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Q63273 (GRIK5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, kainate 5
Short name=GluK5
Alternative name(s):
Glutamate receptor KA-2
Short name=KA2
Gene names
Name:Grik5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA.

Subunit structure

Tetramer of two or more different subunits. Associates with GRIK1 (both edited and unedited versions), GRIK2, or GRIK3 to form functional channels. Homomeric associations do not produce any channel activity. Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein.

Tissue specificity

High expression in the cerebral cortex, pyriform cortex, caudate-putamen, hippocampal complex, medial habenulata and granule cell layer of the cerebellum. Weak expression in globus pallidus, thalamus, colliculi and the reticular thalamic nucleus.

Developmental stage

From embryonic day 14 through postnatal day 1, high expression in spinal cord, brain and some areas of the PNS. At E17 and E19, high expression in spinal cord, mesencephalon and telencephalic structures as in olfactory neurons and in nasal epithelium. Strong expression also in the pituitary.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK5 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose stimulus

Inferred from expression pattern PubMed 16936133. Source: RGD

establishment of localization in cell

Inferred from mutant phenotype PubMed 12878702. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17639597. Source: RGD

protein retention in ER lumen

Inferred from mutant phenotype PubMed 12878702. Source: UniProtKB

receptor clustering

Inferred from direct assay PubMed 9808460. Source: UniProtKB

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Compara

regulation of synaptic vesicle fusion to presynaptic membrane

Inferred from electronic annotation. Source: Compara

synaptic transmission

Inferred from direct assay PubMed 12080343. Source: RGD

synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Compara

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

ionotropic glutamate receptor complex

Inferred from direct assay PubMed 10627597. Source: UniProtKB

kainate selective glutamate receptor complex

Inferred from electronic annotation. Source: Compara

perikaryon

Inferred from direct assay PubMed 15844209. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 11226670. Source: RGD

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from electronic annotation. Source: Compara

terminal bouton

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

   Molecular_functionSH3 domain binding

Inferred from mutant phenotype PubMed 1127911. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from electronic annotation. Source: InterPro

kainate selective glutamate receptor activity

Inferred from direct assay PubMed 12080343. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 979965Glutamate receptor ionotropic, kainate 5
PRO_0000011554

Regions

Topological domain15 – 544530Extracellular Potential
Transmembrane545 – 56521Helical; Potential
Topological domain566 – 62257Cytoplasmic Potential
Transmembrane623 – 64321Helical; Potential
Topological domain644 – 803160Extracellular Potential
Transmembrane804 – 82421Helical; Potential
Topological domain825 – 979155Cytoplasmic Potential
Compositional bias860 – 8667Poly-Arg

Amino acid modifications

Glycosylation2191N-linked (GlcNAc...) Ref.3
Glycosylation2711N-linked (GlcNAc...) Ref.3
Glycosylation2851N-linked (GlcNAc...) Ref.3
Glycosylation3221N-linked (GlcNAc...) Ref.3
Glycosylation3721N-linked (GlcNAc...) Ref.3
Glycosylation3941N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 292 Ref.3 Ref.4
Disulfide bond83 ↔ 334 Ref.3 Ref.4
Disulfide bond165 ↔ 170 Ref.3 Ref.4

Experimental info

Sequence conflict8871N → G Ref.2
Sequence conflict8891K → R Ref.2
Sequence conflict9101D → N in AAA17831. Ref.2

Secondary structure

1 ................................................................... 979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63273 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 313E2862746474B1

FASTA979109,276
        10         20         30         40         50         60 
MPAELLLLLI VAFANPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ INGIIEVPAK 

        70         80         90        100        110        120 
ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP ASASTVSHIC GEKEIPHIKV 

       130        140        150        160        170        180 
GPEETPRLQY LRFASVSLYP SNEDVSLAVS RILKSFNYPS ASLICAKAEC LLRLEELVRG 

       190        200        210        220        230        240 
FLISKETLSV RMLDDSRDPT PLLKEIRDDK VSTIIIDANA SISHLVLRKA SELGMTSAFY 

       250        260        270        280        290        300 
KYILTTMDFP ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYPGP 

       310        320        330        340        350        360 
ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL RMVEYDGLTG 

       370        380        390        400        410        420 
RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN ATTLDINLSQ TLANKTLVVT 

       430        440        450        460        470        480 
TILENPYVMR RPNFQALSGN ERFEGFCVDM LRELAELLRF RYRLRLVEDG LYGAPEPNGS 

       490        500        510        520        530        540 
WTGMVGELIN RKADLAVAAF TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD 

       550        560        570        580        590        600 
PFSPAVWLFM LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV 

       610        620        630        640        650        660 
GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV PVESADDLAD 

       670        680        690        700        710        720 
QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV FVKSTEEGIA RVLNSRYAFL 

       730        740        750        760        770        780 
LESTMNEYHR RLNCNLTQIG GLLDTKGYGI GMPLGSPFRD EITLAILQLQ ENNRLEILKR 

       790        800        810        820        830        840 
KWWEGGRCPK EEDHRAKGLG MENIGGIFVV LICGLIIAVF VAVMEFIWST RRSAESEEVS 

       850        860        870        880        890        900 
VCQEMLQELR HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG 

       910        920        930        940        950        960 
AHGGPQRLLD DPGPPGGPRP QAPTPCTHVR VCQECRRIQA LRASGAGAPP RGLGTPAEAT 

       970 
SPPRPRPGPT GPRELTEHE

« Hide

References

[1]"The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits."
Herb A., Burnashev N., Werner P., Sakmann B., Wisden W., Seeburg P.H.
Neuron 8:775-785(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Boulter J., Pecht G.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains."
Kumar J., Mayer M.L.
J. Mol. Biol. 404:680-696(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-406, GLYCOSYLATION AT ASN-219; ASN-271; ASN-285; ASN-322 AND ASN-372, DISULFIDE BONDS.
[4]"Structure and assembly mechanism for heteromeric kainate receptors."
Kumar J., Schuck P., Mayer M.L.
Neuron 71:319-331(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 20-406 IN COMPLEX WITH GRIK2, DISULFIDE BONDS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z11581 mRNA. Translation: CAA77667.1.
U08258 mRNA. Translation: AAA17831.1.
IPIIPI00207006.
PIRJH0592.
RefSeqNP_113696.1. NM_031508.2.
UniGeneRn.74042.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OM0X-ray1.40A20-406[»]
3OM1X-ray1.68A/B20-406[»]
3QLUX-ray2.91A/B20-406[»]
3QLVX-ray3.94A/B/E/G/I20-406[»]
ProteinModelPortalQ63273.
SMRQ63273. Positions 22-828.
ModBaseSearch...

PTM databases

PhosphoSiteQ63273.

Proteomic databases

PaxDbQ63273.
PRIDEQ63273.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027578; ENSRNOP00000027578; ENSRNOG00000020310.
GeneID24407.
KEGGrno:24407.
UCSCRGD:2735. rat.

Organism-specific databases

CTD2901.
RGD2735. Grik5.

Phylogenomic databases

eggNOGNOG316680.
GeneTreeENSGT00590000082809.
HOGENOMHOG000234371.
HOVERGENHBG051839.
InParanoidQ63273.
KOK05205.
OMANINSVME.
OrthoDBEOG4RV2QP.

Gene expression databases

GenevestigatorQ63273.
GermOnlineENSRNOG00000020310. Rattus norvegicus.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
[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]
ProtoNetSearch...

Other

BindingDBQ63273.
ChEMBLCHEMBL4041.
NextBio603217.

Entry information

Entry nameGRIK5_RAT
AccessionPrimary (citable) accession number: Q63273
Secondary accession number(s): Q62643
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents