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UniProtKB - P42260 (GRIK2_RAT)

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Protein

Glutamate receptor ionotropic, kainate 2

Gene

Grik2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • extracellular-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
Complete GO annotation...

GO - Biological processi

  • chemical synaptic transmission Source: RGD
  • negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
  • neuron apoptotic process Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of synaptic transmission Source: Ensembl
  • receptor clustering Source: UniProtKB
  • regulation of JNK cascade Source: UniProtKB
  • regulation of short-term neuronal synaptic plasticity Source: Ensembl
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2733. Grik2.

Subcellular locationi

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

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB
  • dendrite cytoplasm Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • ionotropic glutamate receptor complex Source: UniProtKB
  • perikaryon Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • synapse Source: RGD
  • terminal bouton Source: RGD
Complete GO annotation...

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

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

WithEntry#Exp.IntActNotes
Map3k11Q66HA12EBI-7809795,EBI-4279420

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
Complete GO annotation...

Protein-protein interaction databases

BioGridi248480. 4 interactors.
DIPiDIP-29256N.
IntActiP42260. 3 interactors.
MINTiMINT-8359884.
STRINGi10116.ENSRNOP00000033070.

Chemistry databases

BindingDBiP42260.

Structurei

Secondary structure

1908
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 47Combined sources14
Helixi52 – 66Combined sources15
Beta strandi68 – 84Combined sources17
Helixi88 – 101Combined sources14
Helixi112 – 124Combined sources13
Beta strandi129 – 131Combined sources3
Beta strandi145 – 151Combined sources7
Helixi153 – 166Combined sources14
Beta strandi170 – 178Combined sources9
Helixi180 – 184Combined sources5
Helixi186 – 189Combined sources4
Helixi191 – 193Combined sources3
Beta strandi198 – 203Combined sources6
Helixi208 – 211Combined sources4
Helixi212 – 220Combined sources9
Beta strandi225 – 230Combined sources6
Helixi232 – 244Combined sources13
Beta strandi249 – 251Combined sources3
Beta strandi253 – 256Combined sources4
Helixi261 – 263Combined sources3
Turni267 – 271Combined sources5
Beta strandi275 – 280Combined sources6
Helixi287 – 298Combined sources12
Beta strandi309 – 311Combined sources3
Helixi318 – 335Combined sources18
Beta strandi347 – 349Combined sources3
Helixi356 – 365Combined sources10
Beta strandi367 – 370Combined sources4
Beta strandi373 – 376Combined sources4
Turni379 – 381Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi389 – 395Combined sources7
Beta strandi398 – 406Combined sources9
Turni407 – 409Combined sources3
Beta strandi410 – 413Combined sources4
Turni425 – 428Combined sources4
Beta strandi433 – 437Combined sources5
Turni441 – 443Combined sources3
Beta strandi444 – 446Combined sources3
Helixi455 – 458Combined sources4
Beta strandi459 – 461Combined sources3
Helixi462 – 474Combined sources13
Beta strandi478 – 482Combined sources5
Turni493 – 495Combined sources3
Helixi500 – 506Combined sources7
Beta strandi511 – 513Combined sources3
Helixi521 – 524Combined sources4
Beta strandi527 – 529Combined sources3
Beta strandi533 – 536Combined sources4
Beta strandi538 – 544Combined sources7
Beta strandi665 – 667Combined sources3
Helixi671 – 675Combined sources5
Beta strandi678 – 685Combined sources8
Helixi689 – 696Combined sources8
Helixi700 – 711Combined sources12
Helixi713 – 716Combined sources4
Beta strandi717 – 720Combined sources4
Helixi721 – 730Combined sources10
Beta strandi731 – 738Combined sources8
Helixi739 – 748Combined sources10
Beta strandi752 – 757Combined sources6
Beta strandi762 – 764Combined sources3
Beta strandi767 – 769Combined sources3
Helixi774 – 787Combined sources14
Helixi790 – 799Combined sources10

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...

Miscellaneous databases

EvolutionaryTraceiP42260.

Family & Domainsi

Region

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

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 helix

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiP42260.
KOiK05202.
OMAiDSDIQHS.
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.

Sequencei

Sequence statusi: Complete.

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

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

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

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.

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: June 7, 2017
This is version 158 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families