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P19491

- GRIA2_RAT

UniProt

P19491 - GRIA2_RAT

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Protein

Glutamate receptor 2

Gene

Gria2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase binding Source: RGD
  8. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 543522ExtracellularAdd
BLAST
Transmembranei544 – 56421HelicalAdd
BLAST
Topological domaini565 – 59127CytoplasmicAdd
BLAST
Intramembranei592 – 60716Helical; Pore-formingAdd
BLAST
Intramembranei608 – 6103
Topological domaini611 – 6166Cytoplasmic
Transmembranei617 – 63721HelicalAdd
BLAST
Topological domaini638 – 812175ExtracellularAdd
BLAST
Transmembranei813 – 83321Helical; Name=M4Add
BLAST
Topological domaini834 – 88350CytoplasmicAdd
BLAST

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 Source: UniProtKB-KW
  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
Complete GO annotation...

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. 1 Publication
Mutagenesisi775 – 7751N → D: Increases rate of desensitization. 1 Publication
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 – 349Combined sources
Helixi38 – 5013Combined sources
Beta strandi57 – 659Combined sources
Helixi70 – 8213Combined sources
Beta strandi86 – 905Combined sources
Turni94 – 963Combined sources
Helixi97 – 10711Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi125 – 1273Combined sources
Helixi133 – 14210Combined sources
Beta strandi147 – 1526Combined sources
Turni154 – 1563Combined sources
Helixi159 – 17113Combined sources
Beta strandi174 – 1796Combined sources
Helixi181 – 1833Combined sources
Helixi186 – 1894Combined sources
Helixi190 – 20011Combined sources
Turni201 – 2033Combined sources
Beta strandi206 – 2116Combined sources
Helixi213 – 22614Combined sources
Turni227 – 2293Combined sources
Helixi230 – 2323Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi239 – 2413Combined sources
Helixi242 – 2443Combined sources
Helixi247 – 2493Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi265 – 2673Combined sources
Helixi268 – 27710Combined sources
Turni282 – 2843Combined sources
Beta strandi289 – 2913Combined sources
Helixi295 – 31622Combined sources
Helixi339 – 35012Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi372 – 3798Combined sources
Beta strandi382 – 3909Combined sources
Turni391 – 3933Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi416 – 4205Combined sources
Turni424 – 4263Combined sources
Beta strandi427 – 4293Combined sources
Helixi433 – 4353Combined sources
Helixi438 – 4414Combined sources
Beta strandi442 – 4443Combined sources
Helixi445 – 45713Combined sources
Beta strandi461 – 4655Combined sources
Beta strandi467 – 4693Combined sources
Beta strandi472 – 4743Combined sources
Turni476 – 4783Combined sources
Helixi483 – 4897Combined sources
Beta strandi494 – 4963Combined sources
Helixi504 – 5074Combined sources
Beta strandi510 – 5123Combined sources
Beta strandi516 – 5194Combined sources
Beta strandi521 – 5266Combined sources
Turni534 – 5385Combined sources
Beta strandi539 – 5424Combined sources
Helixi544 – 56522Combined sources
Helixi617 – 6226Combined sources
Beta strandi644 – 6485Combined sources
Helixi653 – 6553Combined sources
Helixi657 – 6615Combined sources
Beta strandi664 – 6696Combined sources
Beta strandi671 – 6744Combined sources
Helixi675 – 6828Combined sources
Helixi686 – 69712Combined sources
Beta strandi704 – 7063Combined sources
Helixi707 – 71610Combined sources
Turni717 – 7193Combined sources
Beta strandi721 – 7266Combined sources
Helixi727 – 7348Combined sources
Beta strandi736 – 7383Combined sources
Beta strandi741 – 7455Combined sources
Beta strandi751 – 7533Combined sources
Beta strandi756 – 7583Combined sources
Helixi763 – 77614Combined sources
Helixi779 – 78810Combined sources
Turni789 – 7913Combined sources
Beta strandi800 – 8034Combined sources
Helixi810 – 8134Combined sources
Helixi815 – 83117Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4U1OX-ray1.85A413-527[»]
A653-796[»]
4U1WX-ray3.25A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U1XX-ray3.30A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1YX-ray3.90A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1ZX-ray1.94A413-527[»]
A653-796[»]
4U21X-ray1.39A/B413-527[»]
A/B654-796[»]
4U22X-ray1.44A413-527[»]
A653-796[»]
4U23X-ray1.67A413-527[»]
A653-796[»]
4U2PX-ray3.24A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2QX-ray3.52A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2RX-ray1.41A/B/C/D413-527[»]
A/B/C/D653-796[»]
4U4FX-ray4.79A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U5BX-ray3.50A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5CX-ray3.69A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5DX-ray3.58A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5EX-ray3.51A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5FX-ray3.70A/B/C/D25-412[»]
A/B/C/D414-850[»]
4UQ6electron microscopy12.80A/B/C/D22-847[»]
4UQJelectron microscopy10.40A/B/C/D22-847[»]
4UQKelectron microscopy16.40A/B/C/D22-847[»]
ProteinModelPortaliP19491.
SMRiP19491. Positions 412-527, 655-793.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19491.

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.
InParanoidiP19491.
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

        10         20         30         40         50
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ
60 70 80 90 100
FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI
110 120 130 140 150
TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY
160 170 180 190 200
LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE
210 220 230 240 250
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI
260 270 280 290 300
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
310 320 330 340 350
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ
360 370 380 390 400
VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT
410 420 430 440 450
ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA
460 470 480 490 500
AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL
510 520 530 540 550
TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI
560 570 580 590 600
VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
610 620 630 640 650
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM
660 670 680 690 700
VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP
710 720 730 740 750
SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS
760 770 780 790 800
KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD
810 820 830 840 850
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK
860 870 880
NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4U1O X-ray 1.85 A 413-527 [» ]
A 653-796 [» ]
4U1W X-ray 3.25 A/B/C/D 25-412 [» ]
A/B/C/D 414-622 [» ]
A/B/C/D 624-847 [» ]
4U1X X-ray 3.30 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-847 [» ]
4U1Y X-ray 3.90 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-847 [» ]
4U1Z X-ray 1.94 A 413-527 [» ]
A 653-796 [» ]
4U21 X-ray 1.39 A/B 413-527 [» ]
A/B 654-796 [» ]
4U22 X-ray 1.44 A 413-527 [» ]
A 653-796 [» ]
4U23 X-ray 1.67 A 413-527 [» ]
A 653-796 [» ]
4U2P X-ray 3.24 A/B/C/D 25-412 [» ]
A/B/C/D 414-622 [» ]
A/B/C/D 624-847 [» ]
4U2Q X-ray 3.52 A/B/C/D 25-412 [» ]
A/B/C/D 414-622 [» ]
A/B/C/D 624-847 [» ]
4U2R X-ray 1.41 A/B/C/D 413-527 [» ]
A/B/C/D 653-796 [» ]
4U4F X-ray 4.79 A/B/C/D 25-412 [» ]
A/B/C/D 414-847 [» ]
4U5B X-ray 3.50 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-850 [» ]
4U5C X-ray 3.69 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-850 [» ]
4U5D X-ray 3.58 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-850 [» ]
4U5E X-ray 3.51 A/B/C/D 25-412 [» ]
A/B/C/D 414-555 [» ]
A/B/C/D 557-602 [» ]
A/B/C/D 604-622 [» ]
A/B/C/D 624-850 [» ]
4U5F X-ray 3.70 A/B/C/D 25-412 [» ]
A/B/C/D 414-850 [» ]
4UQ6 electron microscopy 12.80 A/B/C/D 22-847 [» ]
4UQJ electron microscopy 10.40 A/B/C/D 22-847 [» ]
4UQK electron microscopy 16.40 A/B/C/D 22-847 [» ]
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.
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.
InParanoidi P19491.
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: November 26, 2014
This is version 172 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