GLT_PYRHO
ID GLT_PYRHO Reviewed; 425 AA.
AC O59010;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Glutamate transporter homolog {ECO:0000303|PubMed:15483603};
DE Short=Glt(Ph) {ECO:0000303|PubMed:15483603};
DE AltName: Full=Sodium-aspartate symporter Glt(Ph) {ECO:0000303|PubMed:28137870};
DE AltName: Full=Sodium-dependent aspartate transporter {ECO:0000303|PubMed:17230192, ECO:0000303|PubMed:19380583};
GN OrderedLocusNames=PH1295 {ECO:0000312|EMBL:BAA30399.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
RC {ECO:0000312|Proteomes:UP000000752};
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-65.
RX PubMed=17435767; DOI=10.1038/nsmb1230;
RA Ryan R.M., Mindell J.A.;
RT "The uncoupled chloride conductance of a bacterial glutamate transporter
RT homolog.";
RL Nat. Struct. Mol. Biol. 14:365-371(2007).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19380583; DOI=10.1074/jbc.m109.005926;
RA Ryan R.M., Compton E.L., Mindell J.A.;
RT "Functional characterization of a Na+-dependent aspartate transporter from
RT Pyrococcus horikoshii.";
RL J. Biol. Chem. 284:17540-17548(2009).
RN [4]
RP ELECTRON MICROSCOPY, DOMAIN, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=28137870; DOI=10.1073/pnas.1616413114;
RA Ruan Y., Miyagi A., Wang X., Chami M., Boudker O., Scheuring S.;
RT "Direct visualization of glutamate transporter elevator mechanism by high-
RT speed AFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:1584-1588(2017).
RN [5] {ECO:0007744|PDB:1XFH}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-417, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=15483603; DOI=10.1038/nature03018;
RA Yernool D., Boudker O., Jin Y., Gouaux E.;
RT "Structure of a glutamate transporter homologue from Pyrococcus
RT horikoshii.";
RL Nature 431:811-818(2004).
RN [6] {ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWW, ECO:0007744|PDB:2NWX}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1-417 IN COMPLEXES WITH
RP ASPARTATE; INHIBITOR AND SODIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP TOPOLOGY, AND MUTAGENESIS OF ASP-405.
RX PubMed=17230192; DOI=10.1038/nature05455;
RA Boudker O., Ryan R.M., Yernool D., Shimamoto K., Gouaux E.;
RT "Coupling substrate and ion binding to extracellular gate of a sodium-
RT dependent aspartate transporter.";
RL Nature 445:387-393(2007).
RN [7] {ECO:0007744|PDB:3KBC}
RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS), SUBUNIT, TOPOLOGY, AND DOMAIN.
RX PubMed=19924125; DOI=10.1038/nature08616;
RA Reyes N., Ginter C., Boudker O.;
RT "Transport mechanism of a bacterial homologue of glutamate transporters.";
RL Nature 462:880-885(2009).
RN [8] {ECO:0007744|PDB:3V8F, ECO:0007744|PDB:3V8G}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 1-417, SUBUNIT, AND TOPOLOGY.
RX PubMed=22343718; DOI=10.1038/nsmb.2233;
RA Verdon G., Boudker O.;
RT "Crystal structure of an asymmetric trimer of a bacterial glutamate
RT transporter homolog.";
RL Nat. Struct. Mol. Biol. 19:355-357(2012).
RN [9] {ECO:0007744|PDB:4IZM}
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 1-417, SUBUNIT, TOPOLOGY, AND
RP DOMAIN.
RX PubMed=23563139; DOI=10.1038/nsmb.2548;
RA Reyes N., Oh S., Boudker O.;
RT "Binding thermodynamics of a glutamate transporter homolog.";
RL Nat. Struct. Mol. Biol. 20:634-640(2013).
RN [10] {ECO:0007744|PDB:4OYE, ECO:0007744|PDB:4OYF, ECO:0007744|PDB:4P19}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-417, SUBUNIT, TOPOLOGY, DOMAIN,
RP AND MUTAGENESIS OF MET-311 AND ARG-397.
RX PubMed=24842876; DOI=10.7554/elife.02283;
RA Verdon G., Oh S., Serio R.N., Boudker O.;
RT "Coupled ion binding and structural transitions along the transport cycle
RT of glutamate transporters.";
RL Elife 3:E02283-E02283(2014).
RN [11] {ECO:0007744|PDB:4X2S}
RP X-RAY CRYSTALLOGRAPHY (4.21 ANGSTROMS) OF 1-417, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND MUTAGENESIS OF ARG-276 AND
RP MET-395.
RX DOI=10.1038/nature14158;
RA Akyuz N., Georgieva E., Zhou Z., Stolzenberg S., Cuendet M.,
RA Khelashvili G., Altman R.B., Terry D.S., Freed J.H., Weinstein H.,
RA Boudker O., Blanchard S.C.;
RT "Transport domain motions in a glutamate transporter homologue determine
RT turnover rate.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates aspartate uptake (PubMed:17435767, PubMed:19380583,
CC PubMed:17230192, Ref.11). Has only very low glutamate transport
CC activity (PubMed:19380583, PubMed:17230192). Functions as a symporter
CC that transports one amino acid molecule together with two or three
CC Na(+) ions, resulting in electrogenic transport (PubMed:17435767,
CC PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for
CC aspartate (PubMed:19380583, Ref.11). 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 (PubMed:17435767).
CC In contrast to mammalian homologs, transport does not depend on pH or
CC K(+) ions (PubMed:19380583). {ECO:0000269|PubMed:17230192,
CC ECO:0000269|PubMed:17435767, ECO:0000269|PubMed:19380583,
CC ECO:0000269|Ref.11}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 nM for L-aspartate transport {ECO:0000269|PubMed:19380583};
CC Vmax=3.7 nmol/min/mg enzyme {ECO:0000269|PubMed:19380583};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15483603,
CC ECO:0000269|PubMed:17230192, ECO:0000269|PubMed:19924125,
CC ECO:0000269|PubMed:22343718, ECO:0000269|PubMed:23563139,
CC ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870,
CC ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC O59010; O59010: PH1295; NbExp=27; IntAct=EBI-15815831, EBI-15815831;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15483603,
CC ECO:0000305|PubMed:17230192, ECO:0000305|PubMed:17435767,
CC ECO:0000305|PubMed:19380583, ECO:0000305|PubMed:28137870,
CC ECO:0000305|Ref.11}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15483603, ECO:0000269|PubMed:17230192,
CC ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:22343718,
CC ECO:0000269|PubMed:23563139, ECO:0000269|PubMed:24842876,
CC ECO:0000269|PubMed:28137870, ECO:0000269|Ref.11}.
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, regions
CC involved in trimerization do not move. {ECO:0000269|PubMed:15483603,
CC ECO:0000269|PubMed:19924125, ECO:0000269|PubMed:23563139,
CC ECO:0000269|PubMed:24842876, ECO:0000269|PubMed:28137870,
CC ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30399.1; -; Genomic_DNA.
DR PIR; E71075; E71075.
DR RefSeq; WP_010885380.1; NC_000961.1.
DR PDB; 1XFH; X-ray; 3.50 A; A/B/C=1-417.
DR PDB; 2NWL; X-ray; 2.96 A; A/B/C=1-417.
DR PDB; 2NWW; X-ray; 3.20 A; A/B/C=1-417.
DR PDB; 2NWX; X-ray; 3.29 A; A/B/C=1-417.
DR PDB; 3KBC; X-ray; 3.51 A; A/B/C=1-425.
DR PDB; 3V8F; X-ray; 3.80 A; A/B/C=1-417.
DR PDB; 3V8G; X-ray; 4.66 A; A/B/C/D/E/F=1-417.
DR PDB; 4IZM; X-ray; 4.50 A; A/B/C=1-417.
DR PDB; 4OYE; X-ray; 4.00 A; A/B/C/D/E/F/G/H/I/J/K/L=8-416.
DR PDB; 4OYF; X-ray; 3.41 A; A/B/C/D/E/F=1-419.
DR PDB; 4P19; X-ray; 3.25 A; A/B/C=1-417.
DR PDB; 4P1A; X-ray; 3.75 A; A/B/C=1-417.
DR PDB; 4P3J; X-ray; 3.50 A; A/B/C=1-417.
DR PDB; 4P6H; X-ray; 4.08 A; A/B/C=1-417.
DR PDB; 4X2S; X-ray; 4.21 A; A/B/C=1-417.
DR PDB; 5CFY; X-ray; 3.50 A; A/B/C/D/E/F=1-425.
DR PDB; 6BAT; X-ray; 3.40 A; A/B/C=1-417.
DR PDB; 6BAU; X-ray; 3.80 A; A/B/C=1-417.
DR PDB; 6BAV; X-ray; 3.70 A; A/B/C=1-417.
DR PDB; 6BMI; X-ray; 3.90 A; A/B/C=1-417.
DR PDB; 6CTF; X-ray; 4.05 A; A/B/C=6-416.
DR PDB; 6UWF; EM; 3.08 A; A=1-419.
DR PDB; 6UWL; EM; 3.62 A; A=1-419.
DR PDB; 6V8G; X-ray; 3.38 A; A/B/C=1-419.
DR PDB; 6WYJ; EM; 3.70 A; A=1-417.
DR PDB; 6WYK; EM; 4.00 A; A=1-417.
DR PDB; 6WYL; EM; 3.90 A; A/B/C=1-417.
DR PDB; 6WZB; X-ray; 3.45 A; A/B/C=1-417.
DR PDB; 6X01; X-ray; 3.65 A; A/B/C=1-417.
DR PDB; 6X12; EM; 3.52 A; A=1-419.
DR PDB; 6X13; EM; 3.66 A; A=1-419.
DR PDB; 6X14; EM; 3.71 A; A/B/C=1-419.
DR PDB; 6X15; EM; 3.05 A; A/B/C=1-419.
DR PDB; 6X16; EM; 3.39 A; A/B/C=1-419.
DR PDB; 6X17; EM; 3.66 A; A/B/C=1-419.
DR PDB; 7AHK; X-ray; 2.50 A; A=1-417.
DR PDBsum; 1XFH; -.
DR PDBsum; 2NWL; -.
DR PDBsum; 2NWW; -.
DR PDBsum; 2NWX; -.
DR PDBsum; 3KBC; -.
DR PDBsum; 3V8F; -.
DR PDBsum; 3V8G; -.
DR PDBsum; 4IZM; -.
DR PDBsum; 4OYE; -.
DR PDBsum; 4OYF; -.
DR PDBsum; 4P19; -.
DR PDBsum; 4P1A; -.
DR PDBsum; 4P3J; -.
DR PDBsum; 4P6H; -.
DR PDBsum; 4X2S; -.
DR PDBsum; 5CFY; -.
DR PDBsum; 6BAT; -.
DR PDBsum; 6BAU; -.
DR PDBsum; 6BAV; -.
DR PDBsum; 6BMI; -.
DR PDBsum; 6CTF; -.
DR PDBsum; 6UWF; -.
DR PDBsum; 6UWL; -.
DR PDBsum; 6V8G; -.
DR PDBsum; 6WYJ; -.
DR PDBsum; 6WYK; -.
DR PDBsum; 6WYL; -.
DR PDBsum; 6WZB; -.
DR PDBsum; 6X01; -.
DR PDBsum; 6X12; -.
DR PDBsum; 6X13; -.
DR PDBsum; 6X14; -.
DR PDBsum; 6X15; -.
DR PDBsum; 6X16; -.
DR PDBsum; 6X17; -.
DR PDBsum; 7AHK; -.
DR AlphaFoldDB; O59010; -.
DR SMR; O59010; -.
DR DIP; DIP-59313N; -.
DR STRING; 70601.3257716; -.
DR BindingDB; O59010; -.
DR ChEMBL; CHEMBL4296295; -.
DR TCDB; 2.A.23.1.5; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR EnsemblBacteria; BAA30399; BAA30399; BAA30399.
DR GeneID; 1443616; -.
DR KEGG; pho:PH1295; -.
DR eggNOG; arCOG04335; Archaea.
DR OMA; YLYIAVI; -.
DR EvolutionaryTrace; O59010; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Chloride; Membrane;
KW Metal-binding; Sodium; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..425
FT /note="Glutamate transporter homolog"
FT /id="PRO_0000440893"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 12..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 31..41
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 63..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 81..103
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 104..121
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 122..160
FT /note="Discontinuously helical; Name=4"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 161..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 197..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 219..230
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 252..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT INTRAMEM 261..289
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 290..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 298..320
FT /note="Discontinuously helical; Name=7"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 321..337
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15483603"
FT INTRAMEM 338..372
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 373..391
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TRANSMEM 392..412
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:15483603"
FT TOPO_DOM 413..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15483603"
FT BINDING 276..278
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:17230192,
FT ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX,
FT ECO:0007744|PDB:3KBC"
FT BINDING 306
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX"
FT BINDING 308
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX"
FT BINDING 310
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX, ECO:0007744|PDB:4X2S"
FT BINDING 314
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:17230192,
FT ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX,
FT ECO:0007744|PDB:3KBC"
FT BINDING 352
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX"
FT BINDING 355
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:17230192,
FT ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX,
FT ECO:0007744|PDB:3KBC"
FT BINDING 394
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:17230192,
FT ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX,
FT ECO:0007744|PDB:3KBC"
FT BINDING 401
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:17230192,
FT ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX,
FT ECO:0007744|PDB:3KBC"
FT BINDING 401
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX"
FT BINDING 405
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:17230192,
FT ECO:0007744|PDB:2NWX"
FT MUTAGEN 65
FT /note="S->V: Strongly decreased chloride conductance."
FT /evidence="ECO:0000269|PubMed:17435767"
FT MUTAGEN 276
FT /note="R->S: Increased rate of aspartate transport; when
FT associated with R-395."
FT /evidence="ECO:0000269|Ref.11"
FT MUTAGEN 311
FT /note="M->A: Decreased dependence of aspartate binding on
FT Na(+) concentration."
FT /evidence="ECO:0000269|PubMed:24842876"
FT MUTAGEN 395
FT /note="M->R: Increased rate of aspartate transport; when
FT associated with S-276."
FT /evidence="ECO:0000269|Ref.11"
FT MUTAGEN 397
FT /note="R->A: Strongly decreased affinity for aspartate."
FT /evidence="ECO:0000269|PubMed:24842876"
FT MUTAGEN 405
FT /note="D->N: Strongly decreased affinity for aspartate."
FT /evidence="ECO:0000269|PubMed:17230192"
FT HELIX 2..8
FT /evidence="ECO:0007829|PDB:6X15"
FT HELIX 13..32
FT /evidence="ECO:0007829|PDB:7AHK"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2NWL"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 75..107
FT /evidence="ECO:0007829|PDB:7AHK"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:7AHK"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4P19"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 174..201
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6V8G"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 227..245
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 312..329
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:7AHK"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:7AHK"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:7AHK"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6UWF"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:7AHK"
FT HELIX 390..415
FT /evidence="ECO:0007829|PDB:7AHK"
SQ 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
