UniProtKB - P42260 (GRIK2_RAT)
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Protein
Glutamate receptor ionotropic, kainate 2
Gene
Grik2
Organism
Rattus norvegicus (Rat)
Status
Functioni
Ionotropic glutamate receptor. 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 (PubMed:17115050, PubMed:17486098). May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity).By similarity2 Publications
Miscellaneous
The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate > quisqualate > glutamate. It does not bind AMPA without coexpression with GRIK5.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 523 | Glutamate | 1 | |
Binding sitei | 738 | Glutamate | 1 |
GO - Molecular functioni
- extracellularly glutamate-gated ion channel activity Source: UniProtKB
- glutamate receptor activity Source: UniProtKB
- identical protein binding Source: RGD
- ionotropic glutamate receptor activity Source: RGD
- kainate selective glutamate receptor activity Source: RGD
- PDZ domain binding Source: UniProtKB
- protein homodimerization activity Source: RGD
- ubiquitin conjugating enzyme binding Source: RGD
- ubiquitin protein ligase binding Source: RGD
GO - Biological processi
- behavioral fear response Source: RGD
- cellular calcium ion homeostasis Source: RGD
- chemical synaptic transmission Source: RGD
- excitatory postsynaptic potential Source: RGD
- inhibitory postsynaptic potential Source: RGD
- intracellular protein transport Source: RGD
- modulation of chemical synaptic transmission Source: RGD
- negative regulation of neuron apoptotic process Source: RGD
- negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
- neuronal action potential Source: RGD
- neuron apoptotic process Source: UniProtKB
- positive regulation of neuron apoptotic process Source: RGD
- positive regulation of synaptic transmission Source: RGD
- receptor clustering Source: UniProtKB
- regulation of JNK cascade Source: UniProtKB
- regulation of long-term neuronal synaptic plasticity Source: RGD
- regulation of membrane potential Source: RGD
- regulation of short-term neuronal synaptic plasticity Source: RGD
- synaptic transmission, glutamatergic Source: RGD
Keywordsi
Molecular function | Ion channel, Ligand-gated ion channel, Receptor |
Biological process | Ion transport, Transport |
Enzyme and pathway databases
Reactomei | R-RNO-451307. Activation of Na-permeable kainate receptors. R-RNO-451308. Activation of Ca-permeable Kainate Receptor. |
Protein family/group databases
TCDBi | 1.A.10.1.11. the glutamate-gated ion channel (gic) family of neurotransmitter receptors. |
Names & Taxonomyi
Protein namesi | Recommended name: Glutamate receptor ionotropic, kainate 2Short name: GluK2 Alternative name(s): Glutamate receptor 6 Short name: GluR-6 Short name: GluR6 |
Gene namesi | Name:Grik2 Synonyms:Glur6 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2733. Grik2. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 32 – 561 | ExtracellularSequence analysisAdd BLAST | 530 | |
Transmembranei | 562 – 582 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 583 – 638 | CytoplasmicSequence analysisAdd BLAST | 56 | |
Transmembranei | 639 – 659 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 660 – 819 | ExtracellularSequence analysisAdd BLAST | 160 | |
Transmembranei | 820 – 840 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 841 – 908 | CytoplasmicSequence analysisAdd BLAST | 68 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, SynapsePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 883 | V → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication | 1 | |
Mutagenesisi | 884 | I → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication | 1 | |
Mutagenesisi | 886 | K → R: Abolishes sumoylation. Loss of kainate-mediated endocytosis. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3607. |
GuidetoPHARMACOLOGYi | 451. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 31 | Sequence analysisAdd BLAST | 31 | |
ChainiPRO_0000011546 | 32 – 908 | Glutamate receptor ionotropic, kainate 2Add BLAST | 877 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 67 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 73 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 96 ↔ 347 | 1 Publication | ||
Glycosylationi | 275 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 378 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 412 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 423 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 430 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 546 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 751 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 846 | Phosphoserine; by PKCBy similarity | 1 | |
Modified residuei | 868 | Phosphoserine; by PKCBy similarity | 1 | |
Cross-linki | 886 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication |
Post-translational modificationi
Sumoylation mediates kainate receptor-mediated endocytosis and regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and desumoylated by SENP1.1 Publication
Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome.1 Publication
Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.By similarity
Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P42260. |
PRIDEi | P42260. |
PTM databases
iPTMneti | P42260. |
PhosphoSitePlusi | P42260. |
Expressioni
Tissue specificityi
Highest expression is found in the olfactory lobe, piriform cortex, dentate gyrus, hippocampus, granular cell layer of the cerebellum, and in caudate-putamen.
Gene expression databases
Bgeei | ENSRNOG00000000368. |
ExpressionAtlasi | P42260. baseline and differential. |
Genevisiblei | P42260. RN. |
Interactioni
Subunit structurei
Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Assembles into a kainate-gated homomeric channel that does not bind AMPA (By similarity). GRIK2 associated to GRIK5 forms functional channels that can be gated by AMPA. Interacts with DLG4. Interacts with NETO2. Interacts (via C-terminus) with KLHL17 (via kelch repeats); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway.By similarity6 Publications
Binary interactionsi
GO - Molecular functioni
- identical protein binding Source: RGD
- PDZ domain binding Source: UniProtKB
- protein homodimerization activity Source: RGD
- ubiquitin conjugating enzyme binding Source: RGD
- ubiquitin protein ligase binding Source: RGD
Protein-protein interaction databases
BioGridi | 248480. 6 interactors. |
DIPi | DIP-29256N. |
ELMi | P42260. |
IntActi | P42260. 5 interactors. |
MINTi | P42260. |
STRINGi | 10116.ENSRNOP00000033070. |
Chemistry databases
BindingDBi | P42260. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 34 – 47 | Combined sources | 14 | |
Helixi | 52 – 66 | Combined sources | 15 | |
Beta strandi | 68 – 84 | Combined sources | 17 | |
Helixi | 88 – 101 | Combined sources | 14 | |
Helixi | 112 – 124 | Combined sources | 13 | |
Beta strandi | 129 – 131 | Combined sources | 3 | |
Beta strandi | 145 – 151 | Combined sources | 7 | |
Helixi | 153 – 166 | Combined sources | 14 | |
Beta strandi | 170 – 178 | Combined sources | 9 | |
Helixi | 180 – 184 | Combined sources | 5 | |
Helixi | 186 – 189 | Combined sources | 4 | |
Helixi | 191 – 193 | Combined sources | 3 | |
Beta strandi | 198 – 203 | Combined sources | 6 | |
Helixi | 208 – 211 | Combined sources | 4 | |
Helixi | 212 – 220 | Combined sources | 9 | |
Beta strandi | 225 – 230 | Combined sources | 6 | |
Helixi | 232 – 244 | Combined sources | 13 | |
Beta strandi | 249 – 251 | Combined sources | 3 | |
Beta strandi | 253 – 256 | Combined sources | 4 | |
Helixi | 261 – 263 | Combined sources | 3 | |
Turni | 267 – 271 | Combined sources | 5 | |
Beta strandi | 275 – 280 | Combined sources | 6 | |
Helixi | 287 – 298 | Combined sources | 12 | |
Beta strandi | 309 – 311 | Combined sources | 3 | |
Helixi | 318 – 335 | Combined sources | 18 | |
Beta strandi | 347 – 349 | Combined sources | 3 | |
Helixi | 351 – 357 | Combined sources | 7 | |
Helixi | 359 – 362 | Combined sources | 4 | |
Beta strandi | 364 – 366 | Combined sources | 3 | |
Helixi | 367 – 372 | Combined sources | 6 | |
Helixi | 374 – 377 | Combined sources | 4 | |
Beta strandi | 378 – 385 | Combined sources | 8 | |
Helixi | 386 – 393 | Combined sources | 8 | |
Beta strandi | 399 – 404 | Combined sources | 6 | |
Beta strandi | 409 – 411 | Combined sources | 3 | |
Helixi | 424 – 429 | Combined sources | 6 | |
Beta strandi | 433 – 437 | Combined sources | 5 | |
Turni | 441 – 443 | Combined sources | 3 | |
Beta strandi | 444 – 446 | Combined sources | 3 | |
Helixi | 455 – 458 | Combined sources | 4 | |
Beta strandi | 459 – 461 | Combined sources | 3 | |
Helixi | 462 – 474 | Combined sources | 13 | |
Beta strandi | 478 – 482 | Combined sources | 5 | |
Turni | 493 – 495 | Combined sources | 3 | |
Helixi | 500 – 506 | Combined sources | 7 | |
Beta strandi | 511 – 513 | Combined sources | 3 | |
Helixi | 521 – 524 | Combined sources | 4 | |
Beta strandi | 527 – 529 | Combined sources | 3 | |
Beta strandi | 533 – 536 | Combined sources | 4 | |
Beta strandi | 538 – 544 | Combined sources | 7 | |
Helixi | 671 – 675 | Combined sources | 5 | |
Beta strandi | 678 – 685 | Combined sources | 8 | |
Helixi | 689 – 696 | Combined sources | 8 | |
Helixi | 700 – 711 | Combined sources | 12 | |
Helixi | 713 – 716 | Combined sources | 4 | |
Beta strandi | 717 – 720 | Combined sources | 4 | |
Helixi | 721 – 730 | Combined sources | 10 | |
Beta strandi | 731 – 738 | Combined sources | 8 | |
Helixi | 739 – 748 | Combined sources | 10 | |
Beta strandi | 752 – 757 | Combined sources | 6 | |
Beta strandi | 762 – 764 | Combined sources | 3 | |
Beta strandi | 767 – 769 | Combined sources | 3 | |
Helixi | 774 – 787 | Combined sources | 14 | |
Helixi | 790 – 799 | Combined sources | 10 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1S50 | X-ray | 1.65 | A | 428-806 | [»] | |
1S7Y | X-ray | 1.75 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
1S9T | X-ray | 1.80 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
1SD3 | X-ray | 1.80 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
1TT1 | X-ray | 1.93 | A/B | 429-806 | [»] | |
1YAE | X-ray | 3.11 | A/B/C/D/E/F | 419-557 | [»] | |
A/B/C/D/E/F | 662-819 | [»] | ||||
2I0B | X-ray | 1.96 | A/B/C | 429-544 | [»] | |
A/B/C | 667-806 | [»] | ||||
2I0C | X-ray | 2.25 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
2XXR | X-ray | 1.60 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
2XXT | X-ray | 1.90 | A/B | 667-806 | [»] | |
2XXU | X-ray | 1.50 | A/B | 667-806 | [»] | |
2XXV | X-ray | 1.70 | A/B | 667-806 | [»] | |
2XXW | X-ray | 2.30 | A/B | 667-806 | [»] | |
2XXX | X-ray | 2.10 | A/B/C/D | 667-806 | [»] | |
2XXY | X-ray | 3.00 | A/B/C/D | 667-806 | [»] | |
3G3F | X-ray | 1.38 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3G3G | X-ray | 1.30 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3G3H | X-ray | 1.50 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3G3I | X-ray | 1.37 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3G3J | X-ray | 1.32 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3G3K | X-ray | 1.24 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
3H6G | X-ray | 2.70 | A/B | 32-420 | [»] | |
3H6H | X-ray | 2.90 | A/B | 32-420 | [»] | |
3QLT | X-ray | 2.99 | A/B | 32-420 | [»] | |
3QLU | X-ray | 2.91 | C/D | 32-420 | [»] | |
3QLV | X-ray | 3.94 | C/D/F/H/J | 32-420 | [»] | |
4BDL | X-ray | 1.75 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
4BDM | X-ray | 3.40 | A/B/C/D | 429-544 | [»] | |
A/B/C/D | 667-806 | [»] | ||||
4BDN | X-ray | 2.50 | A/B/C/D | 429-544 | [»] | |
A/B/C/D | 667-806 | [»] | ||||
4BDO | X-ray | 2.55 | A/B/C/D | 429-544 | [»] | |
A/B/C/D | 667-806 | [»] | ||||
4BDQ | X-ray | 1.90 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
4BDR | X-ray | 1.65 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
4H8I | X-ray | 2.00 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
4UQQ | electron microscopy | 7.60 | A/B/C/D | 32-908 | [»] | |
5CMK | X-ray | 1.80 | A/B | 429-544 | [»] | |
A/B | 667-806 | [»] | ||||
5CMM | X-ray | 1.27 | A | 429-544 | [»] | |
5KUF | electron microscopy | 3.80 | A/B/C/D | 32-908 | [»] | |
5KUH | electron microscopy | 11.60 | A/B/C/D | 32-544 | [»] | |
A/B/C/D | 667-908 | [»] | ||||
ProteinModelPortali | P42260. | |||||
SMRi | P42260. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P42260. |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 516 – 518 | Glutamate binding | 3 | |
Regioni | 689 – 690 | Glutamate binding | 2 |
Sequence similaritiesi
Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK2 subfamily. [View classification]Curated
Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1054. Eukaryota. ENOG410XPSH. LUCA. |
GeneTreei | ENSGT00910000143978. |
HOGENOMi | HOG000234371. |
HOVERGENi | HBG051839. |
InParanoidi | P42260. |
KOi | K05202. |
OMAi | YFASHAQ. |
OrthoDBi | EOG091G02LN. |
PhylomeDBi | P42260. |
Family and domain databases
InterProi | View protein in InterPro IPR001828. ANF_lig-bd_rcpt. IPR019594. Glu/Gly-bd. IPR001508. Iono_rcpt_met. IPR001320. Iontro_rcpt. IPR028082. Peripla_BP_I. |
Pfami | View protein in Pfam PF01094. ANF_receptor. 1 hit. PF00060. Lig_chan. 1 hit. PF10613. Lig_chan-Glu_bd. 1 hit. |
PRINTSi | PR00177. NMDARECEPTOR. |
SMARTi | View protein in SMART SM00918. Lig_chan-Glu_bd. 1 hit. SM00079. PBPe. 1 hit. |
SUPFAMi | SSF53822. SSF53822. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P42260-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKIISPVLSN LVFSRSIKVL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM
60 70 80 90 100
GAEELAFRFA VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS
110 120 130 140 150
LGVAAIFGPS HSSSANAVQS ICNALGVPHI QTRWKHQVSD NKDSFYVSLY
160 170 180 190 200
PDFSSLSRAI LDLVQFFKWK TVTVVYDDST GLIRLQELIK APSRYNLRLK
210 220 230 240 250
IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK QALAMGMMTE
260 270 280 290 300
YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER
310 320 330 340 350
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH
360 370 380 390 400
KPWRFGTRFM SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE
410 420 430 440 450
KIGTWDPASG LNMTESQKGK PANITDSLSN RSLIVTTILE EPYVLFKKSD
460 470 480 490 500
KPLYGNDRFE GYCIDLLREL STILGFTYEI RLVEDGKYGA QDDVNGQWNG
510 520 530 540 550
MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI LYRKPNGTNP
560 570 580 590 600
GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
610 620 630 640 650
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS
660 670 680 690 700
YTANLAAFLT VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS
710 720 730 740 750
TYDKMWAFMS SRRQSVLVKS NEEGIQRVLT SDYAFLMEST TIEFVTQRNC
760 770 780 790 800
NLTQIGGLID SKGYGVGTPM GSPYRDKITI AILQLQEEGK LHMMKEKWWR
810 820 830 840 850
GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG EFLYKSKKNA
860 870 880 890 900
QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR
LPGKETMA
RNA editingi
Edited at positions 567, 571 and 621.1 Publication
Partially edited. The presence of Gln at position 621 (non-edited) determines channels with low calcium permeability, whereas an arginine residue (edited) determines a higher calcium permeability especially if the preceding sites are fully edited. This receptor is nearly completely edited in all gray matter structures (90% of the receptors).
Partially edited. The presence of Gln at position 621 (non-edited) determines channels with low calcium permeability, whereas an arginine residue (edited) determines a higher calcium permeability especially if the preceding sites are fully edited. This receptor is nearly completely edited in all gray matter structures (90% of the receptors).
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 567 | I → C in RNA edited version. | 1 | |
Natural varianti | 571 | Y → C in RNA edited version. | 1 | |
Natural varianti | 621 | Q → R in RNA edited version. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z11548 mRNA. Translation: CAA77647.1. Z11715 mRNA. Translation: CAA77778.1. |
PIRi | S19098. |
RefSeqi | NP_062182.1. NM_019309.2. |
UniGenei | Rn.87696. |
Genome annotation databases
Ensembli | ENSRNOT00000076234; ENSRNOP00000068172; ENSRNOG00000000368. |
GeneIDi | 54257. |
KEGGi | rno:54257. |
UCSCi | RGD:2733. rat. |
Keywords - Coding sequence diversityi
RNA editingSimilar proteinsi
Entry informationi
Entry namei | GRIK2_RAT | |
Accessioni | P42260Primary (citable) accession number: P42260 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | July 15, 1998 | |
Last modified: | March 28, 2018 | |
This is version 166 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |