GRIK2_RAT
ID GRIK2_RAT Reviewed; 908 AA.
AC P42260;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Glutamate receptor ionotropic, kainate 2;
DE Short=GluK2;
DE AltName: Full=Glutamate receptor 6;
DE Short=GluR-6;
DE Short=GluR6;
DE Flags: Precursor;
GN Name=Grik2; Synonyms=Glur6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1648177; DOI=10.1038/351745a0;
RA Egebjerg J., Bettler B., Hermans-Borgmeyer I., Heinemann S.F.;
RT "Cloning of a cDNA for a glutamate receptor subunit activated by kainate
RT but not AMPA.";
RL Nature 351:745-748(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1322826; DOI=10.1016/0014-5793(92)80753-4;
RA Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.;
RT "High-affinity kainate and domoate receptors in rat brain.";
RL FEBS Lett. 307:139-143(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, AND RNA EDITING.
RC TISSUE=Brain;
RX PubMed=7681676; DOI=10.1016/0896-6273(93)90336-p;
RA Koehler M., Burnashev N., Sakmann B., Seeburg P.H.;
RT "Determinants of Ca2+ permeability in both TM1 and TM2 of high affinity
RT kainate receptor channels: diversity by RNA editing.";
RL Neuron 10:491-500(1993).
RN [4]
RP INTERACTION WITH DLG4.
RX PubMed=11744724; DOI=10.1074/jbc.m109453200;
RA Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P.,
RA Marshall J., Mierke D.F.;
RT "The PDZ1 domain of SAP90. Characterization of structure and binding.";
RL J. Biol. Chem. 277:6967-6973(2002).
RN [5]
RP INTERACTION WITH KLHL17, UBIQUITINATION, AND MUTAGENESIS OF VAL-883 AND
RP ILE-884.
RX PubMed=17062563; DOI=10.1074/jbc.m608194200;
RA Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M.,
RA Singer J.D., Marshall J.;
RT "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor
RT subunits to the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 281:40164-40173(2006).
RN [6]
RP SUMOYLATION AT LYS-886, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-886.
RX PubMed=17486098; DOI=10.1038/nature05736;
RA Martin S., Nishimune A., Mellor J.R., Henley J.M.;
RT "SUMOylation regulates kainate-receptor-mediated synaptic transmission.";
RL Nature 447:321-325(2007).
RN [7]
RP INTERACTION WITH NETO2.
RX PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
RA Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
RA Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
RA Tomita S.;
RT "A transmembrane accessory subunit that modulates kainate-type glutamate
RT receptors.";
RL Neuron 61:385-396(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEXES WITH
RP GLUTAMATE; KAINATE; METHYLGLUTAMATE AND QUISQUALATE.
RX PubMed=15721240; DOI=10.1016/j.neuron.2005.01.031;
RA Mayer M.L.;
RT "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular
RT mechanisms underlying kainate receptor selectivity.";
RL Neuron 45:539-552(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 419-819 IN COMPLEX WITH DOMOATE,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-423 AND ASN-751.
RX PubMed=15677325; DOI=10.1073/pnas.0409573102;
RA Nanao M.H., Green T., Stern-Bach Y., Heinemann S.F., Choe S.;
RT "Structure of the kainate receptor subunit GluR6 agonist-binding domain
RT complexed with domoic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1708-1713(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 663-806 IN COMPLEX WITH
RP GLUTAMATE, FUNCTION, AND SUBUNIT.
RX PubMed=17115050; DOI=10.1038/nsmb1178;
RA Weston M.C., Schuck P., Ghosal A., Rosenmund C., Mayer M.L.;
RT "Conformational restriction blocks glutamate receptor desensitization.";
RL Nat. Struct. Mol. Biol. 13:1120-1127(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 32-420 IN COMPLEX WITH GRIK5,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-378 AND ASN-412, AND SUBUNIT.
RX PubMed=21791290; DOI=10.1016/j.neuron.2011.05.038;
RA Kumar J., Schuck P., Mayer M.L.;
RT "Structure and assembly mechanism for heteromeric kainate receptors.";
RL Neuron 71:319-331(2011).
CC -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
CC excitatory neurotransmitter at many synapses in the central nervous
CC system. Binding of the excitatory neurotransmitter L-glutamate induces
CC a conformation change, leading to the opening of the cation channel,
CC and thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist (PubMed:17115050,
CC PubMed:17486098). Modulates cell surface expression of NETO2 (By
CC similarity). {ECO:0000250|UniProtKB:P39087,
CC ECO:0000269|PubMed:17115050, ECO:0000269|PubMed:17486098}.
CC -!- FUNCTION: Independent of its ionotropic glutamate receptor activity,
CC acts as a thermoreceptor conferring sensitivity to cold temperatures
CC (By similarity). Functions in dorsal root ganglion neurons (By
CC similarity). {ECO:0000250|UniProtKB:P39087}.
CC -!- ACTIVITY REGULATION: Cold receptor activity activated by temperatures
CC between 10-19 degrees Celsius. {ECO:0000250|UniProtKB:P39087}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. Assembles into a kainate-gated homomeric channel that does not
CC bind AMPA (By similarity). GRIK2 associated to GRIK5 forms functional
CC channels that can be gated by AMPA. Interacts with DLG4. Interacts with
CC NETO2. Interacts (via C-terminus) with KLHL17 (via kelch repeats); the
CC interaction targets GRIK2 for degradation via ubiquitin-proteasome
CC pathway. {ECO:0000250, ECO:0000269|PubMed:11744724,
CC ECO:0000269|PubMed:15677325, ECO:0000269|PubMed:17062563,
CC ECO:0000269|PubMed:17115050, ECO:0000269|PubMed:19217376,
CC ECO:0000269|PubMed:21791290}.
CC -!- INTERACTION:
CC P42260; P42260: Grik2; NbExp=10; IntAct=EBI-7809795, EBI-7809795;
CC P42260; Q66HA1: Map3k11; NbExp=2; IntAct=EBI-7809795, EBI-4279420;
CC P42260; O70260: Pias3; NbExp=3; IntAct=EBI-7809795, EBI-7974636;
CC P42260; Q5I0H3: Sumo1; NbExp=4; IntAct=EBI-7809795, EBI-7253100;
CC P42260; P63281: Ube2i; NbExp=3; IntAct=EBI-7809795, EBI-7974723;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17486098};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17486098}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:17486098}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:17486098}.
CC -!- TISSUE SPECIFICITY: Highest expression is found in the olfactory lobe,
CC piriform cortex, dentate gyrus, hippocampus, granular cell layer of the
CC cerebellum, and in caudate-putamen.
CC -!- PTM: Sumoylation mediates kainate receptor-mediated endocytosis and
CC regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and
CC desumoylated by SENP1. {ECO:0000269|PubMed:17486098}.
CC -!- PTM: Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the
CC synapse by leading kainate receptor degradation through proteasome.
CC {ECO:0000269|PubMed:17062563}.
CC -!- PTM: Phosphorylated by PKC at Ser-868 upon agonist activation, this
CC directly enhance sumoylation. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=567 {ECO:0000269|PubMed:7681676}, 571
CC {ECO:0000269|PubMed:7681676}, 621 {ECO:0000269|PubMed:7681676};
CC Note=Partially edited. The presence of Gln at position 621 (non-edited)
CC determines channels with low calcium permeability, whereas an arginine
CC residue (edited) determines a higher calcium permeability especially if
CC the preceding sites are fully edited. This receptor is nearly
CC completely edited in all gray matter structures (90% of the
CC receptors).;
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds domoate > kainate > quisqualate >
CC glutamate. It does not bind AMPA without coexpression with GRIK5.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK2 subfamily. {ECO:0000305}.
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DR EMBL; Z11548; CAA77647.1; -; mRNA.
DR EMBL; Z11715; CAA77778.1; -; mRNA.
DR PIR; S19098; S19098.
DR RefSeq; NP_062182.1; NM_019309.2.
DR PDB; 1S50; X-ray; 1.65 A; A=428-806.
DR PDB; 1S7Y; X-ray; 1.75 A; A/B=429-544, A/B=667-806.
DR PDB; 1S9T; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
DR PDB; 1SD3; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
DR PDB; 1TT1; X-ray; 1.93 A; A/B=429-806.
DR PDB; 1YAE; X-ray; 3.11 A; A/B/C/D/E/F=419-557, A/B/C/D/E/F=662-819.
DR PDB; 2I0B; X-ray; 1.96 A; A/B/C=429-544, A/B/C=667-806.
DR PDB; 2I0C; X-ray; 2.25 A; A/B=429-544, A/B=667-806.
DR PDB; 2XXR; X-ray; 1.60 A; A/B=429-544, A/B=667-806.
DR PDB; 2XXT; X-ray; 1.90 A; A/B=667-806.
DR PDB; 2XXU; X-ray; 1.50 A; A/B=667-806.
DR PDB; 2XXV; X-ray; 1.70 A; A/B=667-806.
DR PDB; 2XXW; X-ray; 2.30 A; A/B=667-806.
DR PDB; 2XXX; X-ray; 2.10 A; A/B/C/D=667-806.
DR PDB; 2XXY; X-ray; 3.00 A; A/B/C/D=667-806.
DR PDB; 3G3F; X-ray; 1.38 A; A/B=429-544, A/B=667-806.
DR PDB; 3G3G; X-ray; 1.30 A; A/B=429-544, A/B=667-806.
DR PDB; 3G3H; X-ray; 1.50 A; A/B=429-544, A/B=667-806.
DR PDB; 3G3I; X-ray; 1.37 A; A/B=429-544, A/B=667-806.
DR PDB; 3G3J; X-ray; 1.32 A; A/B=429-544, A/B=667-806.
DR PDB; 3G3K; X-ray; 1.24 A; A/B=429-544, A/B=667-806.
DR PDB; 3H6G; X-ray; 2.70 A; A/B=32-420.
DR PDB; 3H6H; X-ray; 2.90 A; A/B=32-420.
DR PDB; 3QLT; X-ray; 2.99 A; A/B=32-420.
DR PDB; 3QLU; X-ray; 2.91 A; C/D=32-420.
DR PDB; 3QLV; X-ray; 3.94 A; C/D/F/H/J=32-420.
DR PDB; 4BDL; X-ray; 1.75 A; A/B=429-544, A/B=667-806.
DR PDB; 4BDM; X-ray; 3.40 A; A/B/C/D=429-544, A/B/C/D=667-806.
DR PDB; 4BDN; X-ray; 2.50 A; A/B/C/D=429-544, A/B/C/D=667-806.
DR PDB; 4BDO; X-ray; 2.55 A; A/B/C/D=429-544, A/B/C/D=667-806.
DR PDB; 4BDQ; X-ray; 1.90 A; A/B=429-544, A/B=667-806.
DR PDB; 4BDR; X-ray; 1.65 A; A/B=429-544, A/B=667-806.
DR PDB; 4H8I; X-ray; 2.00 A; A/B=429-544, A/B=667-806.
DR PDB; 4UQQ; EM; 7.60 A; A/B/C/D=32-908.
DR PDB; 5CMK; X-ray; 1.80 A; A/B=429-544, A/B=667-806.
DR PDB; 5CMM; X-ray; 1.27 A; A=429-544.
DR PDB; 5KUF; EM; 3.80 A; A/B/C/D=32-908.
DR PDB; 5KUH; EM; 11.60 A; A/B/C/D=32-544, A/B/C/D=667-908.
DR PDB; 7F56; EM; 4.10 A; A/B/C/D=1-908.
DR PDB; 7F57; EM; 3.80 A; A/B/C/D=1-908.
DR PDB; 7F59; EM; 4.20 A; A/B/C/D=1-908.
DR PDB; 7F5A; EM; 6.40 A; A/B/C/D=1-908.
DR PDB; 7F5B; EM; 3.90 A; A/B/C/D=1-908.
DR PDB; 7KS0; EM; 5.30 A; B/D=1-908.
DR PDB; 7KS3; EM; 5.80 A; B/D=1-908.
DR PDBsum; 1S50; -.
DR PDBsum; 1S7Y; -.
DR PDBsum; 1S9T; -.
DR PDBsum; 1SD3; -.
DR PDBsum; 1TT1; -.
DR PDBsum; 1YAE; -.
DR PDBsum; 2I0B; -.
DR PDBsum; 2I0C; -.
DR PDBsum; 2XXR; -.
DR PDBsum; 2XXT; -.
DR PDBsum; 2XXU; -.
DR PDBsum; 2XXV; -.
DR PDBsum; 2XXW; -.
DR PDBsum; 2XXX; -.
DR PDBsum; 2XXY; -.
DR PDBsum; 3G3F; -.
DR PDBsum; 3G3G; -.
DR PDBsum; 3G3H; -.
DR PDBsum; 3G3I; -.
DR PDBsum; 3G3J; -.
DR PDBsum; 3G3K; -.
DR PDBsum; 3H6G; -.
DR PDBsum; 3H6H; -.
DR PDBsum; 3QLT; -.
DR PDBsum; 3QLU; -.
DR PDBsum; 3QLV; -.
DR PDBsum; 4BDL; -.
DR PDBsum; 4BDM; -.
DR PDBsum; 4BDN; -.
DR PDBsum; 4BDO; -.
DR PDBsum; 4BDQ; -.
DR PDBsum; 4BDR; -.
DR PDBsum; 4H8I; -.
DR PDBsum; 4UQQ; -.
DR PDBsum; 5CMK; -.
DR PDBsum; 5CMM; -.
DR PDBsum; 5KUF; -.
DR PDBsum; 5KUH; -.
DR PDBsum; 7F56; -.
DR PDBsum; 7F57; -.
DR PDBsum; 7F59; -.
DR PDBsum; 7F5A; -.
DR PDBsum; 7F5B; -.
DR PDBsum; 7KS0; -.
DR PDBsum; 7KS3; -.
DR AlphaFoldDB; P42260; -.
DR SMR; P42260; -.
DR BioGRID; 248480; 7.
DR DIP; DIP-29256N; -.
DR ELM; P42260; -.
DR IntAct; P42260; 5.
DR MINT; P42260; -.
DR STRING; 10116.ENSRNOP00000068172; -.
DR BindingDB; P42260; -.
DR ChEMBL; CHEMBL3607; -.
DR DrugCentral; P42260; -.
DR GuidetoPHARMACOLOGY; 451; -.
DR TCDB; 1.A.10.1.11; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P42260; 9 sites.
DR iPTMnet; P42260; -.
DR PhosphoSitePlus; P42260; -.
DR PaxDb; P42260; -.
DR Ensembl; ENSRNOT00000076234; ENSRNOP00000068172; ENSRNOG00000000368.
DR GeneID; 54257; -.
DR KEGG; rno:54257; -.
DR UCSC; RGD:2733; rat.
DR CTD; 2898; -.
DR RGD; 2733; Grik2.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000155610; -.
DR InParanoid; P42260; -.
DR OMA; VFAFDSV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P42260; -.
DR Reactome; R-RNO-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR EvolutionaryTrace; P42260; -.
DR PRO; PR:P42260; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000368; Expressed in cerebellum and 11 other tissues.
DR ExpressionAtlas; P42260; baseline and differential.
DR Genevisible; P42260; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:RGD.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:0120169; P:detection of cold stimulus involved in thermoception; ISS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:RGD.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
DR GO; GO:0046328; P:regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Isopeptide bond; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..908
FT /note="Glutamate receptor ionotropic, kainate 2"
FT /id="PRO_0000011546"
FT TOPO_DOM 32..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..819
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 516..518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15721240,
FT ECO:0000269|PubMed:17115050, ECO:0007744|PDB:1S50,
FT ECO:0007744|PDB:1S7Y, ECO:0007744|PDB:2I0B,
FT ECO:0007744|PDB:2I0C"
FT BINDING 523
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15721240,
FT ECO:0000269|PubMed:17115050, ECO:0007744|PDB:1S50,
FT ECO:0007744|PDB:1S7Y, ECO:0007744|PDB:2I0B,
FT ECO:0007744|PDB:2I0C"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15721240,
FT ECO:0000269|PubMed:17115050, ECO:0007744|PDB:1S50,
FT ECO:0007744|PDB:1S7Y, ECO:0007744|PDB:2I0B,
FT ECO:0007744|PDB:2I0C"
FT BINDING 738
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15721240,
FT ECO:0000269|PubMed:17115050, ECO:0007744|PDB:1S50,
FT ECO:0007744|PDB:1S7Y, ECO:0007744|PDB:2I0B,
FT ECO:0007744|PDB:2I0C"
FT MOD_RES 846
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT MOD_RES 868
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21791290"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21791290"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21791290"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15677325"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15677325"
FT DISULFID 96..347
FT /evidence="ECO:0000269|PubMed:21791290,
FT ECO:0007744|PDB:3QLT, ECO:0007744|PDB:3QLU,
FT ECO:0007744|PDB:3QLV"
FT CROSSLNK 886
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:17486098"
FT VARIANT 567
FT /note="I -> C (in RNA edited version)"
FT VARIANT 571
FT /note="Y -> C (in RNA edited version)"
FT VARIANT 621
FT /note="Q -> R (in RNA edited version)"
FT MUTAGEN 883
FT /note="V->A: Abolishes interaction with KLHL17. Abolishes
FT actinfilin-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17062563"
FT MUTAGEN 884
FT /note="I->A: Abolishes interaction with KLHL17. Abolishes
FT actinfilin-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17062563"
FT MUTAGEN 886
FT /note="K->R: Abolishes sumoylation. Loss of kainate-
FT mediated endocytosis."
FT /evidence="ECO:0000269|PubMed:17486098"
FT STRAND 34..47
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 68..84
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3QLT"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3H6G"
FT TURN 267..271
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:3H6G"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3QLT"
FT HELIX 318..335
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3H6H"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3H6G"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:3H6G"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:3H6G"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:3H6H"
FT TURN 425..428
FT /evidence="ECO:0007829|PDB:1YAE"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:3G3K"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:3G3K"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 689..696
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 700..711
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 713..716
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 721..730
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 731..738
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 739..748
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 752..757
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:3G3K"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 774..787
FT /evidence="ECO:0007829|PDB:3G3K"
FT HELIX 790..799
FT /evidence="ECO:0007829|PDB:3G3K"
SQ SEQUENCE 908 AA; 102470 MW; 7F430E2D8B2E982B 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 KIGTWDPASG 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
