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P22756 (GRIK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, kainate 1

Short name=GluK1
Alternative name(s):
Glutamate receptor 5
Short name=GluR-5
Short name=GluR5
Gene names
Name:Grik1
Synonyms:Glur5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length949 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7

Subunit structure

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. Ref.3 Ref.5 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein.

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.

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.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK1 subfamily. [View classification]

RNA editing

Edited at position 636.
Partially edited.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
RNA editing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_procession transmembrane transport

Inferred from direct assay Ref.2. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay PubMed 17395219. Source: RGD

negative regulation of synaptic transmission, GABAergic

Inferred from direct assay PubMed 12533604. Source: RGD

negative regulation of synaptic transmission, glutamatergic

Inferred from direct assay PubMed 17395219. Source: RGD

nervous system development

Inferred from mutant phenotype Ref.2. Source: RGD

positive regulation of synaptic transmission, GABAergic

Inferred from direct assay PubMed 12533604. Source: RGD

regulation of ion transmembrane transport

Inferred from mutant phenotype PubMed 12904467. Source: GOC

regulation of short-term neuronal synaptic plasticity

Inferred from direct assay PubMed 17395219. Source: RGD

regulation of synaptic plasticity

Traceable author statement PubMed 12533604. Source: UniProtKB

synaptic transmission

Traceable author statement PubMed 12533604. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from direct assay PubMed 15844209. Source: RGD

ionotropic glutamate receptor complex

Inferred from direct assay Ref.7. Source: RGD

kainate selective glutamate receptor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from direct assay PubMed 15844209. Source: RGD

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

receptor complex

Inferred from direct assay PubMed 10627597. Source: UniProtKB

terminal bouton

Inferred from direct assay PubMed 15844209PubMed 16360275. Source: RGD

   Molecular_functiondrug binding

Inferred from direct assay PubMed 12904467. Source: RGD

extracellular-glutamate-gated ion channel activity

Inferred from direct assay Ref.2. Source: RGD

glutamate binding

Inferred from direct assay PubMed 12533604Ref.7. Source: RGD

ionotropic glutamate receptor activity

Inferred from direct assay PubMed 17395219. Source: RGD

kainate selective glutamate receptor activity

Inferred from direct assay PubMed 17395219. Source: RGD

protein binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.7. Source: RGD

voltage-gated cation channel activity

Inferred from mutant phenotype PubMed 12904467. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Glur5-2C (identifier: P22756-1)

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.
Isoform Glur5-2 (identifier: P22756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     402-416: Missing.
     870-898: Missing.
Isoform Glur5-2A (identifier: P22756-3)

The sequence of this isoform differs from the canonical sequence as follows:
     870-871: KG → HY
     872-949: Missing.
Isoform Glur5-2B (identifier: P22756-4)

Also known as: Glur5-1;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 949919Glutamate receptor ionotropic, kainate 1
PRO_0000011543

Regions

Topological domain31 – 576546Extracellular Potential
Transmembrane577 – 59721Helical; Potential
Topological domain598 – 65356Cytoplasmic Potential
Transmembrane654 – 67421Helical; Potential
Topological domain675 – 834160Extracellular Potential
Transmembrane835 – 85521Helical; Potential
Topological domain856 – 94994Cytoplasmic Potential
Region531 – 5333Glutamate binding
Region704 – 7052Glutamate binding

Sites

Binding site5381Glutamate
Binding site7531Glutamate

Amino acid modifications

Modified residue7251Phosphoserine; by PKC Potential
Modified residue7611Phosphothreonine; by PKC Potential
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence402 – 41615Missing in isoform Glur5-2.
VSP_000129
Alternative sequence870 – 89829Missing in isoform Glur5-2B and isoform Glur5-2.
VSP_000130
Alternative sequence870 – 8712KG → HY in isoform Glur5-2A.
VSP_000131
Alternative sequence872 – 94978Missing in isoform Glur5-2A.
VSP_000132
Natural variant6361Q → R in RNA edited version.

Experimental info

Sequence conflict2821K → L in AAA02874. Ref.2
Sequence conflict354 – 3552CA → WR in AAA02874. Ref.2
Sequence conflict4771A → G in AAA02874. Ref.2

Secondary structure

..................................................... 949
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Glur5-2C [UniParc].

Last modified November 1, 1995. Version 3.
Checksum: 020660BDD00054E0

FASTA949107,840
        10         20         30         40         50         60 
MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF 

        70         80         90        100        110        120 
AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ 

       130        140        150        160        170        180 
SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS 

       190        200        210        220        230        240 
TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL 

       250        260        270        280        290        300 
KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 

       310        320        330        340        350        360 
RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF 

       370        380        390        400        410        420 
MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI 

       430        440        450        460        470        480 
WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL 

       490        500        510        520        530        540 
DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK 

       550        560        570        580        590        600 
VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 

       610        620        630        640        650        660 
PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL 

       670        680        690        700        710        720 
IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM 

       730        740        750        760        770        780 
WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG 

       790        800        810        820        830        840 
VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI 

       850        860        870        880        890        900 
VLAAGLVLSV FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL 

       910        920        930        940 
SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA 

« Hide

Isoform Glur5-2 [UniParc].

Checksum: B674CECB3FB60F47
Show »

FASTA905102,646
Isoform Glur5-2A [UniParc].

Checksum: CC3EEB35068FDB54
Show »

FASTA87198,853
Isoform Glur5-2B (Glur5-1) [UniParc].

Checksum: 4609F0CDF337B3D1
Show »

FASTA920104,388

References

[1]"A glutamate receptor channel with high affinity for domoate and kainate."
Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B., Seeburg P.H.
EMBO J. 11:1651-1656(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Brain.
[2]"Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development."
Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A., Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.
Neuron 5:583-595(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway."
Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J.
J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL17.
[4]"High-affinity kainate and domoate receptors in rat brain."
Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.
FEBS Lett. 307:139-143(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[5]"Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate."
Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S.
FEBS Lett. 579:1154-1160(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH GLUTAMATE, SUBUNIT.
[6]"Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity."
Mayer M.L.
Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
[7]"Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists."
Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.
J. Neurosci. 26:2852-2861(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302 AND UBP310, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS19808.
RefSeqNP_001104584.1. NM_001111114.1.
NP_001104587.1. NM_001111117.1.
NP_058937.1. NM_017241.2.
UniGeneRn.10449.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
A/B682-821[»]
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/D682-820[»]
3GBBX-ray2.10A/B445-559[»]
A/B682-820[»]
3S2VX-ray2.50A/B445-559[»]
A/B682-820[»]
4DLDX-ray2.00A/B445-559[»]
A/B667-820[»]
4E0XX-ray2.00A/B682-820[»]
ProteinModelPortalP22756.
SMRP22756. Positions 445-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248193. 4 interactions.
DIPDIP-29257N.
STRING10116.ENSRNOP00000045594.

Chemistry

BindingDBP22756.
ChEMBLCHEMBL2094119.
GuidetoPHARMACOLOGY450.

Protein family/group databases

TCDB1.A.10.1.5. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSiteP22756.

Proteomic databases

PaxDbP22756.
PRIDEP22756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000042581; ENSRNOP00000050263; ENSRNOG00000001575.
ENSRNOT00000051060; ENSRNOP00000046164; ENSRNOG00000001575.
GeneID29559.
KEGGrno:29559.
UCSCRGD:2732. rat. [P22756-1]

Organism-specific databases

CTD2897.
RGD2732. Grik1.

Phylogenomic databases

eggNOGNOG316680.
GeneTreeENSGT00740000114953.
HOGENOMHOG000234371.
HOVERGENHBG051839.
InParanoidP22756.
KOK05201.
PhylomeDBP22756.

Gene expression databases

GenevestigatorP22756.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP22756.
NextBio609606.
PROP22756.

Entry information

Entry nameGRIK1_RAT
AccessionPrimary (citable) accession number: P22756
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references