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Protein

Glutamate receptor ionotropic, kainate 2

Gene

Grik2

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

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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei523Glutamate1
Binding sitei738Glutamate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-451307 Activation of Na-permeable kainate receptors
R-RNO-451308 Activation of Ca-permeable Kainate Receptor

Protein family/group databases

TCDBi1.A.10.1.11 the glutamate-gated ion channel (gic) family of neurotransmitter receptors

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, kainate 2
Short name:
GluK2
Alternative name(s):
Glutamate receptor 6
Short name:
GluR-6
Short name:
GluR6
Gene namesi
Name:Grik2
Synonyms:Glur6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2733 Grik2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 561ExtracellularSequence analysisAdd BLAST530
Transmembranei562 – 582HelicalSequence analysisAdd BLAST21
Topological domaini583 – 638CytoplasmicSequence analysisAdd BLAST56
Transmembranei639 – 659HelicalSequence analysisAdd BLAST21
Topological domaini660 – 819ExtracellularSequence analysisAdd BLAST160
Transmembranei820 – 840HelicalSequence analysisAdd BLAST21
Topological domaini841 – 908CytoplasmicSequence analysisAdd BLAST68

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi883V → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication1
Mutagenesisi884I → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication1
Mutagenesisi886K → R: Abolishes sumoylation. Loss of kainate-mediated endocytosis. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3607
GuidetoPHARMACOLOGYi451

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000001154632 – 908Glutamate receptor ionotropic, kainate 2Add BLAST877

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi73N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi96 ↔ 3471 Publication
Glycosylationi275N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi378N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi412N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi423N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi430N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi546N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi751N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei846Phosphoserine; by PKCBy similarity1
Modified residuei868Phosphoserine; by PKCBy similarity1
Cross-linki886Glycyl 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 conjugation

Proteomic databases

PaxDbiP42260
PRIDEiP42260

PTM databases

iPTMnetiP42260
PhosphoSitePlusiP42260

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

BgeeiENSRNOG00000000368 Expressed in 8 organ(s), highest expression level in brain
ExpressionAtlasiP42260 baseline and differential
GenevisibleiP42260 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

Protein-protein interaction databases

BioGridi248480, 6 interactors
DIPiDIP-29256N
ELMiP42260
IntActiP42260, 5 interactors
MINTiP42260
STRINGi10116.ENSRNOP00000033070

Chemistry databases

BindingDBiP42260

Structurei

Secondary structure

1908
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP42260
SMRiP42260
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42260

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni516 – 518Glutamate binding3
Regioni689 – 690Glutamate binding2

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
GeneTreeiENSGT00910000143978
HOGENOMiHOG000234371
HOVERGENiHBG051839
InParanoidiP42260
KOiK05202
OMAiHENPSYT
OrthoDBiEOG091G02LN
PhylomeDBiP42260

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P42260-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:908
Mass (Da):102,470
Last modified:July 15, 1998 - v2
Checksum:i7F430E2D8B2E982B
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1M855F1M855_RAT
Glutamate receptor ionotropic, kain...
Grik2
844Annotation score:

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).

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti567I → C in RNA edited version. 1
Natural varianti571Y → C in RNA edited version. 1
Natural varianti621Q → 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
PIRiS19098
RefSeqiNP_062182.1, NM_019309.2
UniGeneiRn.87696

Genome annotation databases

EnsembliENSRNOT00000076234; ENSRNOP00000068172; ENSRNOG00000000368
GeneIDi54257
KEGGirno:54257
UCSCiRGD:2733 rat

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11548 mRNA Translation: CAA77647.1
Z11715 mRNA Translation: CAA77778.1
PIRiS19098
RefSeqiNP_062182.1, NM_019309.2
UniGeneiRn.87696

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S50X-ray1.65A428-806[»]
1S7YX-ray1.75A/B429-544[»]
A/B667-806[»]
1S9TX-ray1.80A/B429-544[»]
A/B667-806[»]
1SD3X-ray1.80A/B429-544[»]
A/B667-806[»]
1TT1X-ray1.93A/B429-806[»]
1YAEX-ray3.11A/B/C/D/E/F419-557[»]
A/B/C/D/E/F662-819[»]
2I0BX-ray1.96A/B/C429-544[»]
A/B/C667-806[»]
2I0CX-ray2.25A/B429-544[»]
A/B667-806[»]
2XXRX-ray1.60A/B429-544[»]
A/B667-806[»]
2XXTX-ray1.90A/B667-806[»]
2XXUX-ray1.50A/B667-806[»]
2XXVX-ray1.70A/B667-806[»]
2XXWX-ray2.30A/B667-806[»]
2XXXX-ray2.10A/B/C/D667-806[»]
2XXYX-ray3.00A/B/C/D667-806[»]
3G3FX-ray1.38A/B429-544[»]
A/B667-806[»]
3G3GX-ray1.30A/B429-544[»]
A/B667-806[»]
3G3HX-ray1.50A/B429-544[»]
A/B667-806[»]
3G3IX-ray1.37A/B429-544[»]
A/B667-806[»]
3G3JX-ray1.32A/B429-544[»]
A/B667-806[»]
3G3KX-ray1.24A/B429-544[»]
A/B667-806[»]
3H6GX-ray2.70A/B32-420[»]
3H6HX-ray2.90A/B32-420[»]
3QLTX-ray2.99A/B32-420[»]
3QLUX-ray2.91C/D32-420[»]
3QLVX-ray3.94C/D/F/H/J32-420[»]
4BDLX-ray1.75A/B429-544[»]
A/B667-806[»]
4BDMX-ray3.40A/B/C/D429-544[»]
A/B/C/D667-806[»]
4BDNX-ray2.50A/B/C/D429-544[»]
A/B/C/D667-806[»]
4BDOX-ray2.55A/B/C/D429-544[»]
A/B/C/D667-806[»]
4BDQX-ray1.90A/B429-544[»]
A/B667-806[»]
4BDRX-ray1.65A/B429-544[»]
A/B667-806[»]
4H8IX-ray2.00A/B429-544[»]
A/B667-806[»]
4UQQelectron microscopy7.60A/B/C/D32-908[»]
5CMKX-ray1.80A/B429-544[»]
A/B667-806[»]
5CMMX-ray1.27A429-544[»]
5KUFelectron microscopy3.80A/B/C/D32-908[»]
5KUHelectron microscopy11.60A/B/C/D32-544[»]
A/B/C/D667-908[»]
ProteinModelPortaliP42260
SMRiP42260
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248480, 6 interactors
DIPiDIP-29256N
ELMiP42260
IntActiP42260, 5 interactors
MINTiP42260
STRINGi10116.ENSRNOP00000033070

Chemistry databases

BindingDBiP42260
ChEMBLiCHEMBL3607
GuidetoPHARMACOLOGYi451

Protein family/group databases

TCDBi1.A.10.1.11 the glutamate-gated ion channel (gic) family of neurotransmitter receptors

PTM databases

iPTMnetiP42260
PhosphoSitePlusiP42260

Proteomic databases

PaxDbiP42260
PRIDEiP42260

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000076234; ENSRNOP00000068172; ENSRNOG00000000368
GeneIDi54257
KEGGirno:54257
UCSCiRGD:2733 rat

Organism-specific databases

CTDi2898
RGDi2733 Grik2

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
GeneTreeiENSGT00910000143978
HOGENOMiHOG000234371
HOVERGENiHBG051839
InParanoidiP42260
KOiK05202
OMAiHENPSYT
OrthoDBiEOG091G02LN
PhylomeDBiP42260

Enzyme and pathway databases

ReactomeiR-RNO-451307 Activation of Na-permeable kainate receptors
R-RNO-451308 Activation of Ca-permeable Kainate Receptor

Miscellaneous databases

EvolutionaryTraceiP42260
PROiPR:P42260

Gene expression databases

BgeeiENSRNOG00000000368 Expressed in 8 organ(s), highest expression level in brain
ExpressionAtlasiP42260 baseline and differential
GenevisibleiP42260 RN

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGRIK2_RAT
AccessioniPrimary (citable) accession number: P42260
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: November 7, 2018
This is version 172 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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