Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13003 (GRIK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, kainate 3

Short name=GluK3
Alternative name(s):
Excitatory amino acid receptor 5
Short name=EAA5
Glutamate receptor 7
Short name=GluR-7
Short name=GluR7
Gene names
Name:GRIK3
Synonyms:GLUR7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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 domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.

Subunit structure

Homotetramer, and heterotetramer with either GRIK4 or GRIK5. Interacts with PRKCABP By similarity. Interacts with NETO2 By similarity.

Subcellular location

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

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK3 subfamily. [View classification]

RNA editing

Edited at position 352.
Partially edited. Ref.1

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
RNA editing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled glutamate receptor signaling pathway

Inferred from direct assay PubMed 9144652. Source: UniProtKB

adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway

Inferred from direct assay PubMed 9144652. Source: GOC

glutamate receptor signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay Ref.5Ref.1. Source: GOC

negative regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

kainate selective glutamate receptor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

perikaryon

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

terminal bouton

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionadenylate cyclase inhibiting G-protein coupled glutamate receptor activity

Inferred from direct assay PubMed 9144652. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glutamate receptor activity

Traceable author statement Ref.4. Source: UniProtKB

ionotropic glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

kainate selective glutamate receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 919888Glutamate receptor ionotropic, kainate 3
PRO_0000011547

Regions

Topological domain32 – 563532Extracellular Potential
Transmembrane564 – 58421Helical; Potential
Topological domain585 – 63652Cytoplasmic Potential
Transmembrane637 – 65721Helical; Potential
Topological domain658 – 820163Extracellular Potential
Transmembrane821 – 84121Helical; Potential
Topological domain842 – 91978Cytoplasmic Potential
Region690 – 6923Glutamate binding By similarity

Sites

Binding site5201Glutamate By similarity
Binding site5251Glutamate By similarity
Binding site7391Glutamate By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation5481N-linked (GlcNAc...) Potential
Disulfide bond99 ↔ 350 By similarity

Natural variations

Natural variant2151R → H in a colorectal cancer sample; somatic mutation. Ref.6
VAR_035695
Natural variant3101S → A. Ref.1 Ref.5
Corresponds to variant rs6691840 [ dbSNP | Ensembl ].
VAR_000308
Natural variant3521R → Q in RNA edited version.
VAR_000309
Natural variant3911D → H in a breast cancer sample; somatic mutation. Ref.6
VAR_035696

Experimental info

Sequence conflict3031R → L in AAB30157. Ref.2
Sequence conflict6271E → V in AAB60407. Ref.1
Sequence conflict7131S → R in AAB60407. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q13003 [UniParc].

Last modified November 4, 2008. Version 3.
Checksum: 0F68F6CF33E4CE71

FASTA919104,037
        10         20         30         40         50         60 
MTAPWRRLRS LVWEYWAGLL VCAFWIPDSR GMPHVIRIGG IFEYADGPNA QVMNAEEHAF 

        70         80         90        100        110        120 
RFSANIINRN RTLLPNTTLT YDIQRIHFHD SFEATKKACD QLALGVVAIF GPSQGSCTNA 

       130        140        150        160        170        180 
VQSICNALEV PHIQLRWKHH PLDNKDTFYV NLYPDYASLS HAILDLVQYL KWRSATVVYD 

       190        200        210        220        230        240 
DSTGLIRLQE LIMAPSRYNI RLKIRQLPID SDDSRPLLKE MKRGREFRII FDCSHTMAAQ 

       250        260        270        280        290        300 
ILKQAMAMGM MTEYYHFIFT TLDLYALDLE PYRYSGVNLT GFRILNVDNP HVSAIVEKWS 

       310        320        330        340        350        360 
MERLQAAPRS ESGLLDGVMM TDAALLYDAV HIVSVCYQRA PQMTVNSLQC HRHKAWRFGG 

       370        380        390        400        410        420 
RFMNFIKEAQ WEGLTGRIVF NKTSGLRTDF DLDIISLKED GLEKVGVWSP ADGLNITEVA 

       430        440        450        460        470        480 
KGRGPNVTDS LTNRSLIVTT VLEEPFVMFR KSDRTLYGND RFEGYCIDLL KELAHILGFS 

       490        500        510        520        530        540 
YEIRLVEDGK YGAQDDKGQW NGMVKELIDH KADLAVAPLT ITHVREKAID FSKPFMTLGV 

       550        560        570        580        590        600 
SILYRKPNGT NPSVFSFLNP LSPDIWMYVL LAYLGVSCVL FVIARFSPYE WYDAHPCNPG 

       610        620        630        640        650        660 
SEVVENNFTL LNSFWFGMGS LMQQGSELMP KALSTRIIGG IWWFFTLIII SSYTANLAAF 

       670        680        690        700        710        720 
LTVERMESPI DSADDLAKQT KIEYGAVKDG ATMTFFKKSK ISTFEKMWAF MSSKPSALVK 

       730        740        750        760        770        780 
NNEEGIQRAL TADYALLMES TTIEYVTQRN CNLTQIGGLI DSKGYGIGTP MGSPYRDKIT 

       790        800        810        820        830        840 
IAILQLQEED KLHIMKEKWW RGSGCPEEEN KEASALGIQK IGGIFIVLAA GLVLSVLVAV 

       850        860        870        880        890        900 
GEFVYKLRKT AEREQRSFCS TVADEIRFSL TCQRRVKHKP QPPMMVKTDA VINMHTFNDR 

       910 
RLPGKDSMAC STSLAPVFP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of the human EAA5 (GluR7) receptor: a high-affinity kainate receptor with novel potential RNA editing sites."
Nutt S.L., Hoo K.H., Rampersad V., Deverill R.M., Elliott C.E., Fletcher E.J., Adams S.-L., Korczak B., Foldes R.L., Kamboj R.K.
Recept. Channels 2:315-326(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ALA-310, RNA EDITING OF POSITION 352.
Tissue: Fetal brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Chromosomal localization of gene for human glutamate receptor subunit-7."
Puranam R.S., Eubanks J.H., Heinemann S.F., McNamara J.O.
Somat. Cell Mol. Genet. 19:581-588(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 268-320.
Tissue: Placenta.
[5]"Unequal expression of allelic kainate receptor GluR7 mRNAs in human brains."
Schiffer H.H., Swanson G.T., Masliah E., Heinemann S.F.
J. Neurosci. 20:9025-9033(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-310.
[6]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-215 AND HIS-391.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16127 mRNA. Translation: AAB60407.1.
U16128 Genomic DNA. Translation: AAC50421.1.
AL355386, AC117945 Genomic DNA. Translation: CAI19119.1.
CH471059 Genomic DNA. Translation: EAX07351.1.
S69349 Genomic DNA. Translation: AAB30157.1.
PIRI59604.
RefSeqNP_000822.2. NM_000831.3.
UniGeneHs.128848.

3D structure databases

ProteinModelPortalQ13003.
SMRQ13003. Positions 34-416, 432-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109156. 4 interactions.
STRING9606.ENSP00000362183.

Chemistry

BindingDBQ13003.
ChEMBLCHEMBL3684.
DrugBankDB00142. L-Glutamic Acid.
GuidetoPHARMACOLOGY452.

PTM databases

PhosphoSiteQ13003.

Polymorphism databases

DMDM212276502.

Proteomic databases

PaxDbQ13003.
PRIDEQ13003.

Protocols and materials databases

DNASU2899.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373091; ENSP00000362183; ENSG00000163873.
GeneID2899.
KEGGhsa:2899.
UCSCuc001caz.2. human.

Organism-specific databases

CTD2899.
GeneCardsGC01M037261.
H-InvDBHIX0028621.
HGNCHGNC:4581. GRIK3.
HPAHPA014709.
MIM138243. gene.
neXtProtNX_Q13003.
PharmGKBPA28975.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316680.
HOGENOMHOG000234371.
HOVERGENHBG051839.
InParanoidQ13003.
KOK05203.
OMAEEQAFRF.
OrthoDBEOG71G9W6.
PhylomeDBQ13003.
TreeFamTF334668.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ13003.

Gene expression databases

ArrayExpressQ13003.
BgeeQ13003.
CleanExHS_GRIK3.
GenevestigatorQ13003.

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

GeneWikiGRIK3.
GenomeRNAi2899.
NextBio11475.
PROQ13003.
SOURCESearch...

Entry information

Entry nameGRIK3_HUMAN
AccessionPrimary (citable) accession number: Q13003
Secondary accession number(s): B1AMS6, Q13004, Q16136
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM