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Protein

Glutamate receptor ionotropic, kainate 1

Gene

Grik1

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

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.1 Publication

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei538Glutamate2 Publications1
Binding sitei753Glutamate2 Publications1

GO - Molecular functioni

  • drug binding Source: RGD
  • extracellularly glutamate-gated ion channel activity Source: RGD
  • glutamate binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • kainate selective glutamate receptor activity Source: RGD
  • protein homodimerization activity Source: RGD
  • voltage-gated cation channel activity Source: RGD

GO - Biological processi

  • chemical synaptic transmission Source: UniProtKB
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • negative regulation of synaptic transmission, GABAergic Source: RGD
  • negative regulation of synaptic transmission, glutamatergic Source: RGD
  • nervous system development Source: RGD
  • positive regulation of synaptic transmission, GABAergic Source: RGD
  • regulation of short-term neuronal synaptic plasticity Source: RGD
  • regulation of synaptic plasticity Source: UniProtKB

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Protein family/group databases

TCDBi1.A.10.1.5 the glutamate-gated ion channel (gic) family of neurotransmitter receptors

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, kainate 1
Short name:
GluK1
Alternative name(s):
Glutamate receptor 5
Short name:
GluR-5
Short name:
GluR5
Gene namesi
Name:Grik1
Synonyms:Glur5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2732 Grik1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 576ExtracellularSequence analysisAdd BLAST546
Transmembranei577 – 597HelicalSequence analysisAdd BLAST21
Topological domaini598 – 653CytoplasmicSequence analysisAdd BLAST56
Transmembranei654 – 674HelicalSequence analysisAdd BLAST21
Topological domaini675 – 834ExtracellularSequence analysisAdd BLAST160
Transmembranei835 – 855HelicalSequence analysisAdd BLAST21
Topological domaini856 – 949CytoplasmicSequence analysisAdd BLAST94

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2919
GuidetoPHARMACOLOGYi450

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001154331 – 949Glutamate receptor ionotropic, kainate 1Add BLAST919

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi68N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi276N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi379N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi428N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi439N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi561N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei725Phosphoserine; by PKCSequence analysis1
Modified residuei761Phosphothreonine; by PKCSequence analysis1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP22756
PRIDEiP22756

PTM databases

iPTMnetiP22756
PhosphoSitePlusiP22756

Expressioni

Tissue specificityi

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.

Interactioni

Subunit structurei

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.Curated4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248193, 3 interactors
CORUMiP22756
DIPiDIP-29257N
STRINGi10116.ENSRNOP00000045594

Chemistry databases

BindingDBiP22756

Structurei

Secondary structure

1949
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi449 – 453Combined sources5
Turni457 – 459Combined sources3
Beta strandi460 – 462Combined sources3
Helixi471 – 474Combined sources4
Beta strandi475 – 477Combined sources3
Helixi478 – 490Combined sources13
Beta strandi494 – 498Combined sources5
Helixi515 – 521Combined sources7
Beta strandi526 – 528Combined sources3
Helixi536 – 539Combined sources4
Beta strandi542 – 544Combined sources3
Beta strandi548 – 551Combined sources4
Beta strandi553 – 559Combined sources7
Helixi686 – 690Combined sources5
Beta strandi693 – 698Combined sources6
Helixi704 – 711Combined sources8
Helixi715 – 724Combined sources10
Helixi727 – 729Combined sources3
Beta strandi731 – 735Combined sources5
Helixi736 – 745Combined sources10
Beta strandi746 – 753Combined sources8
Helixi754 – 763Combined sources10
Beta strandi767 – 771Combined sources5
Beta strandi777 – 779Combined sources3
Beta strandi782 – 784Combined sources3
Helixi789 – 802Combined sources14
Helixi805 – 813Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TXFX-ray2.10A446-559[»]
A682-821[»]
1VSOX-ray1.85A445-559[»]
A682-820[»]
1YCJX-ray1.95A/B445-559[»]
2F34X-ray1.74A/B446-559[»]
A/B682-821[»]
2F35X-ray1.87A/B446-559[»]
A/B682-821[»]
2F36X-ray2.11A/B/C/D446-559[»]
A/B/C/D682-821[»]
2OJTX-ray1.95A/B446-559[»]
A/B682-821[»]
2PBWX-ray2.50A/B445-559[»]
A/B682-820[»]
2QS1X-ray1.80A/B446-559[»]
A/B682-821[»]
2QS2X-ray1.80A/B446-559[»]
A/B682-821[»]
2QS3X-ray1.76A/B446-559[»]
A/B682-821[»]
2QS4X-ray1.58A/B/C/D446-559[»]
A/B/C/D682-821[»]
2WKYX-ray2.20A/B445-559[»]
A/B667-806[»]
3C31X-ray1.49A/B446-559[»]
A/B682-821[»]
3C32X-ray1.72A/B446-559[»]
A/B682-821[»]
3C33X-ray1.72A/B446-559[»]
A/B682-821[»]
3C34X-ray1.82A/B446-559[»]
A/B682-821[»]
3C35X-ray1.97A/B446-559[»]
A/B682-821[»]
3C36X-ray1.68A/B446-559[»]
A/B682-821[»]
3GBAX-ray1.35A/B/C/D445-559[»]
A/B/C/D667-820[»]
3GBBX-ray2.10A/B445-559[»]
A/B682-820[»]
3S2VX-ray2.50A/B445-559[»]
A/B667-805[»]
4DLDX-ray2.00A/B445-559[»]
A/B667-805[»]
4E0XX-ray2.00A/B682-820[»]
4QF9X-ray2.28A/B/C445-559[»]
A/B/C682-820[»]
4YMBX-ray1.93A/B445-559[»]
A/B682-820[»]
5M2VX-ray3.18A/B445-559[»]
A/B682-820[»]
5MFQX-ray1.90A/B445-559[»]
A/B583-818[»]
5MFVX-ray2.18A/B445-559[»]
A/B583-818[»]
5MFWX-ray2.10A/B445-559[»]
A/B583-818[»]
5NEBX-ray2.05A/B445-559[»]
A/B682-820[»]
5NF5X-ray2.85A/B445-559[»]
A/B682-820[»]
ProteinModelPortaliP22756
SMRiP22756
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22756

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni531 – 533Glutamate binding3
Regioni704 – 705Glutamate binding2

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
HOGENOMiHOG000234371
HOVERGENiHBG051839
InParanoidiP22756
KOiK05201
PhylomeDBiP22756

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform Glur5-2C (identifier: P22756-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP
60 70 80 90 100
VNVEELAFKF AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL
110 120 130 140 150
ALGVAALFGP SHSSSVSAVQ SICNALEVPH IQTRWKHPSV DSRDLFYINL
160 170 180 190 200
YPDYAAISRA VLDLVLYYNW KTVTVVYEDS TGLIRLQELI KAPSRYNIKI
210 220 230 240 250
KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL KQILFMGMMT
260 270 280 290 300
EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME
310 320 330 340 350
RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR
360 370 380 390 400
HKPCALGPRF MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT
410 420 430 440 450
EKASGEVSKH LYKVWKKIGI WNSNSGLNMT DGNRDRSNNI TDSLANRTLI
460 470 480 490 500
VTTILEEPYV MYRKSDKPLY GNDRFEAYCL DLLKELSNIL GFLYDVKLVP
510 520 530 540 550
DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK VIDFSKPFMT
560 570 580 590 600
LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
610 620 630 640 650
PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI
660 670 680 690 700
VGGIWWFFTL IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV
710 720 730 740 750
RDGSTMTFFK KSKISTYEKM WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL
760 770 780 790 800
LMESTSIEYV TQRNCNLTQI GGLIDSKGYG VGTPIGSPYR DKITIAILQL
810 820 830 840 850
QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI VLAAGLVLSV
860 870 880 890 900
FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL
910 920 930 940
SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA
Length:949
Mass (Da):107,840
Last modified:November 1, 1995 - v3
Checksum:i020660BDD00054E0
GO
Isoform Glur5-2 (identifier: P22756-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     402-416: Missing.
     870-898: Missing.

Show »
Length:905
Mass (Da):102,646
Checksum:iB674CECB3FB60F47
GO
Isoform Glur5-2A (identifier: P22756-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     870-871: KG → HY
     872-949: Missing.

Show »
Length:871
Mass (Da):98,853
Checksum:iCC3EEB35068FDB54
GO
Isoform Glur5-2B (identifier: P22756-4) [UniParc]FASTAAdd to basket
Also known as: Glur5-1

The sequence of this isoform differs from the canonical sequence as follows:
     870-898: Missing.

Show »
Length:920
Mass (Da):104,388
Checksum:i4609F0CDF337B3D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti282K → L in AAA02874 (PubMed:1977421).Curated1
Sequence conflicti354 – 355CA → WR in AAA02874 (PubMed:1977421).Curated2
Sequence conflicti477A → G in AAA02874 (PubMed:1977421).Curated1

RNA editingi

Edited at position 636.
Partially edited.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti636Q → R in RNA edited version. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000129402 – 416Missing in isoform Glur5-2. CuratedAdd BLAST15
Alternative sequenceiVSP_000130870 – 898Missing in isoform Glur5-2B and isoform Glur5-2. CuratedAdd BLAST29
Alternative sequenceiVSP_000131870 – 871KG → HY in isoform Glur5-2A. Curated2
Alternative sequenceiVSP_000132872 – 949Missing in isoform Glur5-2A. CuratedAdd BLAST78

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83560 mRNA Translation: AAA02873.1
M83561 mRNA Translation: AAA02874.1
Z11712 mRNA Translation: CAA77775.1
Z11713 mRNA Translation: CAA77776.1
Z11714 mRNA Translation: CAA77777.1
PIRiS19808
RefSeqiNP_001104584.1, NM_001111114.1
NP_001104587.1, NM_001111117.1
NP_058937.1, NM_017241.2
UniGeneiRn.10449

Genome annotation databases

GeneIDi29559
KEGGirno:29559
UCSCiRGD:2732 rat [P22756-1]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Similar proteinsi

Entry informationi

Entry nameiGRIK1_RAT
AccessioniPrimary (citable) accession number: P22756
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 183 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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