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Protein

Excitatory amino acid transporter 3

Gene

SLC1A1

Organism
Oryctolagus cuniculus (Rabbit)
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:1280334). Can also transport L-cysteine (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:1280334). 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 (By similarity).By similarity1 Publication

Miscellaneous

Transport does not depend on chloride.1 Publication

Kineticsi

  1. KM=12 µM for L-glutamate1 Publication
  2. KM=6.5 µM for L-aspartate1 Publication
  3. KM=7.5 µM for D-aspartate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi362Sodium 1; via carbonyl oxygenBy similarity1
    Metal bindingi364Sodium 2; via carbonyl oxygenBy similarity1
    Metal bindingi366Sodium 1By similarity1
    Binding sitei370AspartateBy similarity1
    Binding sitei444AspartateBy similarity1
    Metal bindingi451Sodium 1; via carbonyl oxygenBy similarity1
    Binding sitei451AspartateBy similarity1
    Metal bindingi455Sodium 1By similarity1

    GO - Molecular functioni

    GO - Biological processi

    • chloride transmembrane transport Source: UniProtKB
    • cysteine transport Source: UniProtKB
    • D-aspartate import Source: CACAO
    • D-aspartate import across plasma membrane Source: UniProtKB
    • L-aspartate import across plasma membrane Source: UniProtKB
    • L-glutamate import across plasma membrane Source: UniProtKB
    • L-glutamate transmembrane transport Source: UniProtKB

    Keywordsi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Excitatory amino acid transporter 3
    Alternative name(s):
    Excitatory amino-acid carrier 11 Publication
    Sodium-dependent glutamate/aspartate transporter 3
    Solute carrier family 1 member 1
    Gene namesi
    Name:SLC1A1
    Synonyms:EAAC11 Publication, EAAT3
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    Proteomesi
    • UP000001811 Componenti: Unplaced

    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 – 205ExtracellularCuratedAdd BLAST91
    Transmembranei206 – 229Helical; Name=4By similarityAdd BLAST24
    Topological domaini230 – 238CytoplasmicCurated9
    Transmembranei239 – 266Helical; Name=5By similarityAdd BLAST28
    Topological domaini267 – 286ExtracellularCuratedAdd BLAST20
    Transmembranei287 – 308Helical; Name=6By similarityAdd BLAST22
    Topological domaini309 – 313CytoplasmicCurated5
    Intramembranei314 – 344Discontinuously helicalBy similarityAdd BLAST31
    Topological domaini345 – 353CytoplasmicCurated9
    Transmembranei354 – 380Helical; Name=7By similarityAdd BLAST27
    Topological domaini381 – 393ExtracellularCuratedAdd BLAST13
    Intramembranei394 – 427Discontinuously helicalBy similarityAdd BLAST34
    Topological domaini428 – 440ExtracellularCuratedAdd BLAST13
    Transmembranei441 – 462Helical; Name=8By similarityAdd BLAST22
    Topological domaini463 – 524CytoplasmicCuratedAdd BLAST62

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002020681 – 524Excitatory amino acid transporter 3Add BLAST524

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi43N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi178N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi195N-linked (GlcNAc...) asparagineSequence analysis1
    Modified residuei517PhosphoserineBy similarity1
    Modified residuei522PhosphoserineBy similarity1

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Expressioni

    Tissue specificityi

    Brain, but also small intestine, kidney, liver and heart.1 Publication

    Interactioni

    Subunit structurei

    Homotrimer (Probable). Interacts with ARL6IP5 (By similarity).By similarityCurated

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000022489.

    Structurei

    3D structure databases

    ProteinModelPortaliP31597.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni331 – 333Aspartate bindingBy similarity3
    Regioni411 – 415Aspartate 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.
    InParanoidiP31597.
    KOiK05612.

    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.

    P31597-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGKPARKGCD SKRFLKNNWL LLSTVVAVVL GIVIGVLVRE YSNLSTLDKF
    60 70 80 90 100
    YFAFPGEILM RMLKLVILPL IVSSMITGVA ALDSNVSGKI GLRAVLYYFC
    110 120 130 140 150
    TTIIAVILGI VLVVSIKPGV TQKVDEIDRT GSTPEVSTVD AMLDLIRNMF
    160 170 180 190 200
    PENLVQACFQ QYKTTREEVT ASDDTGKNGT EESVTAVMTT AVSENRTKEY
    210 220 230 240 250
    RVVGLYSDGI NVLGLIVFCL VFGLVIGKMG EKGQILVDFF NALSDATMKI
    260 270 280 290 300
    VQIIMCYMPL GILFLIAGKI IEVEDWEIFR KLGLYMVTVL SGLAIHSIVI
    310 320 330 340 350
    LPLIYFIVVR KNPFRFAMGM TQALLTALMI SSSSATLPVT FRCAEEKNRV
    360 370 380 390 400
    DKRITRFVLP VGATINMDGT ALYEAVAAVF IAQLNDMDLS IGQIITISVT
    410 420 430 440 450
    ATAASIGAAG VPQAGLVTMV IVLSAVGLPA EDVTLIIAVD WLLDRFRTVV
    460 470 480 490 500
    NVLGDAFGTG IVEKLSKKEL EQMDVSSEVN IVNPFALESA TLDNEDSDTK
    510 520
    KSYINGGFAV DKSDTISFTQ TSQF
    Length:524
    Mass (Da):56,939
    Last modified:July 1, 1993 - v1
    Checksum:iF4F483777EFE62D5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12411 mRNA. Translation: AAA31257.1.
    PIRiS28902.
    RefSeqiNP_001075718.1. NM_001082249.1.
    UniGeneiOcu.1980.

    Genome annotation databases

    GeneIDi100009070.
    KEGGiocu:100009070.

    Similar proteinsi

    Entry informationi

    Entry nameiEAA3_RABIT
    AccessioniPrimary (citable) accession number: P31597
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 25, 2017
    This is version 94 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