P19491

PR
Gene name
Gria2
Protein name
Glutamate receptor 2
Names
GluR-2, AMPA-selective glutamate receptor 2, GluR-B, GluR-K2, Glutamate receptor ionotropic, AMPA 2, GluA2
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:29627
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

820-883 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

285 structures for P19491

Entry ID Method Resolution Chain Position Source
1FTJ X-ray 190 A PDB
1FTK X-ray 160 A PDB
1FTL X-ray 180 A PDB
1FTM X-ray 170 A PDB
1FTO X-ray 200 A PDB
1FW0 X-ray 190 A PDB
1GR2 X-ray 190 A PDB
1LB8 X-ray 230 A PDB
1LB9 X-ray 230 A PDB
1LBB X-ray 210 A PDB
1LBC X-ray 180 A PDB
1M5B X-ray 185 A PDB
1M5C X-ray 165 A PDB
1M5D X-ray 173 A PDB
1M5E X-ray 146 A PDB
1M5F X-ray 195 A PDB
1MM6 X-ray 215 A PDB
1MM7 X-ray 165 A PDB
1MQD X-ray 146 A PDB
1MQG X-ray 215 A PDB
1MQH X-ray 180 A PDB
1MQI X-ray 135 A PDB
1MQJ X-ray 165 A PDB
1MS7 X-ray 197 A PDB
1MXU X-ray 180 A PDB
1MXV X-ray 195 A PDB
1MXW X-ray 190 A PDB
1MXX X-ray 200 A PDB
1MXY X-ray 195 A PDB
1MXZ X-ray 190 A PDB
1MY0 X-ray 190 A PDB
1MY1 X-ray 190 A PDB
1MY2 X-ray 180 A PDB
1MY3 X-ray 175 A PDB
1MY4 X-ray 190 A PDB
1N0T X-ray 210 A PDB
1NNK X-ray 185 A PDB
1NNP X-ray 190 A PDB
1P1N X-ray 160 A PDB
1P1O X-ray 160 A PDB
1P1Q X-ray 200 A PDB
1P1U X-ray 200 A PDB
1P1W X-ray 180 A PDB
1SYH X-ray 180 A PDB
1SYI X-ray 210 A PDB
1WVJ X-ray 175 A PDB
1XHY X-ray 185 A PDB
2AIX X-ray 217 A PDB
2AL4 X-ray 170 A PDB
2AL5 X-ray 165 A PDB
2ANJ X-ray 210 A PDB
2CMO X-ray 265 A PDB
2GFE X-ray 154 A PDB
2I3V X-ray 240 A PDB
2I3W X-ray 230 A PDB
2P2A X-ray 226 A PDB
2UXA X-ray 238 A A/B/C 412-795 PDB
2XX7 X-ray 220 A PDB
2XX8 X-ray 155 A PDB
2XX9 X-ray 197 A PDB
2XXH X-ray 150 A PDB
2XXI X-ray 160 A PDB
3B6Q X-ray 200 A PDB
3B6T X-ray 210 A PDB
3B6W X-ray 170 A PDB
3B7D X-ray 250 A PDB
3BBR X-ray 225 A PDB
3BFT X-ray 227 A PDB
3BFU X-ray 195 A PDB
3BKI X-ray 187 A PDB
3DP6 X-ray 155 A PDB
3H03 X-ray 190 A PDB
3H06 X-ray 280 A PDB
3H5V X-ray 233 A A/B/C 21-404 PDB
3H5W X-ray 269 A A/B 21-404 PDB
3H6T X-ray 225 A PDB
3H6U X-ray 185 A PDB
3H6V X-ray 210 A PDB
3H6W X-ray 149 A PDB
3HSY X-ray 175 A A/B 25-400 PDB
3IJO X-ray 200 A PDB
3IJX X-ray 288 A PDB
3IK6 X-ray 210 A PDB
3IL1 X-ray 200 A PDB
3ILT X-ray 211 A PDB
3ILU X-ray 200 A PDB
3KG2 X-ray 360 A PDB
3KGC X-ray 155 A PDB
3LSF X-ray 185 A PDB
3LSL X-ray 212 A PDB
3M3L X-ray 185 A A/D/G 414-794 PDB
3N6V X-ray 320 A A/B/C/D/E/F 27-400 PDB
3O28 X-ray 200 A PDB
3O29 X-ray 202 A PDB
3O2A X-ray 190 A PDB
3O2J X-ray 195 A A/B 22-400 PDB
3O6G X-ray 180 A PDB
3O6H X-ray 210 A PDB
3O6I X-ray 180 A PDB
3PD8 X-ray 248 A PDB
3PD9 X-ray 210 A PDB
3PMV X-ray 180 A PDB
3PMW X-ray 220 A PDB
3PMX X-ray 187 A PDB
3RTF X-ray 170 A PDB
3RTW X-ray 210 A PDB
3T93 X-ray 191 A PDB
3T96 X-ray 187 A PDB
3T9H X-ray 202 A PDB
3T9U X-ray 197 A PDB
3T9V X-ray 198 A PDB
3T9X X-ray 182 A PDB
3TDJ X-ray 195 A PDB
3TKD X-ray 145 A PDB
3TZA X-ray 190 A PDB
4FAT X-ray 140 A PDB
4G8M X-ray 205 A PDB
4GXS X-ray 196 A PDB
4H8J X-ray 180 A PDB
4IGT X-ray 124 A PDB
4ISU X-ray 230 A PDB
4IY5 X-ray 200 A PDB
4IY6 X-ray 172 A PDB
4L17 X-ray 280 A PDB
4LZ5 X-ray 150 A PDB
4LZ7 X-ray 210 A PDB
4LZ8 X-ray 185 A PDB
4N07 X-ray 187 A PDB
4O3A X-ray 180 A PDB
4O3B X-ray 191 A PDB
4O3C X-ray 150 A PDB
4Q30 X-ray 203 A PDB
4U1O X-ray 185 A PDB
4U1W X-ray 325 A PDB
4U1X X-ray 330 A PDB
4U1Y X-ray 390 A PDB
4U1Z X-ray 194 A PDB
4U21 X-ray 139 A PDB
4U22 X-ray 144 A PDB
4U23 X-ray 167 A PDB
4U2P X-ray 324 A PDB
4U2Q X-ray 352 A PDB
4U2R X-ray 141 A PDB
4U4F X-ray 479 A PDB
4U4G X-ray 449 A PDB
4U4S X-ray 190 A PDB
4U4X X-ray 156 A PDB
4U5B X-ray 350 A PDB
4U5C X-ray 369 A PDB
4U5D X-ray 358 A PDB
4U5E X-ray 351 A PDB
4U5F X-ray 370 A PDB
4UQ6 EM 1280 A A/B/C/D 22-847 PDB
4UQJ EM 1040 A A/B/C/D 22-847 PDB
4UQK EM 1640 A A/B/C/D 22-847 PDB
4X48 X-ray 189 A PDB
4YMA X-ray 190 A PDB
4YU0 X-ray 126 A PDB
4Z0I X-ray 145 A PDB
5BUU X-ray 207 A PDB
5CBR X-ray 200 A PDB
5CBS X-ray 180 A PDB
5ELV X-ray 192 A PDB
5FHM X-ray 155 A PDB
5FHN X-ray 160 A PDB
5FHO X-ray 230 A PDB
5FTH X-ray 290 A PDB
5FTI X-ray 135 A PDB
5FWX X-ray 250 A A/C 25-400 PDB
5FWY X-ray 212 A A/C 25-400 PDB
5IDE EM 825 A A/C 23-883 PDB
5IDF EM 1031 A A/C 23-883 PDB
5JEI X-ray 123 A PDB
5KBS EM 870 A A/B/C/D 25-847 PDB
5KBT EM 640 A A/B/C/D 25-847 PDB
5KBU EM 780 A A/B/C/D 25-847 PDB
5KBV EM 680 A PDB
5KK2 EM 730 A A/B/C/D 1-883 PDB
5L1B X-ray 400 A PDB
5L1E X-ray 437 A PDB
5L1F X-ray 400 A PDB
5L1G X-ray 451 A PDB
5L1H X-ray 380 A PDB
5N6P X-ray 280 A A 25-400 PDB
5NG9 X-ray 115 A PDB
5NIH X-ray 130 A PDB
5NS9 X-ray 144 A PDB
5O9A X-ray 178 A PDB
5OEW X-ray 200 A PDB
5VHW EM 780 A A/B/C/D 25-847 PDB
5VHX EM 830 A A/B/C/D/E 25-847 PDB
5VHY EM 460 A A/B/C/D/E/F 25-847 PDB
5VHZ EM 840 A A/B/C/D/E/F 25-847 PDB
5VOT EM 490 A A/B/C/D 1-883 PDB
5VOU EM 640 A A/B/C/D 1-883 PDB
5VOV EM 770 A A/B/C/D 1-883 PDB
5WEK EM 460 A A/B/C/D 25-847 PDB
5WEL EM 440 A A/B/C/D 25-847 PDB
5WEM EM 610 A A/B/C/D 25-847 PDB
5WEN EM 680 A A/B/C/D 25-847 PDB
5WEO EM 420 A A/B/C/D 25-847 PDB
6DLZ EM 390 A A/B/C/D 25-847 PDB
6DM0 EM 440 A A/B/C/D 25-847 PDB
6DM1 EM 420 A A/B/C/D 25-847 PDB
6FAZ X-ray 140 A PDB
6FQG X-ray 234 A PDB
6FQH X-ray 176 A PDB
6FQI X-ray 291 A PDB
6FQJ X-ray 250 A PDB
6FQK X-ray 198 A PDB
6GIV X-ray 175 A PDB
6GL4 X-ray 195 A PDB
6HC9 X-ray 240 A PDB
6HCA X-ray 188 A PDB
6HCB X-ray 190 A PDB
6HCC X-ray 162 A PDB
6HCH X-ray 160 A PDB
6NJL EM 670 A B/D 1-883 PDB
6NJM EM 650 A B/D 1-883 PDB
6NJN EM 650 A B/D 1-883 PDB
6O9G EM 480 A A/B/C/D 25-847 PDB
6PEQ EM 297 A A/B/C/D 1-868 PDB
6Q54 X-ray 140 A PDB
6Q60 X-ray 155 A PDB
6QKC EM 410 A B/D 1-860 PDB
6QKZ EM 630 A B/D 22-860 PDB
6RUQ X-ray 465 A A/B/C/D 25-847 PDB
6U5S EM 307 A A/B/C/D 1-868 PDB
6U6I EM 312 A A/B/C/D 1-868 PDB
6UCB EM 328 A A/B/C/D 1-868 PDB
6UD4 EM 330 A A/B/C/D 1-868 PDB
6UD8 EM 320 A A/B/C/D 1-868 PDB
6XSR X-ray 425 A A/B/C/D 25-838 PDB
6YK2 X-ray 161 A PDB
6YK3 X-ray 120 A PDB
6YK4 X-ray 100 A PDB
6YK5 X-ray 115 A PDB
6YK6 X-ray 147 A PDB
6ZYU X-ray 190 A PDB
7OCA EM 340 A B/D 1-860 PDB
7OCC EM 340 A B/D 1-860 PDB
7OCD EM 350 A B/D 1-860 PDB
7OCE EM 310 A B/D 1-860 PDB
7OCF EM 360 A B/D 1-860 PDB
7QHB EM 350 A B/D 1-860 PDB
7QHH EM 360 A B/D 1-860 PDB
7RYY EM 440 A A/B/C/D 25-847 PDB
7RYZ EM 415 A A/B/C/D 25-847 PDB
7RZ4 EM 360 A A/B/C/D 25-847 PDB
7RZ5 EM 330 A A/B/C/D 25-847 PDB
7RZ6 EM 440 A A/B/C/D 25-847 PDB
7RZ7 EM 420 A A/B/C/D 25-847 PDB
7RZ8 EM 410 A A/B/C/D 25-847 PDB
7RZ9 EM 415 A A/B/C/D 25-847 PDB
7RZA EM 426 A A/B/C/D 25-847 PDB
7TNJ EM 402 A A/B/C/D 25-847 PDB
7TNK EM 450 A A/B/C/D 25-847 PDB
7TNL EM 359 A A/B/C/D 25-847 PDB
7TNM EM 474 A A/B/C/D 25-847 PDB
7TNN EM 391 A A/B/C/D 25-847 PDB
7TNO EM 402 A A/B/C/D 25-847 PDB
7TNP EM 396 A A/B/C/D 25-847 PDB
8AYL EM 320 A B/D 1-860 PDB
8AYM EM 330 A B/D 1-860 PDB
8AYN EM 280 A B/D 1-860 PDB
8AYO EM 330 A B/D 1-860 PDB
8C1R EM 320 A A/B/C/D 1-883 PDB
8C1S EM 300 A A/B/C/D 1-883 PDB
8P3Q EM 295 A A/B/C/D 1-883 PDB
8P3S EM 295 A A/B/C/D 1-883 PDB
8P3X EM 336 A A/B/C/D 1-883 PDB
8P3Y EM 355 A A/B/C/D 1-883 PDB
8P3Z EM 346 A A/B/C/D 1-883 PDB
8QEZ X-ray 155 A PDB
8SS2 EM 358 A A/B/C/D 25-847 PDB
8SS3 EM 321 A A/B/C/D 25-847 PDB
8SS4 EM 330 A A/B/C/D 25-847 PDB
8SS5 EM 356 A A/B/C/D 25-847 PDB
8SS6 EM 301 A A/B/C/D 25-847 PDB
8SS7 EM 276 A A/B/C/D 25-847 PDB
8SS8 EM 281 A A/B/C/D 25-847 PDB
8SS9 EM 272 A A/B/C/D 25-847 PDB
8SSA EM 388 A A/B/C/D 25-847 PDB
8SSB EM 366 A A/B/C/D 25-847 PDB
AF-P19491-F1 Predicted AlphaFoldDB

1 variants for P19491

Variant ID(s) Position Change Description Diseaes Association Provenance
607 Q>R RNA edited version [UniProt] No

No associated diseases with P19491

3 regional properties for P19491

Type Name Position InterPro Accession
domain Ionotropic glutamate receptor, C-terminal 415 - 824 IPR001320
domain Receptor, ligand binding region 55 - 380 IPR001828
domain Ionotropic glutamate receptor, L-glutamate and glycine-binding domain 414 - 529 IPR019594

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
  • Postsynaptic cell membrane ; Multi-pass membrane protein
  • Postsynaptic density membrane ; Multi-pass membrane protein
  • Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (PubMed:19265014)
  • Displays a somatodendritic localization and is excluded from axons in neurons (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

35 GO annotations of cellular component

Name Definition
AMPA glutamate receptor complex An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. The AMPA receptors mediate fast synaptic transmission in the CNS and are composed of subunits GluR1-4, products from separate genes. These subunits have an extracellular N-terminus and an intracellular C-terminus.
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
asymmetric synapse A type of synapse occurring between an axon and a dendritic spine or dendritic shaft. Asymmetric synapses, the most abundant synapse type in the central nervous system, involve axons that contain predominantly spherical vesicles and contain a thickened postsynaptic density. Most or all synapses of this type are excitatory.
cell surface The external part of the cell wall and/or plasma membrane.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
dendrite cytoplasm All of the contents of a dendrite, excluding the surrounding plasma membrane.
dendritic shaft Cylindric portion of the dendrite, directly stemming from the perikaryon, and carrying the dendritic spines.
dendritic spine A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
growth cone The migrating motile tip of a growing neuron projection, where actin accumulates, and the actin cytoskeleton is the most dynamic.
integral component of plasma membrane The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of postsynaptic density membrane The component of the postsynaptic density membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of postsynaptic membrane The component of the postsynaptic membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of presynaptic membrane The component of the presynaptic membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
ionotropic glutamate receptor complex A multimeric assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand-gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
perikaryon The portion of the cell soma (neuronal cell body) that excludes the nucleus.
perisynaptic space The extracellular region immediately adjacent to to a synapse.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
postsynaptic density membrane The membrane component of the postsynaptic density. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated.
postsynaptic membrane A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
presynaptic membrane A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
Schaffer collateral - CA1 synapse A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.
somatodendritic compartment The region of a neuron that includes the cell body (cell soma) and dendrite(s), but excludes the axon.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
synaptic membrane A specialized area of membrane on either the presynaptic or the postsynaptic side of a synapse, the junction between a nerve fiber of one neuron and another neuron or muscle fiber or glial cell.
synaptic vesicle A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
synaptic vesicle membrane The lipid bilayer surrounding a synaptic vesicle.
terminal bouton Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it.

16 GO annotations of molecular function

Name Definition
AMPA glutamate receptor activity An ionotropic glutamate receptor activity that exhibits fast gating by glutamate and acts by opening a cation channel permeable to sodium, potassium, and, in the absence of a GluR2 subunit, calcium.
amyloid-beta binding Binding to an amyloid-beta peptide/protein.
ATPase binding Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
cytoskeletal protein binding Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
extracellularly glutamate-gated ion channel activity Enables the transmembrane transfer of an ion by a channel that opens when glutamate is bound by the channel complex or one of its constituent parts on the extracellular side of the plasma membrane.
glutamate receptor binding Binding to a glutamate receptor.
identical protein binding Binding to an identical protein or proteins.
immunoglobulin binding Binding to an immunoglobulin.
ionotropic glutamate receptor activity Catalysis of the transmembrane transfer of an ion by a channel that opens when glutamate has been bound by the channel complex or one of its constituent parts.
kainate selective glutamate receptor activity An ionotropic glutamate receptor activity that exhibits fast gating by glutamate, acts by opening a cation channel permeable to sodium and potassium, and for which kainate is an agonist.
ligand-gated ion channel activity Enables the transmembrane transfer of an ion by a channel that opens when a specific ligand has been bound by the channel complex or one of its constituent parts.
PDZ domain binding Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
signaling receptor activity Receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response.
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.
transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential Any transmitter-gated ion channel activity that is involved in regulation of postsynaptic membrane potential.

10 GO annotations of biological process

Name Definition
chemical synaptic transmission The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
establishment of protein localization The directed movement of a protein to a specific location.
ionotropic glutamate receptor signaling pathway The series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex, and ending with the regulation of a downstream cellular process, e.g. transcription.
positive regulation of synaptic transmission Any process that activates or increases the frequency, rate or extent of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse.
protein tetramerization The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
receptor internalization A receptor-mediated endocytosis process that results in the movement of receptors from the plasma membrane to the inside of the cell. The process begins when cell surface receptors are monoubiquitinated following ligand-induced activation. Receptors are subsequently taken up into endocytic vesicles from where they are either targeted to the lysosome or vacuole for degradation or recycled back to the plasma membrane.
regulation of receptor recycling Any process that modulates the frequency, rate, or extent of receptor recycling.
regulation of synaptic transmission, glutamatergic Any process that modulates the frequency, rate or extent of glutamatergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter glutamate.
response to fungicide Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a fungicide stimulus. Fungicides are chemicals used to kill fungi.
response to lithium ion Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lithium (Li+) ion stimulus.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P23819 Gria2 Glutamate receptor 2 Mus musculus (Mouse) PR
P35439 Grin1 Glutamate receptor ionotropic, NMDA 1 Rattus norvegicus (Rat) PR
Q8VHN2 Grin3b Glutamate receptor ionotropic, NMDA 3B Rattus norvegicus (Rat) PR
Q9SHV1 GLR2.2 Glutamate receptor 2.2 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SHV2 GLR2.3 Glutamate receptor 2.3 Arabidopsis thaliana (Mouse-ear cress) PR
O81776 GLR2.4 Glutamate receptor 2.4 Arabidopsis thaliana (Mouse-ear cress) PR
O04660 GLR2.1 Glutamate receptor 2.1 Arabidopsis thaliana (Mouse-ear cress) PR
O81078 GLR2.9 Glutamate receptor 2.9 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SDQ4 GLR3.7 Glutamate receptor 3.7 Arabidopsis thaliana (Mouse-ear cress) PR
Q84W41 GLR3.6 Glutamate receptor 3.6 Arabidopsis thaliana (Mouse-ear cress) PR
Q9C8E7 GLR3.3 Glutamate receptor 3.3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
70 80 90 100 110 120
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
130 140 150 160 170 180
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
190 200 210 220 230 240
GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
250 260 270 280 290 300
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
310 320 330 340 350 360
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI
370 380 390 400 410 420
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT
430 440 450 460 470 480
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI
490 500 510 520 530 540
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
550 560 570 580 590 600
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
610 620 630 640 650 660
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
670 680 690 700 710 720
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK
730 740 750 760 770 780
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL
790 800 810 820 830 840
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR
850 860 870 880
AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI