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Protein

Excitatory amino acid transporter 2

Gene

Slc1a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:1448170, PubMed:7913472). 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:1448170). 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 (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi392Sodium 1; via carbonyl oxygenBy similarity1
Metal bindingi394Sodium 2; via carbonyl oxygenBy similarity1
Metal bindingi396Sodium 1By similarity1
Binding sitei400AspartateBy similarity1
Binding sitei474AspartateBy similarity1
Metal bindingi481Sodium 1; via carbonyl oxygenBy similarity1
Binding sitei481AspartateBy similarity1
Metal bindingi485Sodium 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processAmino-acid transport, Symport, Transport
LigandChloride, Metal-binding, Potassium, Sodium

Protein family/group databases

TCDBi2.A.23.2.2. the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Excitatory amino acid transporter 2
Alternative name(s):
GLT-12 Publications
Sodium-dependent glutamate/aspartate transporter 2
Short name:
GLUT-R
Solute carrier family 1 member 2
Gene namesi
Name:Slc1a2
Synonyms:Eaat2, Glt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3697. Slc1a2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 44CytoplasmicSequence analysisAdd BLAST44
Transmembranei45 – 64HelicalSequence analysisAdd BLAST20
Transmembranei88 – 108HelicalSequence analysisAdd BLAST21
Transmembranei121 – 142HelicalSequence analysisAdd BLAST22
Transmembranei235 – 258Helical; Name=4By similarityAdd BLAST24
Transmembranei268 – 295Helical; Name=5By similarityAdd BLAST28
Transmembranei317 – 338Helical; Name=6By similarityAdd BLAST22
Intramembranei344 – 374Discontinuously helicalBy similarityAdd BLAST31
Transmembranei384 – 410Helical; Name=7By similarityAdd BLAST27
Intramembranei424 – 457Discontinuously helicalBy similarityAdd BLAST34
Transmembranei471 – 492Helical; Name=8By similarityAdd BLAST22

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi298K → H or R: Normal transporter activity. 1 Publication1
Mutagenesisi298K → N or T: Reduced transporter activity. 1 Publication1
Mutagenesisi326H → N, T, K or R: No transporter activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2900.
GuidetoPHARMACOLOGYi869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002020631 – 573Excitatory amino acid transporter 2Add BLAST573

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Lipidationi38S-palmitoyl cysteineBy similarity1
Glycosylationi205N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi215N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei505PhosphoserineCombined sources1
Modified residuei520PhosphoserineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei533PhosphoserineBy similarity1
Modified residuei538PhosphotyrosineBy similarity1
Modified residuei543PhosphoserineBy similarity1
Modified residuei559PhosphoserineBy similarity1
Modified residuei563PhosphoserineBy similarity1

Post-translational modificationi

Glycosylated.By similarity
Palmitoylation at Cys-38 is not required for correct subcellular localization, but is important for glutamate uptake activity.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP31596.
PRIDEiP31596.

PTM databases

iPTMnetiP31596.
PhosphoSitePlusiP31596.
SwissPalmiP31596.
UniCarbKBiP31596.

Expressioni

Tissue specificityi

Localized in brain and is highly enriched in the Purkinje cell layer in cerebellum.1 Publication

Interactioni

Subunit structurei

Homotrimer (By similarity). Interacts with AJUBA (PubMed:11860269).By similarity1 Publication

Protein-protein interaction databases

BioGridi248124. 2 interactors.
IntActiP31596. 1 interactor.
STRINGi10116.ENSRNOP00000007604.

Structurei

3D structure databases

ProteinModelPortaliP31596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni361 – 363Aspartate bindingBy similarity3
Regioni441 – 445Aspartate bindingBy similarity5

Domaini

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.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3787. Eukaryota.
COG1301. LUCA.
HOGENOMiHOG000208776.
HOVERGENiHBG000080.
InParanoidiP31596.
KOiK05613.
PhylomeDBiP31596.
TreeFamiTF315206.

Family and domain databases

Gene3Di1.10.3860.10. 1 hit.
InterProiView protein in InterPro
IPR036458. Na-dicarbo_symporter_sf.
IPR001991. Na-dicarboxylate_symporter.
IPR018107. Na-dicarboxylate_symporter_CS.
PfamiView protein in Pfam
PF00375. SDF. 1 hit.
PRINTSiPR00173. EDTRNSPORT.
SUPFAMiSSF118215. SSF118215. 2 hits.
PROSITEiView protein in PROSITE
PS00713. NA_DICARBOXYL_SYMP_1. 1 hit.
PS00714. NA_DICARBOXYL_SYMP_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Glt1 (identifier: P31596-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASTEGANNM PKQVEVRMHD SHLSSEEPKH RNLGMRMCDK LGKNLLLSLT
60 70 80 90 100
VFGVILGAVC GGLLRLAAPI HPDVVMLIAF PGDILMRMLK MLILPLIISS
110 120 130 140 150
LITGLSGLDA KASGRLGTRA MVYYMSTTII AAVLGVILVL AIHPGNPKLK
160 170 180 190 200
KQLGPGKKND EVSSLDAFLD LIRNLFPENL VQACFQQIQT VTKKVLVAPP
210 220 230 240 250
SEEANTTKAV ISLLNETMNE APEETKIVIK KGLEFKDGMN VLGLIGFFIA
260 270 280 290 300
FGIAMGKMGE QAKLMVEFFN ILNEIVMKLV IMIMWYSPLG IACLICGKII
310 320 330 340 350
AIKDLEVVAR QLGMYMITVI VGLIIHGGIF LPLIYFVVTR KNPFSFFAGI
360 370 380 390 400
FQAWITALGT ASSAGTLPVT FRCLEDNLGI DKRVTRFVLP VGATINMDGT
410 420 430 440 450
ALYEAVAAIF IAQMNGVILD GGQIVTVSLT ATLASIGAAS IPSAGLVTML
460 470 480 490 500
LILTAVGLPT EDISLLVAVD WLLDRMRTSV NVVGDSFGAG IVYHLSKSEL
510 520 530 540 550
DTIDSQHRMH EDIEMTKTQS VYDDTKNHRE SNSNQCVYAA HNSVVIDECK
560 570
VTLAANGKSA DCSVEEEPWK REK
Length:573
Mass (Da):62,106
Last modified:October 1, 1993 - v2
Checksum:i8C51D30954E00E7F
GO
Isoform Glt-1A (identifier: P31596-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MASTEG → MVS

Show »
Length:570
Mass (Da):61,847
Checksum:i8231169B6B0F2F1E
GO

Sequence cautioni

The sequence AAA93062 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti521V → I in AAA93061 (Ref. 3) Curated1
Sequence conflicti521V → I in AAA93062 (Ref. 3) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0062661 – 6MASTEG → MVS in isoform Glt-1A. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67857 mRNA. Translation: CAA48042.1. Sequence problems.
U15098 mRNA. Translation: AAA93061.1.
U15098 mRNA. Translation: AAA93062.1. Different initiation.
AF297648 mRNA. Translation: AAG13411.1.
PIRiS28901.
RefSeqiNP_001289018.1. NM_001302089.1.
NP_058911.2. NM_017215.2.
UniGeneiRn.10240.

Genome annotation databases

GeneIDi29482.
KEGGirno:29482.
UCSCiRGD:3697. rat. [P31596-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiEAA2_RAT
AccessioniPrimary (citable) accession number: P31596
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1993
Last modified: November 22, 2017
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families