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Q9Z2W8 (GRIA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 4
Short name=GluR-4
Short name=GluR4
Alternative name(s):
AMPA-selective glutamate receptor 4
GluR-D
Glutamate receptor ionotropic, AMPA 4
Short name=GluA4
Gene names
Name:Gria4
Synonyms:Glur4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length902 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 EPB41L1 via its C-terminus By similarity. Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 and PRKCG By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell projection › dendrite. Note: Interaction with CNIH2, CNIH3 and PRKCG promotes cell surface expression By similarity.

Post-translational modification

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity. Ref.4

Phosphorylated at Ser-862 by PRKCG; phosphorylation increases plasma membrane-associated GRI4 expression By similarity.

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. GRIA4 subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 902882Glutamate receptor 4
PRO_0000011539

Regions

Topological domain22 – 544523Extracellular By similarity
Transmembrane545 – 56521Helical; By similarity
Topological domain566 – 59227Cytoplasmic By similarity
Intramembrane593 – 60816Helical; Pore-forming; By similarity
Intramembrane609 – 6113 By similarity
Topological domain612 – 6176Cytoplasmic By similarity
Transmembrane618 – 63821Helical; By similarity
Topological domain639 – 813175Extracellular By similarity
Transmembrane814 – 83421Helical; By similarity
Topological domain835 – 90268Cytoplasmic By similarity
Region500 – 5023Glutamate binding By similarity
Region676 – 6772Glutamate binding By similarity

Sites

Binding site4721Glutamate By similarity
Binding site5071Glutamate By similarity
Binding site7271Glutamate By similarity

Amino acid modifications

Modified residue8621Phosphoserine; by PKC/PRKCG By similarity
Lipidation6111S-palmitoyl cysteine By similarity
Lipidation8371S-palmitoyl cysteine Ref.4
Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 331 By similarity
Disulfide bond740 ↔ 795 By similarity

Experimental info

Sequence conflict6301F → G in BAA74538. Ref.1
Sequence conflict765 – 7673RTP → GNA in BAA74538. Ref.1
Sequence conflict776 – 7805SEAGV → NEQGL in BAA74538. Ref.1
Sequence conflict797 – 8015PKDSG → SGGGD in BAA74538. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z2W8 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 39844E5CE634B841

FASTA902100,847
        10         20         30         40         50         60 
MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA 

        70         80         90        100        110        120 
PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP 

       130        140        150        160        170        180 
SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH 

       190        200        210        220        230        240 
VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA 

       250        260        270        280        290        300 
NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL 

       310        320        330        340        350        360 
TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN 

       370        380        390        400        410        420 
VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DAPTLGNDTA AIENRTVVVT 

       430        440        450        460        470        480 
TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK 

       490        500        510        520        530        540 
IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL 

       550        560        570        580        590        600 
DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW 

       610        620        630        640        650        660 
FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER MVSPIESAED 

       670        680        690        700        710        720 
LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG 

       730        740        750        760        770        780 
KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSSLRTPVNL AVLKLSEAGV 

       790        800        810        820        830        840 
LDKLKNKWWY DKGECGPKDS GSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS 

       850        860        870        880        890        900 
RAEAKRMKLT FSEAIRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD 


LP

« Hide

References

« Hide 'large scale' references
[1]"Mouse glutamate receptor channel alpha4 subunit."
Sakimura K., Ikeno K.
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]"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].
Strain: C57BL/6.
Tissue: Brain.
[4]"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-837.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB022913 mRNA. Translation: BAA74538.1.
AB079073 mRNA. Translation: BAE06154.1.
BC060697 mRNA. Translation: AAH60697.1.
IPIIPI00131471.
RefSeqNP_001106651.1. NM_001113180.1.
NP_001106652.1. NM_001113181.1.
NP_062665.3. NM_019691.4.
UniGeneMm.209263.

3D structure databases

ProteinModelPortalQ9Z2W8.
SMRQ9Z2W8. Positions 23-839.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z2W8. 2 interactions.
STRING10090.ENSMUSP00000066980.

PTM databases

PhosphoSiteQ9Z2W8.

Proteomic databases

PaxDbQ9Z2W8.
PRIDEQ9Z2W8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063508; ENSMUSP00000066980; ENSMUSG00000025892.
GeneID14802.
KEGGmmu:14802.
UCSCuc009obo.2. mouse.

Organism-specific databases

CTD2893.
MGIMGI:95811. Gria4.

Phylogenomic databases

eggNOGNOG316680.
GeneTreeENSGT00590000082809.
HOGENOMHOG000234372.
HOVERGENHBG051839.
InParanoidQ9Z2W8.
KOK05200.
OrthoDBEOG4DBTD0.

Gene expression databases

ArrayExpressQ9Z2W8.
BgeeQ9Z2W8.
CleanExMM_GRIA4.
GenevestigatorQ9Z2W8.
GermOnlineENSMUSG00000025892. Mus musculus.

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

BindingDBQ9Z2W8.
ChEMBLCHEMBL3615.
ChiTaRSGRIA4. mouse.
NextBio286965.
SOURCESearch...

Entry information

Entry nameGRIA4_MOUSE
AccessionPrimary (citable) accession number: Q9Z2W8
Secondary accession number(s): Q6P9M7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

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