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Protein

Excitatory amino acid transporter 1

Gene

SLC1A3

Organism
Ambystoma tigrinum (Eastern tiger salamander)
Status
Reviewed-Annotation score: Annotation score: 4 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:9425012, PubMed:17008380). 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:17008380). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi395Sodium 1; via carbonyl oxygenBy similarity1
Metal bindingi397Sodium 2; via carbonyl oxygenBy similarity1
Metal bindingi399Sodium 1By similarity1
Binding sitei403AspartateBy similarity1
Binding sitei477AspartateBy similarity1
Metal bindingi484Sodium 1; via carbonyl oxygenBy similarity1
Binding sitei484AspartateBy similarity1
Metal bindingi488Sodium 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processAmino-acid transport, Symport, Transport
LigandMetal-binding, Potassium, Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Excitatory amino acid transporter 11 Publication
Alternative name(s):
SEAAT11 Publication
Sodium-dependent glutamate/aspartate transporter1 Publication
Short name:
GLAST1 Publication
Gene namesi
Name:SLC1A3
Synonyms:EAAT1
OrganismiAmbystoma tigrinum (Eastern tiger salamander)
Taxonomic identifieri8305 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaCaudataSalamandroideaAmbystomatidaeAmbystoma

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 – 47CytoplasmicBy similarityAdd BLAST47
Transmembranei48 – 68Helical; Name=1By similarityAdd BLAST21
Topological domaini69 – 86ExtracellularBy similarityAdd BLAST18
Transmembranei87 – 108Helical; Name=2By similarityAdd BLAST22
Topological domaini109 – 122CytoplasmicBy similarityAdd BLAST14
Transmembranei123 – 145Helical; Name=3By similarityAdd BLAST23
Topological domaini146 – 237ExtracellularBy similarityAdd BLAST92
Transmembranei238 – 261Helical; Name=4By similarityAdd BLAST24
Topological domaini262 – 270CytoplasmicBy similarity9
Transmembranei271 – 298Helical; Name=5By similarityAdd BLAST28
Topological domaini299 – 319ExtracellularBy similarityAdd BLAST21
Transmembranei320 – 341Helical; Name=6By similarityAdd BLAST22
Topological domaini342 – 346CytoplasmicBy similarity5
Intramembranei347 – 377Discontinuously helicalBy similarityAdd BLAST31
Topological domaini378 – 386CytoplasmicBy similarity9
Transmembranei387 – 413Helical; Name=7By similarityAdd BLAST27
Topological domaini414 – 426ExtracellularBy similarityAdd BLAST13
Intramembranei427 – 460Discontinuously helicalBy similarityAdd BLAST34
Topological domaini461 – 473ExtracellularBy similarityAdd BLAST13
Transmembranei474 – 495Helical; Name=8By similarityAdd BLAST22
Topological domaini496 – 543CytoplasmicBy similarityAdd BLAST48

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002020601 – 543Excitatory amino acid transporter 1Add BLAST543

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi206N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi217N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Detected in retina (at protein level).1 Publication

Interactioni

Subunit structurei

Homotrimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO57321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 366Aspartate bindingBy similarity3
Regioni444 – 448Aspartate 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, regions involved in trimerization do not move.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000080.

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.

Sequencei

Sequence statusi: Complete.

O57321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKSNGEDPR AGSRMERFQQ GVRQRTLLAK KKVQNITKDD VKGFLKRNGF
60 70 80 90 100
VLFTVIAVVV GSILGFSVRS YHMTFRELKY FSFPGELLMR MLQMLVLPLI
110 120 130 140 150
VSSLVTGMAA LDSKASGKMG LRAVVYYMTT TVIAVFIGIV IVIIVHPGKG
160 170 180 190 200
TKEHMHREGK IEPVTAADAF LDLIRNMFPP NMVEACFKQF KTSYEKKIFK
210 220 230 240 250
VTMPANETAV MTSVLNNVSE AMETLTKMRE EMIPVPGAVN GVNALGLVVF
260 270 280 290 300
SMCFGLVIGN MKEQGKALKD FFDSLNEAIM RLVAVIMWYA PIGILFLIAG
310 320 330 340 350
KIAEMEDMGV VGGQLGMYTV TVIIGLLIHA VIVLPLLYFA VTRKNPWVFI
360 370 380 390 400
GGILQALITA LGTSSSSATL PITFKCLEEN NKVDKRVTRF VLPVGATINM
410 420 430 440 450
DGTALYEALA AIFIAQVNNY DLNFGQILTI SITATAASIG AAGIPQAGLV
460 470 480 490 500
TMVIVLTSVG LPTDDITLII AVDWFLDRLR TTTNVLGDSL GAGIVEHLSR
510 520 530 540
HELQSGDAEM GNSVIEENEM KKPYQLVSQE NELEKPIDSE TKM
Length:543
Mass (Da):59,395
Last modified:June 1, 1998 - v1
Checksum:i6B495796FE581FFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018256 mRNA. Translation: AAB88286.1.

Similar proteinsi

Entry informationi

Entry nameiEAA1_AMBTI
AccessioniPrimary (citable) accession number: O57321
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: October 25, 2017
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families