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Protein

Excitatory amino acid transporter 3

Gene

Slc1a1

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:9011753, PubMed:11242046). Can also transport L-cysteine. 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. Mediates Cl- flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na+ symport. Plays an important role in L-glutamate and L-aspartate reabsorption in renal tubuli (By similarity). 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). Negatively regulated by ARL6IP5 (PubMed:11242046).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi361Sodium 1; via carbonyl oxygenBy similarity1
Metal bindingi363Sodium 2; via carbonyl oxygenBy similarity1
Metal bindingi365Sodium 1By similarity1
Binding sitei369AspartateBy similarity1
Binding sitei443AspartateBy similarity1
Metal bindingi450Sodium 1; via carbonyl oxygenBy similarity1
Binding sitei450AspartateBy similarity1
Metal bindingi454Sodium 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-RNO-210500. Glutamate Neurotransmitter Release Cycle.
R-RNO-425393. Transport of inorganic cations/anions and amino acids/oligopeptides.

Names & Taxonomyi

Protein namesi
Recommended name:
Excitatory amino acid transporter 3
Alternative name(s):
Excitatory amino-acid carrier 12 Publications
Sodium-dependent glutamate/aspartate transporter 3
Solute carrier family 1 member 1
Gene namesi
Name:Slc1a1
Synonyms:Eaac12 Publications, Eaat3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3696. Slc1a1.

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 – 18CytoplasmicCuratedAdd BLAST18
Transmembranei19 – 38HelicalSequence analysisAdd BLAST20
Topological domaini39 – 61ExtracellularCuratedAdd BLAST23
Transmembranei62 – 82HelicalSequence analysisAdd BLAST21
Topological domaini83 – 93CytoplasmicCuratedAdd BLAST11
Transmembranei94 – 114HelicalSequence analysisAdd BLAST21
Topological domaini115 – 204ExtracellularCuratedAdd BLAST90
Transmembranei205 – 228Helical; Name=4By similarityAdd BLAST24
Topological domaini229 – 237CytoplasmicCurated9
Transmembranei238 – 265Helical; Name=5By similarityAdd BLAST28
Topological domaini266 – 285ExtracellularCuratedAdd BLAST20
Transmembranei286 – 307Helical; Name=6By similarityAdd BLAST22
Topological domaini308 – 312CytoplasmicCurated5
Intramembranei313 – 343Discontinuously helicalBy similarityAdd BLAST31
Topological domaini344 – 352CytoplasmicCurated9
Transmembranei353 – 379Helical; Name=7By similarityAdd BLAST27
Topological domaini380 – 392ExtracellularCuratedAdd BLAST13
Intramembranei393 – 426Discontinuously helicalBy similarityAdd BLAST34
Topological domaini427 – 439ExtracellularCuratedAdd BLAST13
Transmembranei440 – 461Helical; Name=8By similarityAdd BLAST22
Topological domaini462 – 523CytoplasmicCuratedAdd BLAST62

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3113.
GuidetoPHARMACOLOGYi870.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002020671 – 523Excitatory amino acid transporter 3Add BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi128N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi178N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi194N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei516PhosphoserineBy similarity1
Modified residuei521PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP51907.
PRIDEiP51907.

PTM databases

iPTMnetiP51907.
PhosphoSitePlusiP51907.
SwissPalmiP51907.

Expressioni

Tissue specificityi

Expressed to a high extent in brain and kidney, and to a lower extent in heart, lung and skeletal muscle.2 Publications

Gene expression databases

BgeeiENSRNOG00000014816.
GenevisibleiP51907. RN.

Interactioni

Subunit structurei

Homotrimer (Probable). Interacts with ARL6IP5/PRAF3 (PubMed:11242046).Curated1 Publication

Protein-protein interaction databases

MINTiMINT-2839476.
STRINGi10116.ENSRNOP00000020272.

Chemistry databases

BindingDBiP51907.

Structurei

3D structure databases

ProteinModelPortaliP51907.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni330 – 332Aspartate bindingBy similarity3
Regioni410 – 414Aspartate 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.
GeneTreeiENSGT00760000119117.
HOGENOMiHOG000208776.
HOVERGENiHBG000080.
InParanoidiP51907.
KOiK05612.
OMAiYLYIAVI.
OrthoDBiEOG091G0UCE.
PhylomeDBiP51907.
TreeFamiTF315206.

Family and domain databases

Gene3Di1.10.3860.10. 1 hit.
InterProiView protein in InterPro
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.

P51907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKPTSSGCD WRRFLRNHWL LLSTVAAVVL GIVVGVLVRG HSELSNLDKF
60 70 80 90 100
YFAFPGEILM RMLKLVILPL IISSMITGVA ALDSNVSGKI GLRAVVYYFS
110 120 130 140 150
TTVIAVILGI VLVVSIKPGV TQKVNEINRT GKTPEVSTVD AMLDLIRNMF
160 170 180 190 200
PENLVQACFQ QYKTKREEVK PASDPGGNQT EVSVTTAMTT MSENKTKEYK
210 220 230 240 250
IVGLYSDGIN VLGLIIFCLV FGLVIGKMGE KGQILVDFFN ALSDATMKIV
260 270 280 290 300
QIIMCYMPIG ILFLIAGKII EVEDWEIFRK LGLYMATVLS GLAIHSLVVL
310 320 330 340 350
PLIYFIVVRK NPFRFALGMA QALLTALMIS SSSATLPVTF RCAEEKNHVD
360 370 380 390 400
KRITRFVLPV GATINMDGTA LYEAVAAVFI AQLNGMDLSI GQIITISITA
410 420 430 440 450
TAASIGAAGV PQAGLVTMVI VLSAVGLPAE DVTLIIAVDW LLDRFRTMVN
460 470 480 490 500
VLGDAFGTGI VEKLSKKELE QVDVSSEVNI VNPFALEPTI LDNEDSDTKK
510 520
SYVNGGFSVD KSDTISFTQT SQF
Length:523
Mass (Da):56,772
Last modified:October 1, 1996 - v1
Checksum:iD6783244E37640E4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68L → M in BAA09849 (PubMed:8613726).Curated1
Sequence conflicti93R → C in BAA09849 (PubMed:8613726).Curated1
Sequence conflicti149 – 151MFP → ILG in AAB09773 (PubMed:8747153).Curated3
Sequence conflicti156Q → E in AAB51161 (PubMed:8738164).Curated1
Sequence conflicti203G → C in AAB51161 (PubMed:8738164).Curated1
Sequence conflicti218C → F in AAB51161 (PubMed:8738164).Curated1
Sequence conflicti279R → C in AAC25030 (Ref. 7) Curated1
Sequence conflicti309R → T in AAB51161 (PubMed:8738164).Curated1
Sequence conflicti383L → V in BAA09849 (PubMed:8613726).Curated1
Sequence conflicti424A → P in AAF34319 (PubMed:8772431).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94255 mRNA. Translation: CAA63937.1.
U39555 mRNA. Translation: AAB09773.1.
D63772 mRNA. Translation: BAA09849.1.
L35558 mRNA. Translation: AAB51161.1.
BC061743 mRNA. Translation: AAH61743.1.
U21104 mRNA. Translation: AAF34319.1.
AF038571 mRNA. Translation: AAC25030.1.
RefSeqiNP_037164.3. NM_013032.3.
UniGeneiRn.6384.

Genome annotation databases

EnsembliENSRNOT00000020272; ENSRNOP00000020272; ENSRNOG00000014816.
GeneIDi25550.
KEGGirno:25550.
UCSCiRGD:3696. rat.

Similar proteinsi

Entry informationi

Entry nameiEAA3_RAT
AccessioniPrimary (citable) accession number: P51907
Secondary accession number(s): O88389, Q63727, Q9JJP8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: August 30, 2017
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families