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P42260

- GRIK2_RAT

UniProt

P42260 - GRIK2_RAT

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Protein

Glutamate receptor ionotropic, kainate 2

Gene

Grik2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei523 – 5231Glutamate
Binding sitei738 – 7381Glutamate

GO - Molecular functioni

  1. extracellular-glutamate-gated ion channel activity Source: RefGenome
  2. glutamate receptor activity Source: UniProtKB
  3. identical protein binding Source: RGD
  4. ionotropic glutamate receptor activity Source: RGD
  5. kainate selective glutamate receptor activity Source: RGD
  6. PDZ domain binding Source: UniProtKB
  7. protein homodimerization activity Source: RGD
  8. ubiquitin conjugating enzyme binding Source: RGD
  9. ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  1. behavioral fear response Source: Ensembl
  2. cellular calcium ion homeostasis Source: Ensembl
  3. intracellular protein transport Source: Ensembl
  4. ionotropic glutamate receptor signaling pathway Source: GOC
  5. ion transmembrane transport Source: GOC
  6. negative regulation of neuron apoptotic process Source: Ensembl
  7. negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
  8. neuronal action potential Source: Ensembl
  9. neuron apoptotic process Source: UniProtKB
  10. positive regulation of neuron apoptotic process Source: RGD
  11. positive regulation of synaptic transmission Source: Ensembl
  12. receptor clustering Source: UniProtKB
  13. regulation of excitatory postsynaptic membrane potential Source: Ensembl
  14. regulation of inhibitory postsynaptic membrane potential Source: Ensembl
  15. regulation of JNK cascade Source: UniProtKB
  16. regulation of long-term neuronal synaptic plasticity Source: Ensembl
  17. regulation of short-term neuronal synaptic plasticity Source: Ensembl
  18. signal transduction Source: GOC
  19. synaptic transmission Source: RGD
  20. synaptic transmission, glutamatergic Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

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 › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
ProteomesiUP000002494: Chromosome 20

Organism-specific databases

RGDi2733. Grik2.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell junction › synapse › postsynaptic cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 561530ExtracellularSequence AnalysisAdd
BLAST
Transmembranei562 – 58221HelicalSequence AnalysisAdd
BLAST
Topological domaini583 – 63856CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei639 – 65921HelicalSequence AnalysisAdd
BLAST
Topological domaini660 – 819160ExtracellularSequence AnalysisAdd
BLAST
Transmembranei820 – 84021HelicalSequence AnalysisAdd
BLAST
Topological domaini841 – 90868CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: RGD
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: UniProtKB
  4. dendrite cytoplasm Source: RGD
  5. integral component of plasma membrane Source: UniProtKB
  6. ionotropic glutamate receptor complex Source: UniProtKB
  7. kainate selective glutamate receptor complex Source: RefGenome
  8. perikaryon Source: RGD
  9. postsynaptic density Source: Ensembl
  10. postsynaptic membrane Source: RefGenome
  11. presynaptic membrane Source: RefGenome
  12. synapse Source: RGD
  13. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi883 – 8831V → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication
Mutagenesisi884 – 8841I → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication
Mutagenesisi886 – 8861K → R: Abolishes sumoylation. Loss of kainate-mediated endocytosis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 908877Glutamate receptor ionotropic, kainate 2PRO_0000011546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671N-linked (GlcNAc...)1 Publication
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi96 ↔ 3471 Publication
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)1 Publication
Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
Glycosylationi423 – 4231N-linked (GlcNAc...)1 Publication
Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi751 – 7511N-linked (GlcNAc...)1 Publication
Modified residuei846 – 8461Phosphoserine; by PKCBy similarity
Modified residuei868 – 8681Phosphoserine; by PKCBy similarity
Cross-linki886 – 886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)

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

PhosphoSiteiP42260.

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.
GenevestigatoriP42260.

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

Protein-protein interaction databases

BioGridi248480. 3 interactions.
DIPiDIP-29256N.
IntActiP42260. 3 interactions.
MINTiMINT-8359884.
STRINGi10116.ENSRNOP00000000415.

Structurei

Secondary structure

1
908
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 4714Combined sources
Helixi52 – 6615Combined sources
Beta strandi68 – 8417Combined sources
Helixi88 – 10114Combined sources
Helixi112 – 12413Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi145 – 1517Combined sources
Helixi153 – 16614Combined sources
Beta strandi170 – 1789Combined sources
Helixi180 – 1845Combined sources
Helixi186 – 1894Combined sources
Helixi191 – 1933Combined sources
Beta strandi198 – 2036Combined sources
Helixi208 – 2114Combined sources
Helixi212 – 2209Combined sources
Beta strandi225 – 2306Combined sources
Helixi232 – 24413Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi253 – 2564Combined sources
Helixi261 – 2633Combined sources
Turni267 – 2715Combined sources
Beta strandi275 – 2806Combined sources
Helixi287 – 29812Combined sources
Beta strandi309 – 3113Combined sources
Helixi318 – 33518Combined sources
Beta strandi347 – 3493Combined sources
Helixi356 – 36510Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi373 – 3764Combined sources
Turni379 – 3813Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi389 – 3957Combined sources
Beta strandi398 – 4069Combined sources
Turni407 – 4093Combined sources
Beta strandi410 – 4134Combined sources
Turni425 – 4284Combined sources
Beta strandi433 – 4375Combined sources
Turni441 – 4433Combined sources
Beta strandi444 – 4463Combined sources
Helixi455 – 4584Combined sources
Beta strandi459 – 4613Combined sources
Helixi462 – 47413Combined sources
Beta strandi478 – 4825Combined sources
Turni493 – 4953Combined sources
Helixi500 – 5067Combined sources
Beta strandi511 – 5133Combined sources
Helixi521 – 5244Combined sources
Beta strandi527 – 5293Combined sources
Beta strandi533 – 5364Combined sources
Beta strandi538 – 5447Combined sources
Beta strandi665 – 6673Combined sources
Helixi671 – 6755Combined sources
Beta strandi678 – 6858Combined sources
Helixi689 – 6968Combined sources
Helixi700 – 71112Combined sources
Helixi713 – 7164Combined sources
Beta strandi717 – 7204Combined sources
Helixi721 – 73010Combined sources
Beta strandi731 – 7388Combined sources
Helixi739 – 74810Combined sources
Beta strandi752 – 7576Combined sources
Beta strandi762 – 7643Combined sources
Beta strandi767 – 7693Combined sources
Helixi774 – 78714Combined sources
Helixi790 – 79910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP42260.
SMRiP42260. Positions 423-546, 668-804.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42260.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni516 – 5183Glutamate binding
Regioni689 – 6902Glutamate binding

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

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiP42260.
KOiK05202.
PhylomeDBiP42260.

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.

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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti567 – 5671I → C in RNA edited version.
Natural varianti571 – 5711Y → C in RNA edited version.
Natural varianti621 – 6211Q → R in RNA edited version.

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P42260.
SMRi P42260. Positions 423-546, 668-804.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248480. 3 interactions.
DIPi DIP-29256N.
IntActi P42260. 3 interactions.
MINTi MINT-8359884.
STRINGi 10116.ENSRNOP00000000415.

Chemistry

BindingDBi P42260.
ChEMBLi CHEMBL3038481.
GuidetoPHARMACOLOGYi 451.

Protein family/group databases

TCDBi 1.A.10.1.11. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P42260.

Proteomic databases

PaxDbi P42260.
PRIDEi P42260.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000076234 ; ENSRNOP00000068172 ; ENSRNOG00000000368 .
GeneIDi 54257.
KEGGi rno:54257.
UCSCi RGD:2733. rat.

Organism-specific databases

CTDi 2898.
RGDi 2733. Grik2.

Phylogenomic databases

eggNOGi NOG316680.
GeneTreei ENSGT00760000118920.
HOGENOMi HOG000234371.
HOVERGENi HBG051839.
InParanoidi P42260.
KOi K05202.
PhylomeDBi P42260.

Miscellaneous databases

EvolutionaryTracei P42260.
NextBioi 610770.
PROi P42260.

Gene expression databases

ExpressionAtlasi P42260. baseline.
Genevestigatori P42260.

Family and domain databases

InterProi IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view ]
PRINTSi PR00177. NMDARECEPTOR.
SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
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Publicationsi

  1. "Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA."
    Egebjerg J., Bettler B., Hermans-Borgmeyer I., Heinemann S.F.
    Nature 351:745-748(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "High-affinity kainate and domoate receptors in rat brain."
    Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.
    FEBS Lett. 307:139-143(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Determinants of Ca2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: diversity by RNA editing."
    Koehler M., Burnashev N., Sakmann B., Seeburg P.H.
    Neuron 10:491-500(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, RNA EDITING.
    Tissue: Brain.
  4. Cited for: INTERACTION WITH DLG4.
  5. "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway."
    Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J.
    J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLHL17, UBIQUITINATION, MUTAGENESIS OF VAL-883 AND ILE-884.
  6. "SUMOylation regulates kainate-receptor-mediated synaptic transmission."
    Martin S., Nishimune A., Mellor J.R., Henley J.M.
    Nature 447:321-325(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-886, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-886.
  7. Cited for: INTERACTION WITH NETO2.
  8. "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity."
    Mayer M.L.
    Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEXES WITH GLUTAMATE; KAINATE; METHYLGLUTAMATE AND QUISQUALATE.
  9. "Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid."
    Nanao M.H., Green T., Stern-Bach Y., Heinemann S.F., Choe S.
    Proc. Natl. Acad. Sci. U.S.A. 102:1708-1713(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 419-819 IN COMPLEX WITH DOMOATE, SUBUNIT, GLYCOSYLATION AT ASN-423 AND ASN-751.
  10. "Conformational restriction blocks glutamate receptor desensitization."
    Weston M.C., Schuck P., Ghosal A., Rosenmund C., Mayer M.L.
    Nat. Struct. Mol. Biol. 13:1120-1127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 663-806, FUNCTION, SUBUNIT.
  11. "Structure and assembly mechanism for heteromeric kainate receptors."
    Kumar J., Schuck P., Mayer M.L.
    Neuron 71:319-331(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 32-420 IN COMPLEX WITH GRIK5, DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-378 AND ASN-412, SUBUNIT.
+Additional computationally mapped references.

Entry informationi

Entry nameiGRIK2_RAT
AccessioniPrimary (citable) accession number: P42260
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: January 7, 2015
This is version 137 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 domoate > kainate > quisqualate > glutamate. It does not bind AMPA without coexpression with GRIK5.

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

External Data

Dasty 3

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 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.
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