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P23818 (GRIA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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 1
Short name=GluR-1
Alternative name(s):
AMPA-selective glutamate receptor 1
GluR-A
GluR-K1
Glutamate receptor ionotropic, AMPA 1
Short name=GluA1
Gene names
Name:Gria1
Synonyms:Glur1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length907 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. 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.

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with DLG1 via its C-terminus. Interacts with CACNG2 By similarity. Interacts with HIP1 and RASGRF2. Interacts with SYNDIG1 and GRIA2. Interacts with LRFN1 By similarity. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CNIH2, CACNG2 AND CACGN5 By similarity. Ref.2 Ref.4 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell projection › dendrite. Cell projection › dendritic spine. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression By similarity. Ref.6

Post-translational modification

Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. Ref.3

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. GRIA1 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIonic channel
Ligand-gated ion channel
Receptor
   PTMGlycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlong-term memory

Inferred from mutant phenotype. Source: UniProtKB

receptor internalization

Inferred from mutant phenotype. Source: UniProtKB

synaptic transmission

Inferred from genetic interaction. Source: MGI

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

Inferred from direct assay. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction

Inferred from direct assay. Source: MGI

neuronal cell body

Inferred from direct assay. Source: BHF-UCL

postsynaptic density

Inferred from direct assay Ref.6. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.2Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 907889Glutamate receptor 1
PRO_0000011530

Regions

Topological domain19 – 536518Extracellular Potential
Transmembrane537 – 55721Helical; Potential
Topological domain558 – 61760Cytoplasmic Potential
Transmembrane618 – 63821Helical; Potential
Topological domain639 – 805167Extracellular Potential
Transmembrane806 – 82621Helical; Potential
Topological domain827 – 90781Cytoplasmic Potential
Region492 – 4943Glutamate binding By similarity
Region668 – 6692Glutamate binding By similarity

Sites

Binding site4991Glutamate By similarity
Binding site7191Glutamate By similarity

Amino acid modifications

Modified residue6451Phosphoserine By similarity
Modified residue7101Phosphoserine By similarity
Modified residue8491Phosphoserine By similarity
Modified residue8631Phosphoserine By similarity
Lipidation6031S-palmitoyl cysteine Ref.3
Lipidation8291S-palmitoyl cysteine Ref.3
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P23818 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: F0FF7031DADD7CEB

FASTA907101,569
        10         20         30         40         50         60 
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 

        70         80         90        100        110        120 
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 

       130        140        150        160        170        180 
FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT 

       190        200        210        220        230        240 
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL 

       250        260        270        280        290        300 
NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDARDHTR VDWKRPKYTS ALTYDGVKVM 

       310        320        330        340        350        360 
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 

       370        380        390        400        410        420 
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 

       430        440        450        460        470        480 
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 

       490        500        510        520        530        540 
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 

       550        560        570        580        590        600 
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 

       610        620        630        640        650        660 
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 

       670        680        690        700        710        720 
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 

       730        740        750        760        770        780 
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRGPV NLAVLKLSEQ GVLDKLKSKW 

       790        800        810        820        830        840 
WYDKGECGSK DSGSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 

       850        860        870        880        890        900 
GFCLIPQQSI NEAIRTSTLP RNSGAGASGG SGSGENGRVV SQDFPKSMQS IPCMSHSSGM 


PLGATGL

« Hide

References

[1]"Functional expression from cloned cDNAs of glutamate receptor species responsive to kainate and quisqualate."
Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M., Meguro H., Warashina A., Numa S., Mishina M.
FEBS Lett. 272:73-80(1990) [PubMed: 1699805] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Disruption of the endocytic protein HIP1 results in neurological deficits and decreased AMPA receptor trafficking."
Metzler M., Li B., Gan L., Georgiou J., Gutekunst C.A., Wang Y., Torre E., Devon R.S., Oh R., Legendre-Guillemin V., Rich M., Alvarez C., Gertsenstein M., McPherson P.S., Nagy A., Wang Y.T., Roder J.C., Raymond L.A., Hayden M.R.
EMBO J. 22:3254-3266(2003) [PubMed: 12839988] [Abstract]
Cited for: INTERACTION WITH HIP1.
[3]"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: 16129400] [Abstract]
Cited for: PALMITOYLATION AT CYS-603 AND CYS-829.
[4]"Age-dependent participation of Ras-GRF proteins in coupling calcium-permeable AMPA glutamate receptors to Ras/Erk signaling in cortical neurons."
Tian X., Feig L.A.
J. Biol. Chem. 281:7578-7582(2006) [PubMed: 16407208] [Abstract]
Cited for: INTERACTION WITH RASGRF2.
[5]"SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane protein that regulates excitatory synapse development."
Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E.
Neuron 65:80-93(2010) [PubMed: 20152115] [Abstract]
Cited for: INTERACTION WITH SYNDIG1 AND GRIA2.
[6]"Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins."
Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.
Neuron 68:1082-1096(2010) [PubMed: 21172611] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X57497 mRNA. Translation: CAA40734.1.
IPIIPI00136965.
PIRS12874.
RefSeqNP_001106796.1. NM_001113325.2.
UniGeneMm.4920.

3D structure databases

ProteinModelPortalP23818.
SMRP23818. Positions 22-831.
ModBaseSearch...

Protein-protein interaction databases

IntActP23818. 3 interactions.
MINTMINT-1897734.
STRINGP23818.

PTM databases

PhosphoSiteP23818.

Proteomic databases

PRIDEP23818.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036315; ENSMUSP00000044494; ENSMUSG00000020524.
GeneID14799.
KEGGmmu:14799.
UCSCuc007izs.2. mouse.

Organism-specific databases

CTD2890.
MGIMGI:95808. Gria1.

Phylogenomic databases

eggNOGmaNOG06626.
HOGENOMHBG381523.
HOVERGENHBG051839.
InParanoidP23818.

Gene expression databases

ArrayExpressP23818.
BgeeP23818.
CleanExMM_GRIA1.
GenevestigatorP23818.
GermOnlineENSMUSG00000020524. 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]
KOK05197.
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

NextBio286953.
SOURCESearch...

Entry information

Entry nameGRIA1_MOUSE
AccessionPrimary (citable) accession number: P23818
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 25, 2012
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

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