Sodium-dependent neutral amino acid transporter SLC6A17,Solute carrier family 6 member 17
EIAAB37142 Bos taurus,Bovine,NTT4,SLC6A17,Sodium-dependent neurotransmitter transporter NTT4,Sodium-dependent neutral amino acid transporter SLC6A17,Solute carrier family 6 member 17
EIAAB37143 Mouse,Mus musculus,Ntt4,Slc6a17,Sodium-dependent neurotransmitter transporter NTT4,Sodium-dependent neutral amino acid transporter SLC6A17,Solute carrier family 6 member 17
EIAAB37146 Homo sapiens,Human,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
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
EIAAB36763 Homo sapiens,hSVCT2,Human,KIAA0238,Na(+)_L-ascorbic acid transporter 2,NBTL1,Nucleobase transporter-like 1 protein,SLC23A1,SLC23A2,Sodium-dependent vitamin C transporter 2,Solute carrier family 23 mem
EIAAB36615 Na(+)_citrate cotransporter,NaCT,Nact,Rat,Rattus norvegicus,Slc13a5,Sodium-coupled citrate transporter,Sodium-dependent citrate transporter,Solute carrier family 13 member 5
EIAAB36616 Mouse,Mus musculus,Na(+)_citrate cotransporter,NaCT,Nact,Slc13a5,Sodium-coupled citrate transporter,Sodium-dependent citrate transporter,Solute carrier family 13 member 5


 

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