P31596 · EAA2_RAT
- ProteinExcitatory amino acid transporter 2
- GeneSlc1a2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids573 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
Catalytic activity
- H+(out) + K+(in) + L-glutamate(out) + 3 Na+(out) = H+(in) + K+(out) + L-glutamate(in) + 3 Na+(in)H+ (out)CHEBI:15378
+ K+ (in)CHEBI:29103+ L-glutamate (out)CHEBI:29985+ 3 Na+ (out)CHEBI:29101= H+ (in)CHEBI:15378+ K+ (out)CHEBI:29103+ L-glutamate (in)CHEBI:29985+ 3 Na+ (in)CHEBI:29101 - D-aspartate(out) + H+(out) + K+(in) + 3 Na+(out) = D-aspartate(in) + H+(in) + K+(out) + 3 Na+(in)
- H+(out) + K+(in) + L-aspartate(out) + 3 Na+(out) = H+(in) + K+(out) + L-aspartate(in) + 3 Na+(in)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 361-363 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: ASS | ||||||
Binding site | 392 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 394 | Na+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 396 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 400 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 441-445 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: IPSAG | ||||||
Binding site | 474 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 481 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 481 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 485 | Na+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameExcitatory amino acid transporter 2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP31596
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-44 | Cytoplasmic | ||||
Sequence: MASTEGANNMPKQVEVRMHDSHLSSEEPKHRNLGMRMCDKLGKN | ||||||
Transmembrane | 45-64 | Helical | ||||
Sequence: LLLSLTVFGVILGAVCGGLL | ||||||
Transmembrane | 88-108 | Helical | ||||
Sequence: MLKMLILPLIISSLITGLSGL | ||||||
Transmembrane | 121-142 | Helical | ||||
Sequence: MVYYMSTTIIAAVLGVILVLAI | ||||||
Transmembrane | 235-258 | Helical; Name=4 | ||||
Sequence: FKDGMNVLGLIGFFIAFGIAMGKM | ||||||
Transmembrane | 268-295 | Helical; Name=5 | ||||
Sequence: FFNILNEIVMKLVIMIMWYSPLGIACLI | ||||||
Transmembrane | 317-338 | Helical; Name=6 | ||||
Sequence: ITVIVGLIIHGGIFLPLIYFVV | ||||||
Intramembrane | 344-374 | Discontinuously helical | ||||
Sequence: FSFFAGIFQAWITALGTASSAGTLPVTFRCL | ||||||
Transmembrane | 384-410 | Helical; Name=7 | ||||
Sequence: VTRFVLPVGATINMDGTALYEAVAAIF | ||||||
Intramembrane | 424-457 | Discontinuously helical | ||||
Sequence: IVTVSLTATLASIGAASIPSAGLVTMLLILTAVG | ||||||
Transmembrane | 471-492 | Helical; Name=8 | ||||
Sequence: WLLDRMRTSVNVVGDSFGAGIV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 298 | Normal transporter activity. | ||||
Sequence: K → H or R | ||||||
Mutagenesis | 298 | Reduced transporter activity. | ||||
Sequence: K → N or T | ||||||
Mutagenesis | 326 | No transporter activity. | ||||
Sequence: H → N, T, K, or R |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, lipidation, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000202063 | 1-573 | Excitatory amino acid transporter 2 | |||
Sequence: MASTEGANNMPKQVEVRMHDSHLSSEEPKHRNLGMRMCDKLGKNLLLSLTVFGVILGAVCGGLLRLAAPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPSEEANTTKAVISLLNETMNEAPEETKIVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGEQAKLMVEFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMITVIVGLIIHGGIFLPLIYFVVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEDNLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVILDGGQIVTVSLTATLASIGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRMHEDIEMTKTQSVYDDTKNHRESNSNQCVYAAHNSVVIDECKVTLAANGKSADCSVEEEPWKREK | ||||||
Modified residue | 3 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 24 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 25 | Phosphoserine | ||||
Sequence: S | ||||||
Lipidation | 38 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Glycosylation | 205 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 215 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 505 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 520 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 531 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 533 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 538 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 543 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 559 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 563 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Glycosylated.
Palmitoylation at Cys-38 is not required for correct subcellular localization, but is important for glutamate uptake activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Localized in brain and is highly enriched in the Purkinje cell layer in cerebellum.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MASTEGANNMPKQVEVRMHDSHLSSEEPK | ||||||
Compositional bias | 15-29 | Basic and acidic residues | ||||
Sequence: EVRMHDSHLSSEEPK |
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.
Sequence similarities
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. SLC1A2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P31596-1
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.
- NameGlt1
- Length573
- Mass (Da)62,106
- Last updated1993-10-01 v2
- Checksum8C51D30954E00E7F
P31596-2
- NameGlt-1A
- Differences from canonical
- 1-6: MASTEG → MVS
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AJ89 | A0A8I6AJ89_RAT | Slc1a2 | 567 | ||
A0A8I6AL04 | A0A8I6AL04_RAT | Slc1a2 | 562 | ||
A0A8I6B5J7 | A0A8I6B5J7_RAT | Slc1a2 | 579 | ||
A0A8I6AS41 | A0A8I6AS41_RAT | Slc1a2 | 567 | ||
A0A8I6GKB5 | A0A8I6GKB5_RAT | Slc1a2 | 559 | ||
A0A8I6GIX2 | A0A8I6GIX2_RAT | Slc1a2 | 568 | ||
G3V6R0 | G3V6R0_RAT | Slc1a2 | 577 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006266 | 1-6 | in isoform Glt-1A | |||
Sequence: MASTEG → MVS | ||||||
Compositional bias | 15-29 | Basic and acidic residues | ||||
Sequence: EVRMHDSHLSSEEPK | ||||||
Sequence conflict | 521 | in Ref. 4; AAA93061/AAA93062 | ||||
Sequence: V → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X67857 EMBL· GenBank· DDBJ | CAA48042.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
U15098 EMBL· GenBank· DDBJ | AAA93061.1 EMBL· GenBank· DDBJ | mRNA | ||
U15098 EMBL· GenBank· DDBJ | AAA93062.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF297648 EMBL· GenBank· DDBJ | AAG13411.1 EMBL· GenBank· DDBJ | mRNA |