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Q9Z2W9 (GRIA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 3

Short name=GluR-3
Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name=GluA3
Gene names
Name:Gria3
Synonyms:Glur3, Kiaa4184
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length888 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 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. 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. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate By similarity.

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 By similarity. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity. Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein By similarity. Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression By similarity.

Domain

The M4 transmembrane segment mediates tetramerization and is required for cell surface expression By similarity.

Post-translational modification

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-841 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity. Ref.8

Miscellaneous

The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA3 subfamily. [View classification]

Sequence caution

The sequence BAD90527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 17093100. Source: MGI

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 14687553. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform Flip (identifier: Q9Z2W9-1)

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 Flop (identifier: Q9Z2W9-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 888866Glutamate receptor 3
PRO_0000042230

Regions

Topological domain23 – 546524Extracellular By similarity
Transmembrane547 – 56721Helical; By similarity
Topological domain568 – 59629Cytoplasmic By similarity
Intramembrane597 – 61216Helical; Pore-forming; By similarity
Intramembrane613 – 6153 By similarity
Topological domain616 – 6216Cytoplasmic By similarity
Transmembrane622 – 64221Helical; By similarity
Topological domain643 – 817175Extracellular By similarity
Transmembrane818 – 83821Helical; Name=M4; By similarity
Topological domain839 – 88850Cytoplasmic By similarity
Region502 – 5043Glutamate binding
Region680 – 6812Glutamate binding

Sites

Binding site4741Glutamate
Binding site5091Glutamate
Binding site7311Glutamate

Amino acid modifications

Modified residue8711Phosphotyrosine Ref.9
Modified residue8811Phosphotyrosine Ref.9
Lipidation6151S-palmitoyl cysteine By similarity
Lipidation8411S-palmitoyl cysteine Ref.8
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Disulfide bond85 ↔ 334 By similarity
Disulfide bond744 ↔ 799 Ref.10

Experimental info

Sequence conflict3001T → I in BAD90527. Ref.4
Sequence conflict7691R → G in BAA37124. Ref.1
Sequence conflict7691R → G in BAE06153. Ref.1
Sequence conflict7691R → G in AAL90768. Ref.3
Sequence conflict7691R → G in AAL90769. Ref.3
Sequence conflict7691R → G in BAD90527. Ref.4

Secondary structure

.......................... 888
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Flip [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 9F68C5D80E81DC02

FASTA888100,527
        10         20         30         40         50         60 
MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE 

        70         80         90        100        110        120 
KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT 

       130        140        150        160        170        180 
PSFPTDADVQ FVIQMRPALK GAILSLLGYY KWEKFVYLYD TERGFSILQA IMEAAVQNNW 

       190        200        210        220        230        240 
QVTARSVGNI KDIQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM 

       250        260        270        280        290        300 
LANLGFTDIV LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT 

       310        320        330        340        350        360 
SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER ALKMVQVQGM 

       370        380        390        400        410        420 
TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV PFSDQQISND SSSSENRTIV 

       430        440        450        460        470        480 
VTTILESPYV MYKKNHEQLE GNERYEGYCV DLAYEIAKHV RIKYKLSIVG DGKYGARDPE 

       490        500        510        520        530        540 
TKIWNGMVGE LVYGRADIAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS 

       550        560        570        580        590        600 
FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF 

       610        620        630        640        650        660 
NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL TVERMVSPIE 

       670        680        690        700        710        720 
SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM KSAEPSVFTK TTADGVARVR 

       730        740        750        760        770        780 
KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG GNLDSKGYGV ATPKGSALRT PVNLAVLKLS 

       790        800        810        820        830        840 
EQGILDKLKN KWWYDKGECG AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF 

       850        860        870        880 
CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI 

« Hide

Isoform Flop (Sequence not available).

References

« Hide 'large scale' references
[1]"Mouse glutamate receptor channel alpha3 subunit."
Sakimura K., Yamazaki M.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"Expression of AMPA-selective glutamate receptors in mouse spinal cord."
Doi Y., Nishizawa M., Minami T., Ito S.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ddY.
Tissue: Spinal cord.
[3]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites."
Hayashi T., Rumbaugh G., Huganir R.L.
Neuron 47:709-723(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-841.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-871 AND TYR-881, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"Piracetam defines a new binding site for allosteric modulators of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors."
Ahmed A.H., Oswald R.E.
J. Med. Chem. 53:2197-2203(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 658-799 IN COMPLEX WITH GLUTAMATE, SUBUNIT, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022342 mRNA. Translation: BAA37124.1.
AB079072 mRNA. Translation: BAE06153.1.
AF483494 mRNA. Translation: AAL90768.1.
AF483495 mRNA. Translation: AAL90769.1.
AK220530 mRNA. Translation: BAD90527.1. Different initiation.
CH466570 Genomic DNA. Translation: EDL29035.1.
AL672290, AL672232 Genomic DNA. Translation: CAQ11290.1.
AL672232, AL672290 Genomic DNA. Translation: CAQ12028.1.
BC129855 mRNA. Translation: AAI29856.1.
CCDSCCDS30097.1. [Q9Z2W9-1]
RefSeqNP_001268858.1. NM_001281929.1.
NP_001277380.1. NM_001290451.1.
NP_058582.3. NM_016886.4.
XP_006541583.1. XM_006541520.1. [Q9Z2W9-1]
UniGeneMm.327681.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LSWX-ray1.75A658-799[»]
3LSXX-ray2.01A658-799[»]
ProteinModelPortalQ9Z2W9.
SMRQ9Z2W9. Positions 26-843.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207340. 2 interactions.
IntActQ9Z2W9. 4 interactions.
MINTMINT-4131411.

Chemistry

BindingDBQ9Z2W9.
ChEMBLCHEMBL2096617.
GuidetoPHARMACOLOGY446.

PTM databases

PhosphoSiteQ9Z2W9.

Proteomic databases

MaxQBQ9Z2W9.
PaxDbQ9Z2W9.
PRIDEQ9Z2W9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076349; ENSMUSP00000075687; ENSMUSG00000001986. [Q9Z2W9-1]
GeneID53623.
KEGGmmu:53623.
UCSCuc009tal.2. mouse. [Q9Z2W9-1]

Organism-specific databases

CTD2892.
MGIMGI:95810. Gria3.
RougeSearch...

Phylogenomic databases

eggNOGNOG316680.
GeneTreeENSGT00740000115362.
HOGENOMHOG000234372.
HOVERGENHBG051839.
KOK05199.
OrthoDBEOG7C2R0J.
TreeFamTF315232.

Gene expression databases

ArrayExpressQ9Z2W9.
BgeeQ9Z2W9.
CleanExMM_GRIA3.
GenevestigatorQ9Z2W9.

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

EvolutionaryTraceQ9Z2W9.
NextBio310361.
PROQ9Z2W9.
SOURCESearch...

Entry information

Entry nameGRIA3_MOUSE
AccessionPrimary (citable) accession number: Q9Z2W9
Secondary accession number(s): A2VDF4, Q5DTJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 113 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot