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Protein

Glutamate receptor 2

Gene

Gria2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei471Glutamate1 Publication1
Binding sitei501Kainate; via amide nitrogen1 Publication1
Binding sitei506Glutamate1 Publication1
Binding sitei506Kainate1 Publication1
Sitei654Crucial to convey clamshell closure to channel opening1 Publication1
Binding sitei675Kainate; via amide nitrogen1 Publication1
Binding sitei676Kainate; via amide nitrogen1 Publication1
Binding sitei726Glutamate1 Publication1
Binding sitei726Kainate1 Publication1

GO - Molecular functioni

  • AMPA glutamate receptor activity Source: UniProtKB
  • cytoskeletal protein binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor activity Source: UniProtKB
  • kainate selective glutamate receptor activity Source: UniProtKB
  • PDZ domain binding Source: UniProtKB
  • protein kinase binding Source: RGD
  • receptor activity Source: UniProtKB

GO - Biological processi

  • chemical synaptic transmission Source: RGD
  • establishment of protein localization Source: UniProtKB
  • ionotropic glutamate receptor signaling pathway Source: UniProtKB
  • positive regulation of synaptic transmission Source: UniProtKB
  • protein tetramerization Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • regulation of receptor recycling Source: UniProtKB
  • regulation of synaptic transmission, glutamatergic Source: UniProtKB
  • response to fungicide Source: RGD
  • response to lithium ion Source: UniProtKB
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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61862. Gria2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 543ExtracellularAdd BLAST522
Transmembranei544 – 564HelicalAdd BLAST21
Topological domaini565 – 591CytoplasmicAdd BLAST27
Intramembranei592 – 607Helical; Pore-formingAdd BLAST16
Intramembranei608 – 6103
Topological domaini611 – 616Cytoplasmic6
Transmembranei617 – 637HelicalAdd BLAST21
Topological domaini638 – 812ExtracellularAdd BLAST175
Transmembranei813 – 833Helical; Name=M4Add BLAST21
Topological domaini834 – 883CytoplasmicAdd BLAST50

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: UniProtKB
  • asymmetric synapse Source: RGD
  • cell junction Source: UniProtKB-KW
  • cell surface Source: RGD
  • dendrite Source: RGD
  • dendrite cytoplasm Source: RGD
  • dendritic shaft Source: UniProtKB
  • dendritic spine Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • growth cone Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • ionotropic glutamate receptor complex Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • perikaryon Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: RGD
  • protein complex Source: UniProtKB
  • synapse Source: UniProtKB
  • synaptic vesicle membrane Source: RGD
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi504L → Y: Promotes dimerization. Strongly reduced desensitization. 1 Publication1
Mutagenesisi775N → D: Increases rate of desensitization. 1 Publication1
Mutagenesisi851 – 852NP → AA: Strongly reduces interaction with NSF. 1 Publication2

Chemistry databases

ChEMBLiCHEMBL3503.
GuidetoPHARMACOLOGYi445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001153522 – 883Glutamate receptor 2Add BLAST862

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi78 ↔ 330
Glycosylationi256N-linked (GlcNAc...)1 Publication1
Glycosylationi370N-linked (GlcNAc...)3 Publications1
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi413N-linked (GlcNAc...)Sequence analysis1
Lipidationi610S-palmitoyl cysteineBy similarity1
Modified residuei683Phosphoserine; by PKC1 Publication1
Modified residuei717Phosphoserine; by PKG1 Publication1
Disulfide bondi739 ↔ 794
Lipidationi836S-palmitoyl cysteineBy similarity1
Modified residuei860PhosphoserineBy similarity1
Modified residuei863PhosphoserineBy similarity1
Modified residuei876Phosphotyrosine1 Publication1
Modified residuei880PhosphoserineBy similarity1

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

iPTMnetiP19491.
PhosphoSitePlusiP19491.
SwissPalmiP19491.

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

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. Interacts with OLFM2 (By similarity).By similarity16 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei474Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei681Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei773Interaction with the cone snail toxin Con-ikot-ikot1 Publication1

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-77718,EBI-77718
Agap2Q8CGU44EBI-77718,EBI-4409108
Atad1Q505J93EBI-77718,EBI-4280289
Cacng2Q71RJ22EBI-77718,EBI-8538384
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

GO - Molecular functioni

  • cytoskeletal protein binding Source: RGD
  • identical protein binding Source: IntAct
  • PDZ domain binding Source: UniProtKB
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi248250. 6 interactors.
DIPiDIP-30952N.
IntActiP19491. 21 interactors.
MINTiMINT-86056.
STRINGi10116.ENSRNOP00000062152.

Chemistry databases

BindingDBiP19491.

Structurei

Secondary structure

1883
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 34Combined sources9
Helixi38 – 50Combined sources13
Beta strandi57 – 65Combined sources9
Helixi70 – 82Combined sources13
Beta strandi86 – 90Combined sources5
Turni94 – 96Combined sources3
Helixi97 – 107Combined sources11
Beta strandi110 – 113Combined sources4
Beta strandi125 – 127Combined sources3
Helixi133 – 142Combined sources10
Beta strandi147 – 152Combined sources6
Turni154 – 156Combined sources3
Helixi159 – 171Combined sources13
Beta strandi174 – 179Combined sources6
Beta strandi182 – 185Combined sources4
Helixi188 – 199Combined sources12
Turni201 – 203Combined sources3
Beta strandi206 – 211Combined sources6
Helixi213 – 226Combined sources14
Turni227 – 229Combined sources3
Helixi230 – 232Combined sources3
Beta strandi234 – 237Combined sources4
Beta strandi239 – 241Combined sources3
Helixi242 – 244Combined sources3
Helixi247 – 249Combined sources3
Beta strandi251 – 254Combined sources4
Beta strandi256 – 262Combined sources7
Beta strandi265 – 267Combined sources3
Helixi268 – 277Combined sources10
Turni282 – 284Combined sources3
Beta strandi289 – 291Combined sources3
Helixi295 – 316Combined sources22
Helixi339 – 350Combined sources12
Beta strandi353 – 355Combined sources3
Beta strandi358 – 360Combined sources3
Beta strandi366 – 368Combined sources3
Beta strandi372 – 379Combined sources8
Beta strandi382 – 390Combined sources9
Turni391 – 393Combined sources3
Beta strandi394 – 397Combined sources4
Beta strandi416 – 420Combined sources5
Turni424 – 426Combined sources3
Beta strandi427 – 429Combined sources3
Helixi433 – 435Combined sources3
Helixi438 – 441Combined sources4
Beta strandi442 – 444Combined sources3
Helixi445 – 457Combined sources13
Beta strandi461 – 465Combined sources5
Beta strandi467 – 469Combined sources3
Beta strandi472 – 474Combined sources3
Turni476 – 478Combined sources3
Helixi483 – 489Combined sources7
Beta strandi494 – 496Combined sources3
Helixi504 – 507Combined sources4
Beta strandi510 – 512Combined sources3
Beta strandi516 – 519Combined sources4
Beta strandi521 – 526Combined sources6
Turni534 – 538Combined sources5
Beta strandi539 – 542Combined sources4
Helixi544 – 565Combined sources22
Helixi617 – 622Combined sources6
Beta strandi644 – 648Combined sources5
Helixi653 – 655Combined sources3
Helixi657 – 661Combined sources5
Beta strandi664 – 669Combined sources6
Beta strandi671 – 674Combined sources4
Helixi675 – 682Combined sources8
Helixi686 – 697Combined sources12
Beta strandi704 – 706Combined sources3
Helixi707 – 716Combined sources10
Turni717 – 719Combined sources3
Beta strandi721 – 726Combined sources6
Helixi727 – 734Combined sources8
Beta strandi736 – 738Combined sources3
Beta strandi741 – 745Combined sources5
Beta strandi751 – 753Combined sources3
Beta strandi756 – 758Combined sources3
Helixi763 – 776Combined sources14
Helixi779 – 788Combined sources10
Turni789 – 791Combined sources3
Beta strandi800 – 803Combined sources4
Helixi810 – 813Combined sources4
Helixi815 – 831Combined sources17
Helixi833 – 836Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U4GX-ray4.49A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4SX-ray1.90A/B413-527[»]
A/B653-796[»]
4U4XX-ray1.56A/B413-527[»]
A/B653-796[»]
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[»]
4X48X-ray1.89A/B/C413-527[»]
A/B/C653-796[»]
4YMAX-ray1.90A/B413-527[»]
A/B653-797[»]
4YU0X-ray1.26A/B413-527[»]
A/B653-796[»]
4Z0IX-ray1.45A/B413-527[»]
A/B653-796[»]
5BUUX-ray2.07A/B413-527[»]
A/B653-796[»]
5CBRX-ray2.00A413-527[»]
A653-797[»]
5CBSX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
5ELVX-ray1.92A/B413-527[»]
A/B653-797[»]
5FHMX-ray1.55A/B413-527[»]
A/B653-797[»]
5FHNX-ray1.60A413-527[»]
A653-797[»]
5FHOX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-797[»]
5FTHX-ray2.90A/B/C404-527[»]
A/B/C653-795[»]
5FTIX-ray1.35A/B404-527[»]
A/B653-795[»]
5FWXX-ray2.50A/C25-400[»]
5FWYX-ray2.12A/C25-400[»]
5IDEelectron microscopy8.25A/C23-883[»]
5IDFelectron microscopy10.31A/C23-883[»]
5KBSelectron microscopy8.70A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBTelectron microscopy6.40A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBUelectron microscopy7.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBVelectron microscopy6.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KK2electron microscopy7.30A/B/C/D1-883[»]
5L1BX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1EX-ray4.37A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1FX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1GX-ray4.51A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1HX-ray3.80A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
ProteinModelPortaliP19491.
SMRiP19491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19491.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni499 – 501Glutamate binding3
Regioni675 – 676Glutamate binding2

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

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19491.
KOiK05198.
PhylomeDBiP19491.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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. AlignAdd to basket

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

Edited at position 607.1 Publication
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)DescriptionActionsGraphical viewLength
Natural varianti607Q → R in RNA edited version. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000111765 – 766NA → TP in isoform Flip. 3 Publications2
Alternative sequenceiVSP_000112775N → S in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000113779L → V in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000114796 – 800SGGGD → AKDSG in isoform Flip. 3 Publications5
Alternative sequenceiVSP_029310848 – 883VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedAdd BLAST36

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.
PIRiS13677.
RefSeqiNP_001077280.1. NM_001083811.1.
NP_058957.1. NM_017261.2.
UniGeneiRn.91361.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4U4GX-ray4.49A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4SX-ray1.90A/B413-527[»]
A/B653-796[»]
4U4XX-ray1.56A/B413-527[»]
A/B653-796[»]
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[»]
4X48X-ray1.89A/B/C413-527[»]
A/B/C653-796[»]
4YMAX-ray1.90A/B413-527[»]
A/B653-797[»]
4YU0X-ray1.26A/B413-527[»]
A/B653-796[»]
4Z0IX-ray1.45A/B413-527[»]
A/B653-796[»]
5BUUX-ray2.07A/B413-527[»]
A/B653-796[»]
5CBRX-ray2.00A413-527[»]
A653-797[»]
5CBSX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
5ELVX-ray1.92A/B413-527[»]
A/B653-797[»]
5FHMX-ray1.55A/B413-527[»]
A/B653-797[»]
5FHNX-ray1.60A413-527[»]
A653-797[»]
5FHOX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-797[»]
5FTHX-ray2.90A/B/C404-527[»]
A/B/C653-795[»]
5FTIX-ray1.35A/B404-527[»]
A/B653-795[»]
5FWXX-ray2.50A/C25-400[»]
5FWYX-ray2.12A/C25-400[»]
5IDEelectron microscopy8.25A/C23-883[»]
5IDFelectron microscopy10.31A/C23-883[»]
5KBSelectron microscopy8.70A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBTelectron microscopy6.40A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBUelectron microscopy7.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KBVelectron microscopy6.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KK2electron microscopy7.30A/B/C/D1-883[»]
5L1BX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1EX-ray4.37A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1FX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1GX-ray4.51A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1HX-ray3.80A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
ProteinModelPortaliP19491.
SMRiP19491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248250. 6 interactors.
DIPiDIP-30952N.
IntActiP19491. 21 interactors.
MINTiMINT-86056.
STRINGi10116.ENSRNOP00000062152.

Chemistry databases

BindingDBiP19491.
ChEMBLiCHEMBL3503.
GuidetoPHARMACOLOGYi445.

PTM databases

iPTMnetiP19491.
PhosphoSitePlusiP19491.
SwissPalmiP19491.

Proteomic databases

PaxDbiP19491.
PRIDEiP19491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2891.
RGDi61862. Gria2.

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19491.
KOiK05198.
PhylomeDBiP19491.

Miscellaneous databases

EvolutionaryTraceiP19491.
PROiP19491.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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.
ProtoNetiSearch...

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 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.