ID   GRIK1_RAT               Reviewed;         949 AA.
AC   P22756;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   27-MAR-2024, entry version 211.
DE   RecName: Full=Glutamate receptor ionotropic, kainate 1;
DE            Short=GluK1;
DE   AltName: Full=Glutamate receptor 5;
DE            Short=GluR-5;
DE            Short=GluR5;
DE   Flags: Precursor;
GN   Name=Grik1; Synonyms=Glur5;
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], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=1373382; DOI=10.1002/j.1460-2075.1992.tb05211.x;
RA   Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B.,
RA   Seeburg P.H.;
RT   "A glutamate receptor channel with high affinity for domoate and kainate.";
RL   EMBO J. 11:1651-1656(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1977421; DOI=10.1016/0896-6273(90)90213-y;
RA   Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A.,
RA   Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.;
RT   "Cloning of a novel glutamate receptor subunit, GluR5: expression in the
RT   nervous system during development.";
RL   Neuron 5:583-595(1990).
RN   [3]
RP   INTERACTION WITH KLHL17.
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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH
RP   GLUTAMATE, AND SUBUNIT.
RX   PubMed=15710405; DOI=10.1016/j.febslet.2005.01.012;
RA   Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S.;
RT   "Crystal structure of the kainate receptor GluR5 ligand-binding core in
RT   complex with (S)-glutamate.";
RL   FEBS Lett. 579:1154-1160(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302
RP   AND UBP310, FUNCTION, AND SUBUNIT.
RX   PubMed=16540562; DOI=10.1523/jneurosci.0123-06.2005;
RA   Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.;
RT   "Crystal structures of the kainate receptor GluR5 ligand binding core dimer
RT   with novel GluR5-selective antagonists.";
RL   J. Neurosci. 26:2852-2861(2006).
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. May be involved
CC       in the transmission of light information from the retina to the
CC       hypothalamus. {ECO:0000269|PubMed:16540562}.
CC   -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC       receptor subunits. Tetramers may be formed by the dimerization of
CC       dimers (Probable). The unedited version (Q) assembles into a functional
CC       kainate-gated homomeric channel, whereas the edited version (R) is
CC       unable to produce channel activity when expressed alone. Both edited
CC       and unedited versions can form functional channels with GRIK4 and
CC       GRIK5. Interacts with KLHL17. {ECO:0000269|PubMed:15710405,
CC       ECO:0000269|PubMed:15721240, ECO:0000269|PubMed:16540562,
CC       ECO:0000269|PubMed:17062563, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Postsynaptic cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=Glur5-2C;
CC         IsoId=P22756-1; Sequence=Displayed;
CC       Name=Glur5-2;
CC         IsoId=P22756-2; Sequence=VSP_000129, VSP_000130;
CC       Name=Glur5-2A;
CC         IsoId=P22756-3; Sequence=VSP_000131, VSP_000132;
CC       Name=Glur5-2B; Synonyms=Glur5-1;
CC         IsoId=P22756-4; Sequence=VSP_000130;
CC   -!- TISSUE SPECIFICITY: Expressed in subsets of neurons throughout the
CC       developing and adult central and peripheral nervous systems. In the CNS
CC       principally in the medial amygdaloid nuclei, medial habenulae, pyriform
CC       and cingulate cortices, and Purkinje cell layer. Also highly expressed
CC       in embryonic and adult dorsal root ganglia.
CC   -!- RNA EDITING: Modified_positions=636; Note=Partially edited.;
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 > L-glutamate =
CC       quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. GRIK1 subfamily. {ECO:0000305}.
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DR   EMBL; M83560; AAA02873.1; -; mRNA.
DR   EMBL; M83561; AAA02874.1; -; mRNA.
DR   EMBL; Z11712; CAA77775.1; -; mRNA.
DR   EMBL; Z11713; CAA77776.1; -; mRNA.
DR   EMBL; Z11714; CAA77777.1; -; mRNA.
DR   PIR; S19808; S19808.
DR   RefSeq; NP_001104584.1; NM_001111114.1.
DR   RefSeq; NP_001104587.1; NM_001111117.1.
DR   RefSeq; NP_058937.1; NM_017241.2.
DR   PDB; 1TXF; X-ray; 2.10 A; A=446-559, A=682-821.
DR   PDB; 1VSO; X-ray; 1.85 A; A=445-559, A=682-820.
DR   PDB; 1YCJ; X-ray; 1.95 A; A/B=445-559.
DR   PDB; 2F34; X-ray; 1.74 A; A/B=446-559, A/B=682-821.
DR   PDB; 2F35; X-ray; 1.87 A; A/B=446-559, A/B=682-821.
DR   PDB; 2F36; X-ray; 2.11 A; A/B/C/D=446-559, A/B/C/D=682-821.
DR   PDB; 2OJT; X-ray; 1.95 A; A/B=446-559, A/B=682-821.
DR   PDB; 2PBW; X-ray; 2.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 2QS1; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
DR   PDB; 2QS2; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
DR   PDB; 2QS3; X-ray; 1.76 A; A/B=446-559, A/B=682-821.
DR   PDB; 2QS4; X-ray; 1.58 A; A/B/C/D=446-559, A/B/C/D=682-821.
DR   PDB; 2WKY; X-ray; 2.20 A; A/B=445-559, A/B=667-806.
DR   PDB; 3C31; X-ray; 1.49 A; A/B=446-559, A/B=682-821.
DR   PDB; 3C32; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
DR   PDB; 3C33; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
DR   PDB; 3C34; X-ray; 1.82 A; A/B=446-559, A/B=682-821.
DR   PDB; 3C35; X-ray; 1.97 A; A/B=446-559, A/B=682-821.
DR   PDB; 3C36; X-ray; 1.68 A; A/B=446-559, A/B=682-821.
DR   PDB; 3GBA; X-ray; 1.35 A; A/B/C/D=445-559, A/B/C/D=667-820.
DR   PDB; 3GBB; X-ray; 2.10 A; A/B=445-559, A/B=682-820.
DR   PDB; 3S2V; X-ray; 2.50 A; A/B=445-559, A/B=667-805.
DR   PDB; 4DLD; X-ray; 2.00 A; A/B=445-559, A/B=667-805.
DR   PDB; 4E0X; X-ray; 2.00 A; A/B=682-820.
DR   PDB; 4QF9; X-ray; 2.28 A; A/B/C=445-559, A/B/C=682-820.
DR   PDB; 4YMB; X-ray; 1.93 A; A/B=445-559, A/B=682-820.
DR   PDB; 5M2V; X-ray; 3.18 A; A/B=445-559, A/B=682-820.
DR   PDB; 5MFQ; X-ray; 1.90 A; A/B=445-559, A/B=583-818.
DR   PDB; 5MFV; X-ray; 2.18 A; A/B=445-559, A/B=583-818.
DR   PDB; 5MFW; X-ray; 2.10 A; A/B=445-559, A/B=583-818.
DR   PDB; 5NEB; X-ray; 2.05 A; A/B=445-559, A/B=682-820.
DR   PDB; 5NF5; X-ray; 2.85 A; A/B=445-559, A/B=682-820.
DR   PDB; 6FZ4; X-ray; 1.85 A; A=445-559, A=682-820.
DR   PDB; 6SBT; X-ray; 2.30 A; A=445-559, A=682-820.
DR   PDB; 7LVT; EM; 4.60 A; A/B/C/D=36-949.
DR   PDBsum; 1TXF; -.
DR   PDBsum; 1VSO; -.
DR   PDBsum; 1YCJ; -.
DR   PDBsum; 2F34; -.
DR   PDBsum; 2F35; -.
DR   PDBsum; 2F36; -.
DR   PDBsum; 2OJT; -.
DR   PDBsum; 2PBW; -.
DR   PDBsum; 2QS1; -.
DR   PDBsum; 2QS2; -.
DR   PDBsum; 2QS3; -.
DR   PDBsum; 2QS4; -.
DR   PDBsum; 2WKY; -.
DR   PDBsum; 3C31; -.
DR   PDBsum; 3C32; -.
DR   PDBsum; 3C33; -.
DR   PDBsum; 3C34; -.
DR   PDBsum; 3C35; -.
DR   PDBsum; 3C36; -.
DR   PDBsum; 3GBA; -.
DR   PDBsum; 3GBB; -.
DR   PDBsum; 3S2V; -.
DR   PDBsum; 4DLD; -.
DR   PDBsum; 4E0X; -.
DR   PDBsum; 4QF9; -.
DR   PDBsum; 4YMB; -.
DR   PDBsum; 5M2V; -.
DR   PDBsum; 5MFQ; -.
DR   PDBsum; 5MFV; -.
DR   PDBsum; 5MFW; -.
DR   PDBsum; 5NEB; -.
DR   PDBsum; 5NF5; -.
DR   PDBsum; 6FZ4; -.
DR   PDBsum; 6SBT; -.
DR   PDBsum; 7LVT; -.
DR   AlphaFoldDB; P22756; -.
DR   EMDB; EMD-23017; -.
DR   EMDB; EMD-23542; -.
DR   SMR; P22756; -.
DR   BioGRID; 248193; 3.
DR   CORUM; P22756; -.
DR   DIP; DIP-29257N; -.
DR   STRING; 10116.ENSRNOP00000045594; -.
DR   BindingDB; P22756; -.
DR   ChEMBL; CHEMBL2919; -.
DR   DrugCentral; P22756; -.
DR   GuidetoPHARMACOLOGY; 450; -.
DR   TCDB; 1.A.10.1.5; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR   GlyCosmos; P22756; 9 sites, No reported glycans.
DR   GlyGen; P22756; 9 sites.
DR   iPTMnet; P22756; -.
DR   PhosphoSitePlus; P22756; -.
DR   jPOST; P22756; -.
DR   PaxDb; 10116-ENSRNOP00000045594; -.
DR   GeneID; 29559; -.
DR   KEGG; rno:29559; -.
DR   UCSC; RGD:2732; rat. [P22756-1]
DR   AGR; RGD:2732; -.
DR   CTD; 2897; -.
DR   RGD; 2732; Grik1.
DR   eggNOG; KOG1052; Eukaryota.
DR   InParanoid; P22756; -.
DR   OrthoDB; 511851at2759; -.
DR   PhylomeDB; P22756; -.
DR   Reactome; R-RNO-451307; Activation of Na-permeable kainate receptors.
DR   Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR   EvolutionaryTrace; P22756; -.
DR   PRO; PR:P22756; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:RGD.
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; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR   GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:RGD.
DR   GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR   GO; GO:0004970; F:glutamate-gated receptor activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
DR   GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
DR   GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0030534; P:adult behavior; ISO:RGD.
DR   GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR   GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; ISO:RGD.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:RGD.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR   GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:RGD.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:RGD.
DR   GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:RGD.
DR   GO; GO:0007399; P:nervous system development; IMP:RGD.
DR   GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:RGD.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:RGD.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; 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; IDA:RGD.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR   CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF36; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 1; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW   RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..949
FT                   /note="Glutamate receptor ionotropic, kainate 1"
FT                   /id="PRO_0000011543"
FT   TOPO_DOM        31..576
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..653
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        654..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        675..834
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        835..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        856..949
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         531..533
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   BINDING         538
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000269|PubMed:15710405,
FT                   ECO:0000269|PubMed:15721240"
FT   BINDING         704..705
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT   BINDING         753
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000269|PubMed:15710405,
FT                   ECO:0000269|PubMed:15721240"
FT   MOD_RES         725
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         761
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         402..416
FT                   /note="Missing (in isoform Glur5-2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000129"
FT   VAR_SEQ         870..898
FT                   /note="Missing (in isoform Glur5-2B and isoform Glur5-2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000130"
FT   VAR_SEQ         870..871
FT                   /note="KG -> HY (in isoform Glur5-2A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000131"
FT   VAR_SEQ         872..949
FT                   /note="Missing (in isoform Glur5-2A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000132"
FT   VARIANT         636
FT                   /note="Q -> R (in RNA edited version)"
FT   CONFLICT        282
FT                   /note="K -> L (in Ref. 2; AAA02874)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354..355
FT                   /note="CA -> WR (in Ref. 2; AAA02874)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477
FT                   /note="A -> G (in Ref. 2; AAA02874)"
FT                   /evidence="ECO:0000305"
FT   STRAND          449..453
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   TURN            457..459
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           471..474
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           478..490
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          494..498
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           515..521
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          526..528
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           536..539
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          548..551
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          553..559
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           686..690
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          693..698
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           704..711
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           715..724
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           726..729
FT                   /evidence="ECO:0007829|PDB:6FZ4"
FT   STRAND          731..735
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           736..745
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          746..753
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           754..763
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          767..771
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          777..779
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   STRAND          782..784
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           789..802
FT                   /evidence="ECO:0007829|PDB:3GBA"
FT   HELIX           805..813
FT                   /evidence="ECO:0007829|PDB:3GBA"
SQ   SEQUENCE   949 AA;  107840 MW;  020660BDD00054E0 CRC64;
     MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF
     AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ
     SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS
     TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL
     KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME
     RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF
     MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI
     WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL
     DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK
     VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
     PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL
     IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM
     WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG
     VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI
     VLAAGLVLSV FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL
     SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA
//