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Glutamate receptor ionotropic, kainate 2 (GluK2) (Glutamate receptor 6) (GluR-6) (GluR6) (Glutamate receptor beta-2) (GluR beta-2)

 GRIK2_MOUSE             Reviewed;         908 AA.
P39087; Q60933;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 4.
12-SEP-2018, entry version 179.
RecName: Full=Glutamate receptor ionotropic, kainate 2;
Short=GluK2;
AltName: Full=Glutamate receptor 6;
Short=GluR-6;
Short=GluR6;
AltName: Full=Glutamate receptor beta-2;
Short=GluR beta-2;
Flags: Precursor;
Name=Grik2; Synonyms=Glur6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLUR6-2).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8260617;
Gregor P., O'Hara B.F., Yang X., Uhl G.R.;
"Expression and novel subunit isoforms of glutamate receptor genes
GluR5 and GluR6.";
NeuroReport 4:1343-1346(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-864 (ISOFORM GLUR6-2).
PubMed=1379666; DOI=10.1016/0169-328X(92)90023-5;
Morita T., Sakimura K., Kushiya E., Yamazaki M., Meguro H., Araki K.,
Abe T., Mori K.J., Mishina M.;
"Cloning and functional expression of a cDNA encoding the mouse beta 2
subunit of the kainate-selective glutamate receptor channel.";
Brain Res. Mol. Brain Res. 14:143-146(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 584-695, AND RNA EDITING OF
POSITION 621.
STRAIN=BALB/cJ;
PubMed=8700852; DOI=10.1073/pnas.93.5.1875;
Herb A., Higuchi M., Sprengel R., Seeburg P.H.;
"Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs
requires distant intronic sequences.";
Proc. Natl. Acad. Sci. U.S.A. 93:1875-1880(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, AND RNA EDITING OF POSITIONS
567; 571 AND 621.
TISSUE=Brain;
PubMed=7681676; DOI=10.1016/0896-6273(93)90336-P;
Koehler M., Burnashev N., Sakmann B., Seeburg P.H.;
"Determinants of Ca2+ permeability in both TM1 and TM2 of high
affinity kainate receptor channels: diversity by RNA editing.";
Neuron 10:491-500(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 855-908.
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
FUNCTION, AND INTERACTION WITH NETO2.
PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
Tomita S.;
"A transmembrane accessory subunit that modulates kainate-type
glutamate receptors.";
Neuron 61:385-396(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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. {ECO:0000269|PubMed:19217376}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers (Probable). Assembles into a kainate-gated homomeric
channel that does not bind AMPA. GRIK2 associated to GRIK5 forms
functional channels that can be gated by AMPA. Interacts with DLG4
(By similarity). Interacts (via C-terminus) with KLHL17 (via kelch
repeats); the interaction targets GRIK2 for degradation via
ubiquitin-proteasome pathway (By similarity). Interacts with
NETO2. {ECO:0000250, ECO:0000269|PubMed:19217376, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell junction, synapse, postsynaptic cell membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=GluR6 Beta2;
IsoId=P39087-1; Sequence=Displayed;
Name=GluR6-2;
IsoId=P39087-2; Sequence=VSP_000133;
-!- TISSUE SPECIFICITY: Most abundant in the cerebellum and the
hypothalamus.
-!- DEVELOPMENTAL STAGE: Expressed during brain development.
Expression drops in the adult.
-!- PTM: Sumoylation mediates kainate receptor-mediated endocytosis
and regulates synaptic transmission. Sumoylation is enhanced by
PIAS3 and desumoylated by SENP1 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at
the synapse by leading kainate receptor degradation through
proteasome (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by PKC at Ser-868 upon agonist activation,
this directly enhance sumoylation. {ECO:0000250}.
-!- RNA EDITING: Modified_positions=567 {ECO:0000269|PubMed:7681676},
571 {ECO:0000269|PubMed:7681676}, 621 {ECO:0000269|PubMed:7681676,
ECO:0000269|PubMed:8700852}; Note=Partially edited. The presence
of Gln at position 621 (non-edited) determines channels with low
calcium permeability, whereas Arg (edited) determines a higher
calcium permeability especially if the preceding sites are fully
edited (By similarity). {ECO:0000250};
-!- 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 > 6-
cyano-7-nitroquinoxaline-2,3-dione > L-glutamate = 6,7-
dinitroquinoxaline-2,3-dione > dihydrokainate (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIK2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X66117; CAA46907.1; -; mRNA.
EMBL; D10054; BAA00943.1; -; mRNA.
EMBL; U31443; AAA85221.1; -; Genomic_DNA.
EMBL; AC113305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS23830.1; -. [P39087-2]
CCDS; CCDS48554.1; -. [P39087-1]
PIR; A43954; A43954.
PIR; S35792; S35792.
RefSeq; XP_017169293.1; XM_017313804.1.
UniGene; Mm.185993; -.
UniGene; Mm.332838; -.
ProteinModelPortal; P39087; -.
SMR; P39087; -.
BioGrid; 200064; 7.
CORUM; P39087; -.
IntAct; P39087; 5.
MINT; P39087; -.
STRING; 10090.ENSMUSP00000101124; -.
iPTMnet; P39087; -.
PhosphoSitePlus; P39087; -.
SwissPalm; P39087; -.
MaxQB; P39087; -.
PaxDb; P39087; -.
PeptideAtlas; P39087; -.
PRIDE; P39087; -.
Ensembl; ENSMUST00000079751; ENSMUSP00000078687; ENSMUSG00000056073. [P39087-2]
Ensembl; ENSMUST00000105484; ENSMUSP00000101124; ENSMUSG00000056073. [P39087-1]
Ensembl; ENSMUST00000218441; ENSMUSP00000151671; ENSMUSG00000056073. [P39087-2]
Ensembl; ENSMUST00000218823; ENSMUSP00000151921; ENSMUSG00000056073. [P39087-1]
GeneID; 14806; -.
CTD; 2898; -.
MGI; MGI:95815; Grik2.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
GeneTree; ENSGT00910000143978; -.
HOGENOM; HOG000234371; -.
HOVERGEN; HBG051839; -.
InParanoid; P39087; -.
OMA; YFASHAQ; -.
OrthoDB; EOG091G02LN; -.
PhylomeDB; P39087; -.
TreeFam; TF334668; -.
Reactome; R-MMU-451307; Activation of Na-permeable kainate receptors.
Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
PRO; PR:P39087; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000056073; Expressed in 101 organ(s), highest expression level in lumbar subsegment of spinal cord.
ExpressionAtlas; P39087; baseline and differential.
Genevisible; P39087; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:MGI.
GO; GO:0032983; C:kainate selective glutamate receptor complex; IPI:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0043195; C:terminal bouton; ISO:MGI.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISS:UniProtKB.
GO; GO:0008066; F:glutamate receptor activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IMP:UniProtKB.
GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:MGI.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IGI:MGI.
GO; GO:0051402; P:neuron apoptotic process; ISO:MGI.
GO; GO:0019228; P:neuronal action potential; IMP:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
GO; GO:0043113; P:receptor clustering; ISO:MGI.
GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Isopeptide bond; Ligand-gated ion channel; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 908 Glutamate receptor ionotropic, kainate 2.
/FTId=PRO_0000011545.
TOPO_DOM 32 561 Extracellular. {ECO:0000255}.
TRANSMEM 562 582 Helical. {ECO:0000255}.
TOPO_DOM 583 638 Cytoplasmic. {ECO:0000255}.
TRANSMEM 639 659 Helical. {ECO:0000255}.
TOPO_DOM 660 819 Extracellular. {ECO:0000255}.
TRANSMEM 820 840 Helical. {ECO:0000255}.
TOPO_DOM 841 908 Cytoplasmic. {ECO:0000255}.
REGION 516 518 Glutamate binding. {ECO:0000250}.
REGION 689 690 Glutamate binding. {ECO:0000250}.
BINDING 523 523 Glutamate. {ECO:0000250}.
BINDING 738 738 Glutamate. {ECO:0000250}.
MOD_RES 846 846 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q13002}.
MOD_RES 868 868 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q13002}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 96 347 {ECO:0000250}.
CROSSLNK 886 886 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q13002}.
VAR_SEQ 855 908 RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHT
FNDRRLPGKETMA -> ESSIWLVPPYHPDTV (in
isoform GluR6-2).
{ECO:0000303|PubMed:1379666,
ECO:0000303|PubMed:8260617}.
/FTId=VSP_000133.
VARIANT 567 567 I -> V (in RNA edited version).
VARIANT 571 571 Y -> C (in RNA edited version).
VARIANT 621 621 Q -> R (in RNA edited version).
CONFLICT 611 611 S -> G (in Ref. 1; CAA46907).
{ECO:0000305}.
CONFLICT 849 864 NAQLEKRSFCSAMVEE -> TLNWKRGPSVAPWWKN (in
Ref. 2; BAA00943). {ECO:0000305}.
SEQUENCE 908 AA; 102486 MW; EF430E2D8E0A87D4 CRC64;
MKIISPVLSN LVFSRSIKVL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM GAEELAFRFA
VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS LGVAAIFGPS HSSSANAVQS
ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST
GLIRLQELIK APSRYNLRLK IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK
QALAMGMMTE YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER
LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH KPWRFGTRFM
SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE KIGTWDPSSG LNMTESQKGK
PANITDSLSN RSLIVTTILE EPYVLFKKSD KPLYGNDRFE GYCIDLLREL STILGFTYEI
RLVEDGKYGA QDDVNGQWNG MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI
LYRKPNGTNP GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT
VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS TYDKMWAFMS SRRQSVLVKS
NEEGIQRVLT SDYAFLMEST TIEFVTQRNC NLTQIGGLID SKGYGVGTPM GSPYRDKITI
AILQLQEEGK LHMMKEKWWR GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG
EFLYKSKKNA QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR
LPGKETMA


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