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Glutamate receptor ionotropic, kainate 1 (GluK1) (Glutamate receptor 5) (GluR-5) (GluR5)

 GRIK1_RAT               Reviewed;         949 AA.
P22756;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 3.
23-MAY-2018, entry version 183.
RecName: Full=Glutamate receptor ionotropic, kainate 1;
Short=GluK1;
AltName: Full=Glutamate receptor 5;
Short=GluR-5;
Short=GluR5;
Flags: Precursor;
Name=Grik1; Synonyms=Glur5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1373382;
Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B.,
Seeburg P.H.;
"A glutamate receptor channel with high affinity for domoate and
kainate.";
EMBO J. 11:1651-1656(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1977421; DOI=10.1016/0896-6273(90)90213-Y;
Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A.,
Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.;
"Cloning of a novel glutamate receptor subunit, GluR5: expression in
the nervous system during development.";
Neuron 5:583-595(1990).
[3]
INTERACTION WITH KLHL17.
PubMed=17062563; DOI=10.1074/jbc.M608194200;
Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y.,
Li M., Singer J.D., Marshall J.;
"Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate
receptor subunits to the ubiquitin-proteasome pathway.";
J. Biol. Chem. 281:40164-40173(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1322826; DOI=10.1016/0014-5793(92)80753-4;
Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B.,
Seeburg P.H.;
"High-affinity kainate and domoate receptors in rat brain.";
FEBS Lett. 307:139-143(1992).
[5]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH
GLUTAMATE, AND SUBUNIT.
PubMed=15710405; DOI=10.1016/j.febslet.2005.01.012;
Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M.,
Kastrup J.S.;
"Crystal structure of the kainate receptor GluR5 ligand-binding core
in complex with (S)-glutamate.";
FEBS Lett. 579:1154-1160(2005).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH
GLUTAMATE.
PubMed=15721240; DOI=10.1016/j.neuron.2005.01.031;
Mayer M.L.;
"Crystal structures of the GluR5 and GluR6 ligand binding cores:
molecular mechanisms underlying kainate receptor selectivity.";
Neuron 45:539-552(2005).
[7]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH
UBP302 AND UBP310, FUNCTION, AND SUBUNIT.
PubMed=16540562; DOI=10.1523/JNEUROSCI.0123-06.2005;
Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.;
"Crystal structures of the kainate receptor GluR5 ligand binding core
dimer with novel GluR5-selective antagonists.";
J. Neurosci. 26:2852-2861(2006).
-!- 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.
{ECO:0000269|PubMed:16540562}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers (Probable). The unedited version (Q) assembles into a
functional kainate-gated homomeric channel, whereas the edited
version (R) is unable to produce channel activity when expressed
alone. Both edited and unedited versions can form functional
channels with GRIK4 and GRIK5. Interacts with KLHL17.
{ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240,
ECO:0000269|PubMed:16540562, ECO:0000269|PubMed:17062563,
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=4;
Comment=Additional isoforms seem to exist.;
Name=Glur5-2C;
IsoId=P22756-1; Sequence=Displayed;
Name=Glur5-2;
IsoId=P22756-2; Sequence=VSP_000129, VSP_000130;
Name=Glur5-2A;
IsoId=P22756-3; Sequence=VSP_000131, VSP_000132;
Name=Glur5-2B; Synonyms=Glur5-1;
IsoId=P22756-4; Sequence=VSP_000130;
-!- TISSUE SPECIFICITY: Expressed in subsets of neurons throughout the
developing and adult central and peripheral nervous systems. In
the CNS principally in the medial amygdaloid nuclei, medial
habenulae, pyriform and cingulate cortices, and Purkinje cell
layer. Also highly expressed in embryonic and adult dorsal root
ganglia.
-!- RNA EDITING: Modified_positions=636; Note=Partially edited.;
-!- 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 > L-glutamate =
quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIK1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M83560; AAA02873.1; -; mRNA.
EMBL; M83561; AAA02874.1; -; mRNA.
EMBL; Z11712; CAA77775.1; -; mRNA.
EMBL; Z11713; CAA77776.1; -; mRNA.
EMBL; Z11714; CAA77777.1; -; mRNA.
PIR; S19808; S19808.
RefSeq; NP_001104584.1; NM_001111114.1.
RefSeq; NP_001104587.1; NM_001111117.1.
RefSeq; NP_058937.1; NM_017241.2.
UniGene; Rn.10449; -.
PDB; 1TXF; X-ray; 2.10 A; A=446-559, A=682-821.
PDB; 1VSO; X-ray; 1.85 A; A=445-559, A=682-820.
PDB; 1YCJ; X-ray; 1.95 A; A/B=445-559.
PDB; 2F34; X-ray; 1.74 A; A/B=446-559, A/B=682-821.
PDB; 2F35; X-ray; 1.87 A; A/B=446-559, A/B=682-821.
PDB; 2F36; X-ray; 2.11 A; A/B/C/D=446-559, A/B/C/D=682-821.
PDB; 2OJT; X-ray; 1.95 A; A/B=446-559, A/B=682-821.
PDB; 2PBW; X-ray; 2.50 A; A/B=445-559, A/B=682-820.
PDB; 2QS1; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
PDB; 2QS2; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
PDB; 2QS3; X-ray; 1.76 A; A/B=446-559, A/B=682-821.
PDB; 2QS4; X-ray; 1.58 A; A/B/C/D=446-559, A/B/C/D=682-821.
PDB; 2WKY; X-ray; 2.20 A; A/B=445-559, A/B=667-806.
PDB; 3C31; X-ray; 1.49 A; A/B=446-559, A/B=682-821.
PDB; 3C32; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
PDB; 3C33; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
PDB; 3C34; X-ray; 1.82 A; A/B=446-559, A/B=682-821.
PDB; 3C35; X-ray; 1.97 A; A/B=446-559, A/B=682-821.
PDB; 3C36; X-ray; 1.68 A; A/B=446-559, A/B=682-821.
PDB; 3GBA; X-ray; 1.35 A; A/B/C/D=445-559, A/B/C/D=667-820.
PDB; 3GBB; X-ray; 2.10 A; A/B=445-559, A/B=682-820.
PDB; 3S2V; X-ray; 2.50 A; A/B=445-559, A/B=667-805.
PDB; 4DLD; X-ray; 2.00 A; A/B=445-559, A/B=667-805.
PDB; 4E0X; X-ray; 2.00 A; A/B=682-820.
PDB; 4QF9; X-ray; 2.28 A; A/B/C=445-559, A/B/C=682-820.
PDB; 4YMB; X-ray; 1.93 A; A/B=445-559, A/B=682-820.
PDB; 5M2V; X-ray; 3.18 A; A/B=445-559, A/B=682-820.
PDB; 5MFQ; X-ray; 1.90 A; A/B=445-559, A/B=583-818.
PDB; 5MFV; X-ray; 2.18 A; A/B=445-559, A/B=583-818.
PDB; 5MFW; X-ray; 2.10 A; A/B=445-559, A/B=583-818.
PDB; 5NEB; X-ray; 2.05 A; A/B=445-559, A/B=682-820.
PDB; 5NF5; X-ray; 2.85 A; A/B=445-559, A/B=682-820.
PDBsum; 1TXF; -.
PDBsum; 1VSO; -.
PDBsum; 1YCJ; -.
PDBsum; 2F34; -.
PDBsum; 2F35; -.
PDBsum; 2F36; -.
PDBsum; 2OJT; -.
PDBsum; 2PBW; -.
PDBsum; 2QS1; -.
PDBsum; 2QS2; -.
PDBsum; 2QS3; -.
PDBsum; 2QS4; -.
PDBsum; 2WKY; -.
PDBsum; 3C31; -.
PDBsum; 3C32; -.
PDBsum; 3C33; -.
PDBsum; 3C34; -.
PDBsum; 3C35; -.
PDBsum; 3C36; -.
PDBsum; 3GBA; -.
PDBsum; 3GBB; -.
PDBsum; 3S2V; -.
PDBsum; 4DLD; -.
PDBsum; 4E0X; -.
PDBsum; 4QF9; -.
PDBsum; 4YMB; -.
PDBsum; 5M2V; -.
PDBsum; 5MFQ; -.
PDBsum; 5MFV; -.
PDBsum; 5MFW; -.
PDBsum; 5NEB; -.
PDBsum; 5NF5; -.
ProteinModelPortal; P22756; -.
SMR; P22756; -.
BioGrid; 248193; 3.
CORUM; P22756; -.
DIP; DIP-29257N; -.
STRING; 10116.ENSRNOP00000045594; -.
BindingDB; P22756; -.
ChEMBL; CHEMBL2919; -.
GuidetoPHARMACOLOGY; 450; -.
TCDB; 1.A.10.1.5; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P22756; -.
PhosphoSitePlus; P22756; -.
PaxDb; P22756; -.
PRIDE; P22756; -.
GeneID; 29559; -.
KEGG; rno:29559; -.
UCSC; RGD:2732; rat. [P22756-1]
CTD; 2897; -.
RGD; 2732; Grik1.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
HOGENOM; HOG000234371; -.
HOVERGEN; HBG051839; -.
InParanoid; P22756; -.
KO; K05201; -.
PhylomeDB; P22756; -.
EvolutionaryTrace; P22756; -.
PRO; PR:P22756; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:RGD.
GO; GO:0016595; F:glutamate binding; IDA:RGD.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:RGD.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:RGD.
GO; GO:0007399; P:nervous system development; IMP:RGD.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:RGD.
GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:RGD.
GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
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;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 949 Glutamate receptor ionotropic, kainate 1.
/FTId=PRO_0000011543.
TOPO_DOM 31 576 Extracellular. {ECO:0000255}.
TRANSMEM 577 597 Helical. {ECO:0000255}.
TOPO_DOM 598 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 674 Helical. {ECO:0000255}.
TOPO_DOM 675 834 Extracellular. {ECO:0000255}.
TRANSMEM 835 855 Helical. {ECO:0000255}.
TOPO_DOM 856 949 Cytoplasmic. {ECO:0000255}.
REGION 531 533 Glutamate binding.
REGION 704 705 Glutamate binding.
BINDING 538 538 Glutamate. {ECO:0000269|PubMed:15710405,
ECO:0000269|PubMed:15721240}.
BINDING 753 753 Glutamate. {ECO:0000269|PubMed:15710405,
ECO:0000269|PubMed:15721240}.
MOD_RES 725 725 Phosphoserine; by PKC. {ECO:0000255}.
MOD_RES 761 761 Phosphothreonine; by PKC. {ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 402 416 Missing (in isoform Glur5-2).
{ECO:0000305}.
/FTId=VSP_000129.
VAR_SEQ 870 898 Missing (in isoform Glur5-2B and isoform
Glur5-2). {ECO:0000305}.
/FTId=VSP_000130.
VAR_SEQ 870 871 KG -> HY (in isoform Glur5-2A).
{ECO:0000305}.
/FTId=VSP_000131.
VAR_SEQ 872 949 Missing (in isoform Glur5-2A).
{ECO:0000305}.
/FTId=VSP_000132.
VARIANT 636 636 Q -> R (in RNA edited version).
CONFLICT 282 282 K -> L (in Ref. 2; AAA02874).
{ECO:0000305}.
CONFLICT 354 355 CA -> WR (in Ref. 2; AAA02874).
{ECO:0000305}.
CONFLICT 477 477 A -> G (in Ref. 2; AAA02874).
{ECO:0000305}.
STRAND 449 453 {ECO:0000244|PDB:3GBA}.
TURN 457 459 {ECO:0000244|PDB:3GBA}.
STRAND 460 462 {ECO:0000244|PDB:3GBA}.
HELIX 471 474 {ECO:0000244|PDB:3GBA}.
STRAND 475 477 {ECO:0000244|PDB:3GBA}.
HELIX 478 490 {ECO:0000244|PDB:3GBA}.
STRAND 494 498 {ECO:0000244|PDB:3GBA}.
HELIX 515 521 {ECO:0000244|PDB:3GBA}.
STRAND 526 528 {ECO:0000244|PDB:3GBA}.
HELIX 536 539 {ECO:0000244|PDB:3GBA}.
STRAND 542 544 {ECO:0000244|PDB:3GBA}.
STRAND 548 551 {ECO:0000244|PDB:3GBA}.
STRAND 553 559 {ECO:0000244|PDB:3GBA}.
HELIX 686 690 {ECO:0000244|PDB:3GBA}.
STRAND 693 698 {ECO:0000244|PDB:3GBA}.
HELIX 704 711 {ECO:0000244|PDB:3GBA}.
HELIX 715 724 {ECO:0000244|PDB:3GBA}.
HELIX 727 729 {ECO:0000244|PDB:5NEB}.
STRAND 731 735 {ECO:0000244|PDB:3GBA}.
HELIX 736 745 {ECO:0000244|PDB:3GBA}.
STRAND 746 753 {ECO:0000244|PDB:3GBA}.
HELIX 754 763 {ECO:0000244|PDB:3GBA}.
STRAND 767 771 {ECO:0000244|PDB:3GBA}.
STRAND 777 779 {ECO:0000244|PDB:3GBA}.
STRAND 782 784 {ECO:0000244|PDB:3GBA}.
HELIX 789 802 {ECO:0000244|PDB:3GBA}.
HELIX 805 813 {ECO:0000244|PDB:3GBA}.
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


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