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P19491

- GRIA2_RAT

UniProt

P19491 - GRIA2_RAT

Protein

Glutamate receptor 2

Gene

Gria2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.14 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei471 – 4711Glutamate1 Publication
    Binding sitei506 – 5061Glutamate1 Publication
    Binding sitei726 – 7261Glutamate1 Publication

    GO - Molecular functioni

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
    2. extracellular-glutamate-gated ion channel activity Source: RefGenome
    3. identical protein binding Source: IntAct
    4. ionotropic glutamate receptor activity Source: UniProtKB
    5. kainate selective glutamate receptor activity Source: UniProtKB
    6. PDZ domain binding Source: UniProtKB
    7. protein binding Source: IntAct
    8. protein kinase binding Source: RGD
    9. receptor activity Source: UniProtKB

    GO - Biological processi

    1. establishment of protein localization Source: UniProtKB
    2. ionotropic glutamate receptor signaling pathway Source: UniProtKB
    3. ion transmembrane transport Source: GOC
    4. positive regulation of synaptic transmission Source: UniProtKB
    5. protein tetramerization Source: UniProtKB
    6. receptor internalization Source: UniProtKB
    7. regulation of receptor recycling Source: UniProtKB
    8. regulation of synaptic transmission, glutamatergic Source: UniProtKB
    9. response to fungicide Source: RGD
    10. response to lithium ion Source: UniProtKB
    11. synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor 2
    Short name:
    GluR-2
    Alternative name(s):
    AMPA-selective glutamate receptor 2
    GluR-B
    GluR-K2
    Glutamate receptor ionotropic, AMPA 2
    Short name:
    GluA2
    Gene namesi
    Name:Gria2
    Synonyms:Glur2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61862. Gria2.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
    2. asymmetric synapse Source: RGD
    3. cell junction Source: UniProtKB-KW
    4. cell surface Source: RGD
    5. dendrite Source: RGD
    6. dendrite cytoplasm Source: RGD
    7. dendritic shaft Source: UniProtKB
    8. dendritic spine Source: UniProtKB
    9. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    10. growth cone Source: RGD
    11. integral component of plasma membrane Source: UniProtKB
    12. ionotropic glutamate receptor complex Source: UniProtKB
    13. neuronal cell body Source: UniProtKB
    14. perikaryon Source: RGD
    15. postsynaptic density Source: RGD
    16. postsynaptic membrane Source: RefGenome
    17. presynaptic membrane Source: RGD
    18. protein complex Source: UniProtKB
    19. synapse Source: UniProtKB
    20. synaptic vesicle membrane Source: RGD
    21. terminal bouton Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi504 – 5041L → Y: Promotes dimerization. Strongly reduced desensitization. 2 Publications
    Mutagenesisi775 – 7751N → D: Increases rate of desensitization. 2 Publications
    Mutagenesisi851 – 8522NP → AA: Strongly reduces interaction with NSF. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 883862Glutamate receptor 2PRO_0000011535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi78 ↔ 330
    Glycosylationi256 – 2561N-linked (GlcNAc...)1 Publication
    Glycosylationi370 – 3701N-linked (GlcNAc...)2 Publications
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Lipidationi610 – 6101S-palmitoyl cysteineBy similarity
    Modified residuei683 – 6831Phosphoserine; by PKC1 Publication
    Modified residuei717 – 7171Phosphoserine; by PKG1 Publication
    Disulfide bondi739 ↔ 794
    Lipidationi836 – 8361S-palmitoyl cysteineBy similarity
    Modified residuei876 – 8761Phosphotyrosine1 Publication
    Modified residuei880 – 8801PhosphoserineBy similarity

    Post-translational modificationi

    Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP19491.
    PRIDEiP19491.

    PTM databases

    PhosphoSiteiP19491.

    Expressioni

    Tissue specificityi

    Detected in forebrain. Detected in dendrites of neuronal cells.3 Publications

    Developmental stagei

    Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 8 to 14 day old animals. Detected at intermediate levels at day 42 (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP19491.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4 By similarity. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with NSF via its C-terminus. Interacts with CACNG2, PRKCABP and GRIP2. Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ domain) By similarity. Interacts with GRIA1 and SYNDIG1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes By similarity. Interacts with LRFN1. Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself9EBI-77718,EBI-77718
    Agap2Q8CGU44EBI-77718,EBI-4409108
    Atad1Q505J93EBI-77718,EBI-4280289
    Gria1P194903EBI-77718,EBI-371642
    Grip1P9787915EBI-77718,EBI-936113
    Grip2Q9WTW1-37EBI-77718,EBI-936068
    Mapk8P491852EBI-9118256,EBI-7456505
    NsfQ9QUL65EBI-77718,EBI-925794
    Pick1Q9EP8012EBI-77718,EBI-77728
    PPFIA1Q131362EBI-77718,EBI-745426From a different organism.
    Ppfia4Q91Z803EBI-77718,EBI-8276907

    Protein-protein interaction databases

    BioGridi248250. 6 interactions.
    DIPiDIP-30952N.
    IntActiP19491. 20 interactions.
    MINTiMINT-86056.

    Structurei

    Secondary structure

    1
    883
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 349
    Helixi38 – 5013
    Beta strandi57 – 659
    Helixi70 – 8213
    Beta strandi86 – 905
    Turni94 – 963
    Helixi97 – 10711
    Beta strandi110 – 1134
    Beta strandi125 – 1273
    Helixi133 – 14210
    Beta strandi147 – 1526
    Turni154 – 1563
    Helixi159 – 17113
    Beta strandi174 – 1796
    Helixi190 – 20011
    Turni201 – 2033
    Beta strandi206 – 2116
    Helixi213 – 22614
    Helixi230 – 2323
    Beta strandi234 – 2374
    Beta strandi239 – 2413
    Helixi242 – 2443
    Helixi247 – 2493
    Beta strandi251 – 2544
    Beta strandi256 – 2627
    Helixi268 – 27710
    Turni282 – 2843
    Beta strandi289 – 2913
    Helixi295 – 31622
    Helixi339 – 35012
    Beta strandi353 – 3553
    Beta strandi358 – 3603
    Beta strandi366 – 3683
    Beta strandi372 – 3798
    Beta strandi382 – 3909
    Turni391 – 3933
    Beta strandi394 – 3974
    Beta strandi416 – 4205
    Turni424 – 4263
    Beta strandi427 – 4293
    Helixi433 – 4353
    Helixi438 – 4414
    Beta strandi442 – 4443
    Helixi445 – 45713
    Beta strandi461 – 4655
    Beta strandi472 – 4743
    Turni476 – 4783
    Helixi483 – 4897
    Beta strandi494 – 4963
    Helixi504 – 5074
    Beta strandi510 – 5123
    Beta strandi516 – 5194
    Beta strandi521 – 5266
    Beta strandi644 – 6485
    Helixi657 – 6615
    Beta strandi664 – 6696
    Beta strandi671 – 6744
    Helixi675 – 6828
    Helixi686 – 69712
    Beta strandi704 – 7063
    Helixi707 – 71610
    Turni717 – 7193
    Beta strandi721 – 7266
    Helixi727 – 7348
    Beta strandi736 – 7383
    Beta strandi741 – 7455
    Beta strandi751 – 7533
    Beta strandi756 – 7583
    Helixi763 – 77614
    Helixi779 – 78810
    Turni789 – 7913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FTJX-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1FTKX-ray1.60A404-528[»]
    A653-796[»]
    1FTLX-ray1.80A/B413-527[»]
    A/B653-796[»]
    1FTMX-ray1.70A/B/C413-527[»]
    A/B/C653-796[»]
    1FTOX-ray2.00A/B413-527[»]
    A/B653-796[»]
    1FW0X-ray1.90A413-527[»]
    A653-796[»]
    1GR2X-ray1.90A404-528[»]
    A652-796[»]
    1LB8X-ray2.30A/B413-527[»]
    A/B653-796[»]
    1LB9X-ray2.30A/B413-527[»]
    A/B653-796[»]
    1LBBX-ray2.10A413-527[»]
    A653-796[»]
    1LBCX-ray1.80A/B/C413-527[»]
    A/B/C653-796[»]
    1M5BX-ray1.85A/B/C413-527[»]
    A/B/C653-796[»]
    1M5CX-ray1.65A413-527[»]
    A653-796[»]
    1M5DX-ray1.73A413-527[»]
    A653-796[»]
    1M5EX-ray1.46A/B/C413-527[»]
    A/B/C653-796[»]
    1M5FX-ray1.95A/B/C413-527[»]
    A/B/C653-796[»]
    1MM6X-ray2.15A/B413-527[»]
    A/B653-796[»]
    1MM7X-ray1.65A/B/C413-527[»]
    A/B/C653-796[»]
    1MQDX-ray1.46A/B/C/D413-527[»]
    A/B/C/D653-794[»]
    1MQGX-ray2.15A/B413-527[»]
    A/B653-796[»]
    1MQHX-ray1.80A413-527[»]
    A653-796[»]
    1MQIX-ray1.35A413-527[»]
    A653-796[»]
    1MQJX-ray1.65A413-527[»]
    A653-796[»]
    1MS7X-ray1.97A/B/C413-527[»]
    A/B/C653-796[»]
    1MXUX-ray1.80A/B/C413-527[»]
    A/B/C653-796[»]
    1MXVX-ray1.95A/B/C413-527[»]
    A/B/C653-796[»]
    1MXWX-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1MXXX-ray2.00A/B/C413-527[»]
    A/B/C653-796[»]
    1MXYX-ray1.95A/B/C413-527[»]
    A/B/C653-796[»]
    1MXZX-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1MY0X-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1MY1X-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1MY2X-ray1.80A/B/C413-527[»]
    A/B/C653-796[»]
    1MY3X-ray1.75A/B/C413-527[»]
    A/B/C653-796[»]
    1MY4X-ray1.90A/B/C413-527[»]
    A/B/C653-796[»]
    1N0TX-ray2.10A/B/C/D413-527[»]
    A/B/C/D653-796[»]
    1NNKX-ray1.85A413-527[»]
    A653-796[»]
    1NNPX-ray1.90A/B413-527[»]
    A/B653-796[»]
    1P1NX-ray1.60A413-527[»]
    A653-796[»]
    1P1OX-ray1.60A413-527[»]
    A653-796[»]
    1P1QX-ray2.00A/B/C413-527[»]
    A/B/C653-796[»]
    1P1UX-ray2.00A/B413-527[»]
    A/B653-796[»]
    1P1WX-ray1.80A/B413-527[»]
    A/B653-796[»]
    1SYHX-ray1.80A413-527[»]
    A653-796[»]
    1SYIX-ray2.10A/B413-527[»]
    A/B653-796[»]
    1WVJX-ray1.75A413-527[»]
    A653-796[»]
    1XHYX-ray1.85A413-527[»]
    A653-796[»]
    2AIXX-ray2.17A413-527[»]
    A653-796[»]
    2AL4X-ray1.70A/B/C/D/E/F413-527[»]
    A/B/C/D/E/F653-796[»]
    2AL5X-ray1.65A/B413-527[»]
    A/B653-796[»]
    2ANJX-ray2.10A413-527[»]
    A653-796[»]
    2CMOX-ray2.65A/B413-527[»]
    A/B653-796[»]
    2GFEX-ray1.54A/B/C413-527[»]
    A/B/C653-795[»]
    2I3VX-ray2.40A/B/C/D413-527[»]
    A/B/C/D655-794[»]
    2I3WX-ray2.30A/B413-527[»]
    A/B653-794[»]
    2P2AX-ray2.26A/B413-527[»]
    A/B653-796[»]
    2UXAX-ray2.38A/B/C412-795[»]
    2XX7X-ray2.20A/B/C413-527[»]
    A/B/C653-795[»]
    2XX8X-ray1.55A/B/C413-527[»]
    A/B/C653-796[»]
    2XX9X-ray1.97A/B/C413-527[»]
    A/B/C653-796[»]
    2XXHX-ray1.50A/B/C413-527[»]
    A/B/C653-796[»]
    2XXIX-ray1.60A/B/C413-527[»]
    A/B/C653-796[»]
    3B6QX-ray2.00A413-527[»]
    A653-796[»]
    3B6TX-ray2.10A413-527[»]
    A653-796[»]
    3B6WX-ray1.70A/B/C/D413-527[»]
    A/B/C/D653-796[»]
    3B7DX-ray2.50A/B/C/D/E/F/G/H413-527[»]
    A/B/C/D/E/F/G/H653-794[»]
    3BBRX-ray2.25A/B413-527[»]
    A/B653-796[»]
    3BFTX-ray2.27A/B/C413-527[»]
    A/B/C653-796[»]
    3BFUX-ray1.95A/B/C/D413-527[»]
    A/B/C/D653-796[»]
    3BKIX-ray1.87B/C/D/P413-527[»]
    B/C/D/P653-796[»]
    3DP6X-ray1.55A/B/C413-527[»]
    A/B/C653-794[»]
    3H03X-ray1.90A/B/D/G414-527[»]
    A/B/D/G653-794[»]
    3H06X-ray2.80B/E/G/H/J/L/N/P414-527[»]
    B/E/G/H/J/L/N/P653-794[»]
    3H5VX-ray2.33A/B/C21-404[»]
    3H5WX-ray2.69A/B21-404[»]
    3H6TX-ray2.25A/B/C413-527[»]
    A/B/C653-796[»]
    3H6UX-ray1.85A413-527[»]
    A653-796[»]
    3H6VX-ray2.10A/B413-527[»]
    A/B653-796[»]
    3H6WX-ray1.49A/B413-527[»]
    A/B653-796[»]
    3HSYX-ray1.75A/B25-400[»]
    3IJOX-ray2.00B/E/H414-527[»]
    B/E/H653-794[»]
    3IJXX-ray2.88B/D/H414-527[»]
    B/D/H653-794[»]
    3IK6X-ray2.10B/E/H414-527[»]
    B/E/H653-794[»]
    3IL1X-ray2.00B/E/H414-527[»]
    B/E/H653-794[»]
    3ILTX-ray2.11B/E/H414-527[»]
    B/E/H653-794[»]
    3ILUX-ray2.00B/E/H414-527[»]
    B/E/H653-794[»]
    3KG2X-ray3.60A/B/C/D25-412[»]
    A/B/C/D414-847[»]
    3KGCX-ray1.55A/B414-527[»]
    A/B654-795[»]
    3LSFX-ray1.85B/E/H414-527[»]
    B/E/H653-794[»]
    3LSLX-ray2.12A/D/G414-527[»]
    A/D/G653-794[»]
    3M3LX-ray1.85A/D/G414-794[»]
    3N6VX-ray3.20A/B/C/D/E/F27-400[»]
    3O28X-ray2.00A413-527[»]
    A653-795[»]
    3O29X-ray2.02A413-527[»]
    A653-795[»]
    3O2AX-ray1.90A413-527[»]
    A653-795[»]
    3O2JX-ray1.95A/B22-400[»]
    3O6GX-ray1.80A413-527[»]
    A653-795[»]
    3O6HX-ray2.10A413-527[»]
    A653-795[»]
    3O6IX-ray1.80A413-527[»]
    A653-795[»]
    3PD8X-ray2.48A/B/C413-527[»]
    A/B/C653-795[»]
    3PD9X-ray2.10A/B413-527[»]
    A/B653-795[»]
    3PMVX-ray1.80A413-527[»]
    A653-795[»]
    3PMWX-ray2.20A413-527[»]
    A653-795[»]
    3PMXX-ray1.87A413-527[»]
    A653-795[»]
    3RTFX-ray1.70B/D/F414-527[»]
    B/D/F653-794[»]
    3RTWX-ray2.10B/D/F414-527[»]
    B/D/F653-794[»]
    3T93X-ray1.91B/D/F414-527[»]
    B/D/F653-794[»]
    3T96X-ray1.87B/D/F414-527[»]
    B/D/F653-794[»]
    3T9HX-ray2.02B/D/F414-527[»]
    B/D/F653-794[»]
    3T9UX-ray1.97A/B/C414-527[»]
    A/B/C653-794[»]
    3T9VX-ray1.98A/B414-527[»]
    A/B653-794[»]
    3T9XX-ray1.82B/D/F414-527[»]
    B/D/F653-794[»]
    3TDJX-ray1.95A/B413-527[»]
    A/B653-796[»]
    3TKDX-ray1.45A/B413-527[»]
    A/B653-795[»]
    3TZAX-ray1.90A/B413-527[»]
    A/B653-796[»]
    4FATX-ray1.40A413-527[»]
    A653-796[»]
    4G8MX-ray2.05A/B413-527[»]
    A/B653-796[»]
    4GXSX-ray1.96B/D414-527[»]
    B/D653-794[»]
    4H8JX-ray1.80A/B/C/D413-527[»]
    A/B/C/D653-797[»]
    4IGTX-ray1.24A413-527[»]
    A653-796[»]
    4ISUX-ray2.30A/B/C/D413-527[»]
    A/B/C/D653-796[»]
    4IY5X-ray2.00A/B413-527[»]
    A/B653-796[»]
    4IY6X-ray1.72A413-527[»]
    A653-796[»]
    4L17X-ray2.80A/C/E/G413-527[»]
    A/C/E/G653-796[»]
    4LZ5X-ray1.50A/B/C404-527[»]
    A/B/C653-796[»]
    4LZ7X-ray2.10A/B/C404-527[»]
    A/B/C653-796[»]
    4LZ8X-ray1.85A/B/C404-527[»]
    A/B/C653-796[»]
    4N07X-ray1.87A/B/C413-527[»]
    A/B/C653-796[»]
    4O3AX-ray1.80A/B/C413-527[»]
    A/B/C653-796[»]
    4O3BX-ray1.91A/B413-527[»]
    A/B653-796[»]
    4O3CX-ray1.50A413-527[»]
    A653-796[»]
    4Q30X-ray2.03B/D/F414-527[»]
    B/D/F653-794[»]
    ProteinModelPortaliP19491.
    SMRiP19491. Positions 412-527, 655-793.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19491.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 543522ExtracellularAdd
    BLAST
    Topological domaini565 – 59127CytoplasmicAdd
    BLAST
    Topological domaini611 – 6166Cytoplasmic
    Topological domaini638 – 812175ExtracellularAdd
    BLAST
    Topological domaini834 – 88350CytoplasmicAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei592 – 60716Helical; Pore-formingAdd
    BLAST
    Intramembranei608 – 6103

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei544 – 56421HelicalAdd
    BLAST
    Transmembranei617 – 63721HelicalAdd
    BLAST
    Transmembranei813 – 83321Helical; Name=M4Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni499 – 5013Glutamate binding
    Regioni675 – 6762Glutamate binding

    Domaini

    The M4 transmembrane segment mediates tetramerization and is required for cell surface expression.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    HOGENOMiHOG000234372.
    HOVERGENiHBG051839.
    KOiK05198.
    PhylomeDBiP19491.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR019594. Glu_rcpt_Glu/Gly-bd.
    IPR001320. Iontro_glu_rcpt.
    IPR001508. NMDA_rcpt.
    IPR028082. Peripla_BP_I.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF10613. Lig_chan-Glu_bd. 1 hit.
    [Graphical view]
    PRINTSiPR00177. NMDARECEPTOR.
    SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Flop (identifier: P19491-1) [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

    MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ    50
    FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI 100
    TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY 150
    LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE 200
    LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI 250
    QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 300
    YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ 350
    VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT 400
    ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA 450
    AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL 500
    TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI 550
    VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 600
    SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM 650
    VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP 700
    SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS 750
    KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD 800
    SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK 850
    NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI 883
    Length:883
    Mass (Da):98,688
    Last modified:July 15, 1998 - v2
    Checksum:iDEFA817027C1CCD1
    GO
    Isoform Flip (identifier: P19491-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         765-766: NA → TP
         775-775: N → S
         779-779: L → V
         796-800: SGGGD → AKDSG

    Show »
    Length:883
    Mass (Da):98,745
    Checksum:i3B70561B4F9E1C61
    GO
    Isoform 3 (identifier: P19491-3) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         848-883: VAKNPQNINP...NVYGIESVKI → MTLSDVMRSK...GMNVSVTDLS

    Show »
    Length:901
    Mass (Da):100,409
    Checksum:i13CE9B51B120A799
    GO

    RNA editingi

    Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions By similarity.By similarity

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti607 – 6071Q → R in RNA edited version.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei765 – 7662NA → TP in isoform Flip. 3 PublicationsVSP_000111
    Alternative sequencei775 – 7751N → S in isoform Flip. 3 PublicationsVSP_000112
    Alternative sequencei779 – 7791L → V in isoform Flip. 3 PublicationsVSP_000113
    Alternative sequencei796 – 8005SGGGD → AKDSG in isoform Flip. 3 PublicationsVSP_000114
    Alternative sequencei848 – 88336VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedVSP_029310Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36419 mRNA. Translation: AAA41244.1.
    M38061 mRNA. Translation: AAC37652.1.
    M85035 mRNA. Translation: AAA41240.1.
    X54655 mRNA. Translation: CAA38465.1.
    AF164344 mRNA. Translation: AAD51284.1.
    PIRiS13677.
    RefSeqiNP_001077280.1. NM_001083811.1.
    NP_058957.1. NM_017261.2.
    UniGeneiRn.91361.

    Genome annotation databases

    GeneIDi29627.
    KEGGirno:29627.
    UCSCiRGD:61862. rat. [P19491-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36419 mRNA. Translation: AAA41244.1 .
    M38061 mRNA. Translation: AAC37652.1 .
    M85035 mRNA. Translation: AAA41240.1 .
    X54655 mRNA. Translation: CAA38465.1 .
    AF164344 mRNA. Translation: AAD51284.1 .
    PIRi S13677.
    RefSeqi NP_001077280.1. NM_001083811.1.
    NP_058957.1. NM_017261.2.
    UniGenei Rn.91361.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FTJ X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1FTK X-ray 1.60 A 404-528 [» ]
    A 653-796 [» ]
    1FTL X-ray 1.80 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1FTM X-ray 1.70 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1FTO X-ray 2.00 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1FW0 X-ray 1.90 A 413-527 [» ]
    A 653-796 [» ]
    1GR2 X-ray 1.90 A 404-528 [» ]
    A 652-796 [» ]
    1LB8 X-ray 2.30 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1LB9 X-ray 2.30 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1LBB X-ray 2.10 A 413-527 [» ]
    A 653-796 [» ]
    1LBC X-ray 1.80 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1M5B X-ray 1.85 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1M5C X-ray 1.65 A 413-527 [» ]
    A 653-796 [» ]
    1M5D X-ray 1.73 A 413-527 [» ]
    A 653-796 [» ]
    1M5E X-ray 1.46 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1M5F X-ray 1.95 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MM6 X-ray 2.15 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1MM7 X-ray 1.65 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MQD X-ray 1.46 A/B/C/D 413-527 [» ]
    A/B/C/D 653-794 [» ]
    1MQG X-ray 2.15 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1MQH X-ray 1.80 A 413-527 [» ]
    A 653-796 [» ]
    1MQI X-ray 1.35 A 413-527 [» ]
    A 653-796 [» ]
    1MQJ X-ray 1.65 A 413-527 [» ]
    A 653-796 [» ]
    1MS7 X-ray 1.97 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXU X-ray 1.80 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXV X-ray 1.95 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXW X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXX X-ray 2.00 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXY X-ray 1.95 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MXZ X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MY0 X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MY1 X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MY2 X-ray 1.80 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MY3 X-ray 1.75 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1MY4 X-ray 1.90 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1N0T X-ray 2.10 A/B/C/D 413-527 [» ]
    A/B/C/D 653-796 [» ]
    1NNK X-ray 1.85 A 413-527 [» ]
    A 653-796 [» ]
    1NNP X-ray 1.90 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1P1N X-ray 1.60 A 413-527 [» ]
    A 653-796 [» ]
    1P1O X-ray 1.60 A 413-527 [» ]
    A 653-796 [» ]
    1P1Q X-ray 2.00 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    1P1U X-ray 2.00 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1P1W X-ray 1.80 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1SYH X-ray 1.80 A 413-527 [» ]
    A 653-796 [» ]
    1SYI X-ray 2.10 A/B 413-527 [» ]
    A/B 653-796 [» ]
    1WVJ X-ray 1.75 A 413-527 [» ]
    A 653-796 [» ]
    1XHY X-ray 1.85 A 413-527 [» ]
    A 653-796 [» ]
    2AIX X-ray 2.17 A 413-527 [» ]
    A 653-796 [» ]
    2AL4 X-ray 1.70 A/B/C/D/E/F 413-527 [» ]
    A/B/C/D/E/F 653-796 [» ]
    2AL5 X-ray 1.65 A/B 413-527 [» ]
    A/B 653-796 [» ]
    2ANJ X-ray 2.10 A 413-527 [» ]
    A 653-796 [» ]
    2CMO X-ray 2.65 A/B 413-527 [» ]
    A/B 653-796 [» ]
    2GFE X-ray 1.54 A/B/C 413-527 [» ]
    A/B/C 653-795 [» ]
    2I3V X-ray 2.40 A/B/C/D 413-527 [» ]
    A/B/C/D 655-794 [» ]
    2I3W X-ray 2.30 A/B 413-527 [» ]
    A/B 653-794 [» ]
    2P2A X-ray 2.26 A/B 413-527 [» ]
    A/B 653-796 [» ]
    2UXA X-ray 2.38 A/B/C 412-795 [» ]
    2XX7 X-ray 2.20 A/B/C 413-527 [» ]
    A/B/C 653-795 [» ]
    2XX8 X-ray 1.55 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    2XX9 X-ray 1.97 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    2XXH X-ray 1.50 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    2XXI X-ray 1.60 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    3B6Q X-ray 2.00 A 413-527 [» ]
    A 653-796 [» ]
    3B6T X-ray 2.10 A 413-527 [» ]
    A 653-796 [» ]
    3B6W X-ray 1.70 A/B/C/D 413-527 [» ]
    A/B/C/D 653-796 [» ]
    3B7D X-ray 2.50 A/B/C/D/E/F/G/H 413-527 [» ]
    A/B/C/D/E/F/G/H 653-794 [» ]
    3BBR X-ray 2.25 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3BFT X-ray 2.27 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    3BFU X-ray 1.95 A/B/C/D 413-527 [» ]
    A/B/C/D 653-796 [» ]
    3BKI X-ray 1.87 B/C/D/P 413-527 [» ]
    B/C/D/P 653-796 [» ]
    3DP6 X-ray 1.55 A/B/C 413-527 [» ]
    A/B/C 653-794 [» ]
    3H03 X-ray 1.90 A/B/D/G 414-527 [» ]
    A/B/D/G 653-794 [» ]
    3H06 X-ray 2.80 B/E/G/H/J/L/N/P 414-527 [» ]
    B/E/G/H/J/L/N/P 653-794 [» ]
    3H5V X-ray 2.33 A/B/C 21-404 [» ]
    3H5W X-ray 2.69 A/B 21-404 [» ]
    3H6T X-ray 2.25 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    3H6U X-ray 1.85 A 413-527 [» ]
    A 653-796 [» ]
    3H6V X-ray 2.10 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3H6W X-ray 1.49 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3HSY X-ray 1.75 A/B 25-400 [» ]
    3IJO X-ray 2.00 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3IJX X-ray 2.88 B/D/H 414-527 [» ]
    B/D/H 653-794 [» ]
    3IK6 X-ray 2.10 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3IL1 X-ray 2.00 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3ILT X-ray 2.11 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3ILU X-ray 2.00 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3KG2 X-ray 3.60 A/B/C/D 25-412 [» ]
    A/B/C/D 414-847 [» ]
    3KGC X-ray 1.55 A/B 414-527 [» ]
    A/B 654-795 [» ]
    3LSF X-ray 1.85 B/E/H 414-527 [» ]
    B/E/H 653-794 [» ]
    3LSL X-ray 2.12 A/D/G 414-527 [» ]
    A/D/G 653-794 [» ]
    3M3L X-ray 1.85 A/D/G 414-794 [» ]
    3N6V X-ray 3.20 A/B/C/D/E/F 27-400 [» ]
    3O28 X-ray 2.00 A 413-527 [» ]
    A 653-795 [» ]
    3O29 X-ray 2.02 A 413-527 [» ]
    A 653-795 [» ]
    3O2A X-ray 1.90 A 413-527 [» ]
    A 653-795 [» ]
    3O2J X-ray 1.95 A/B 22-400 [» ]
    3O6G X-ray 1.80 A 413-527 [» ]
    A 653-795 [» ]
    3O6H X-ray 2.10 A 413-527 [» ]
    A 653-795 [» ]
    3O6I X-ray 1.80 A 413-527 [» ]
    A 653-795 [» ]
    3PD8 X-ray 2.48 A/B/C 413-527 [» ]
    A/B/C 653-795 [» ]
    3PD9 X-ray 2.10 A/B 413-527 [» ]
    A/B 653-795 [» ]
    3PMV X-ray 1.80 A 413-527 [» ]
    A 653-795 [» ]
    3PMW X-ray 2.20 A 413-527 [» ]
    A 653-795 [» ]
    3PMX X-ray 1.87 A 413-527 [» ]
    A 653-795 [» ]
    3RTF X-ray 1.70 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3RTW X-ray 2.10 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3T93 X-ray 1.91 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3T96 X-ray 1.87 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3T9H X-ray 2.02 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3T9U X-ray 1.97 A/B/C 414-527 [» ]
    A/B/C 653-794 [» ]
    3T9V X-ray 1.98 A/B 414-527 [» ]
    A/B 653-794 [» ]
    3T9X X-ray 1.82 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    3TDJ X-ray 1.95 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3TKD X-ray 1.45 A/B 413-527 [» ]
    A/B 653-795 [» ]
    3TZA X-ray 1.90 A/B 413-527 [» ]
    A/B 653-796 [» ]
    4FAT X-ray 1.40 A 413-527 [» ]
    A 653-796 [» ]
    4G8M X-ray 2.05 A/B 413-527 [» ]
    A/B 653-796 [» ]
    4GXS X-ray 1.96 B/D 414-527 [» ]
    B/D 653-794 [» ]
    4H8J X-ray 1.80 A/B/C/D 413-527 [» ]
    A/B/C/D 653-797 [» ]
    4IGT X-ray 1.24 A 413-527 [» ]
    A 653-796 [» ]
    4ISU X-ray 2.30 A/B/C/D 413-527 [» ]
    A/B/C/D 653-796 [» ]
    4IY5 X-ray 2.00 A/B 413-527 [» ]
    A/B 653-796 [» ]
    4IY6 X-ray 1.72 A 413-527 [» ]
    A 653-796 [» ]
    4L17 X-ray 2.80 A/C/E/G 413-527 [» ]
    A/C/E/G 653-796 [» ]
    4LZ5 X-ray 1.50 A/B/C 404-527 [» ]
    A/B/C 653-796 [» ]
    4LZ7 X-ray 2.10 A/B/C 404-527 [» ]
    A/B/C 653-796 [» ]
    4LZ8 X-ray 1.85 A/B/C 404-527 [» ]
    A/B/C 653-796 [» ]
    4N07 X-ray 1.87 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    4O3A X-ray 1.80 A/B/C 413-527 [» ]
    A/B/C 653-796 [» ]
    4O3B X-ray 1.91 A/B 413-527 [» ]
    A/B 653-796 [» ]
    4O3C X-ray 1.50 A 413-527 [» ]
    A 653-796 [» ]
    4Q30 X-ray 2.03 B/D/F 414-527 [» ]
    B/D/F 653-794 [» ]
    ProteinModelPortali P19491.
    SMRi P19491. Positions 412-527, 655-793.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248250. 6 interactions.
    DIPi DIP-30952N.
    IntActi P19491. 20 interactions.
    MINTi MINT-86056.

    Chemistry

    BindingDBi P19491.
    ChEMBLi CHEMBL3503.
    DrugBanki DB00606. Cyclothiazide.
    GuidetoPHARMACOLOGYi 445.

    PTM databases

    PhosphoSitei P19491.

    Proteomic databases

    PaxDbi P19491.
    PRIDEi P19491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29627.
    KEGGi rno:29627.
    UCSCi RGD:61862. rat. [P19491-1 ]

    Organism-specific databases

    CTDi 2891.
    RGDi 61862. Gria2.

    Phylogenomic databases

    eggNOGi NOG316680.
    HOGENOMi HOG000234372.
    HOVERGENi HBG051839.
    KOi K05198.
    PhylomeDBi P19491.

    Miscellaneous databases

    EvolutionaryTracei P19491.
    NextBioi 609842.

    Gene expression databases

    Genevestigatori P19491.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR019594. Glu_rcpt_Glu/Gly-bd.
    IPR001320. Iontro_glu_rcpt.
    IPR001508. NMDA_rcpt.
    IPR028082. Peripla_BP_I.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF10613. Lig_chan-Glu_bd. 1 hit.
    [Graphical view ]
    PRINTSi PR00177. NMDARECEPTOR.
    SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP).
      Tissue: Brain.
    2. "Molecular cloning and functional expression of glutamate receptor subunit genes."
      Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F.
      Science 249:1033-1037(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
    3. "A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties."
      Nakanishi N., Schneider N.A., Axel R.
      Neuron 5:569-581(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
      Tissue: Brain cortex and Hippocampus.
    4. "N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation."
      Everts I., Villmann C., Hollmann M.
      Mol. Pharmacol. 52:861-873(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), FUNCTION.
      Strain: Sprague-Dawley.
    5. "RNA editing in brain controls a determinant of ion flow in glutamate-gated channels."
      Sommer B., Koehler M., Sprengel R., Seeburg P.H.
      Cell 67:11-19(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITION 607.
    6. "The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs."
      Osten P., Srivastava S., Inman G.J., Vilim F.S., Khatri L., Lee L.M., States B.A., Einheber S., Milner T.A., Hanson P.I., Ziff E.B.
      Neuron 21:99-110(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NSF, IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB, MUTAGENESIS OF 851-ASN-PRO-852.
    7. "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
      Xia J., Zhang X., Staudinger J., Huganir R.L.
      Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCABP.
    8. "Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS."
      Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.
      Science 249:1580-1585(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
    9. "Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696."
      Nakazawa K., Tadakuma T., Nokihara K., Ito M.
      Neurosci. Res. 24:75-86(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-683 AND SER-717.
    10. "GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors."
      Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.
      Nature 386:279-284(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRIP1.
      Tissue: Hippocampus.
    11. "Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo."
      Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., Standaert D.G., Weinberg R., Sheng M.
      J. Neurosci. 19:6528-6537(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRIP2.
    12. "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors."
      Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P.
      Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    13. "Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases."
      Hayashi T., Huganir R.L.
      J. Neurosci. 24:6152-6160(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-876, TISSUE SPECIFICITY.
    14. "Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics."
      Bedoukian M.A., Weeks A.M., Partin K.M.
      J. Biol. Chem. 281:23908-23921(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
    15. "SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
      Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
      Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRFN1.
    16. "AMPA receptor subunit-specific regulation by a distinct family of type II TARPs."
      Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.
      Neuron 59:986-996(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNG5.
    17. "Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
      Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
      Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNG5.
    18. "Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors."
      Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.
      Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    19. "Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins."
      Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.
      Neuron 68:1082-1096(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior."
      Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., Dawson V.L.
      Cell 145:284-299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATAD1 AND GRIP1.
    21. "Structure of a glutamate-receptor ligand-binding core in complex with kainate."
      Armstrong N., Sun Y., Chen G.Q., Gouaux E.
      Nature 395:913-917(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE.
    22. "Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core."
      Armstrong N., Gouaux E.
      Neuron 28:165-181(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC.
    23. "Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate."
      Jin R., Horning M., Mayer M.L., Gouaux E.
      Biochemistry 41:15635-15643(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH QUISQUALATE, FUNCTION.
    24. "Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core."
      Hogner A., Kastrup J.S., Jin R., Liljefors T., Mayer M.L., Egebjerg J., Larsen I.K., Gouaux E.
      J. Mol. Biol. 322:93-109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA AND BR-HIBO.
    25. "Mechanism of glutamate receptor desensitization."
      Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E.
      Nature 417:245-253(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; DNQX AND KAINATE, FUNCTION, SUBUNIT, MUTAGENESIS OF LEU-504 AND ASN-775.
    26. "Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity."
      Lunn M.-L., Hogner A., Stensboel T.B., Gouaux E., Egebjerg J., Kastrup J.S.
      J. Med. Chem. 46:872-875(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA AND ZINC IONS.
    27. "Structural basis for partial agonist action at ionotropic glutamate receptors."
      Jin R., Banke T.G., Mayer M.L., Traynelis S.F., Gouaux E.
      Nat. Neurosci. 6:803-810(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH WILLARDIINES, FUNCTION.
    28. "Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes."
      Armstrong N., Mayer M., Gouaux E.
      Proc. Natl. Acad. Sci. U.S.A. 100:5736-5741(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; KAINATE AND QUISQUALATE, FUNCTION.
    29. "Mechanism of positive allosteric modulators acting on AMPA receptors."
      Jin R., Clark S., Weeks A.M., Dudman J.T., Gouaux E., Partin K.M.
      J. Neurosci. 25:9027-9036(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ANIRACETAM AND CX614, FUNCTION.
    30. "Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2."
      Frandsen A., Pickering D.S., Vestergaard B., Kasper C., Nielsen B.B., Greenwood J.R., Campiani G., Fattorusso C., Gajhede M., Schousboe A., Kastrup J.S.
      Mol. Pharmacol. 67:703-713(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 AND KAINATE, FUNCTION.
    31. "Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor."
      Armstrong N., Jasti J., Beich-Frandsen M., Gouaux E.
      Cell 127:85-97(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    32. "The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209."
      Kasper C., Pickering D.S., Mirza O., Olsen L., Kristensen A.S., Greenwood J.R., Liljefors T., Schousboe A., Waetjen F., Gajhede M., Sigurskjold B.W., Kastrup J.S.
      J. Mol. Biol. 357:1184-1201(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND S1209, FUNCTION.
    33. "X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor."
      Sobolevsky A.I., Rosconi M.P., Gouaux E.
      Nature 462:745-756(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITH GLUTAMATE ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796, FUNCTION, SUBUNIT, MEMBRANE TOPOLOGY, GLYCOSYLATION AT ASN-370.
    34. "Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers."
      Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M., Greger I.H.
      EMBO J. 30:959-971(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-256 AND ASN-370.
    35. "Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations."
      Ahmed A.H., Wang S., Chuang H.H., Oswald R.E.
      J. Biol. Chem. 286:35257-35266(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 414-794 IN COMPLEXES WITH GLUTAMATE; IODOWILLARDIINE AND KAINATE, FUNCTION, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGRIA2_RAT
    AccessioniPrimary (citable) accession number: P19491
    Secondary accession number(s): Q9R174
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 170 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3