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UniProtKB/Swiss-Prot entry P19492


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRIA3_RAT
Primary accession number P19492
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 90)
Name and origin of the protein
Protein name Glutamate receptor 3 [Precursor]
Synonyms GluR-3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
AMPA-selective glutamate receptor 3
Gene name
Name: Gria3
Synonyms: Glur3
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2166337 [NCBI, ExPASy, EBI, Israel, Japan]
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H.;
"A family of AMPA-selective glutamate receptors.";
Science 249:556-560(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Forebrain;
PubMed=2168579 [NCBI, ExPASy, EBI, Israel, Japan]
Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F.;
"Molecular cloning and functional expression of glutamate receptor subunit genes.";
Science 249:1033-1037(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (VARIANT FLIP).
TISSUE=Brain cortex, and Hippocampus;
DOI=10.1016/0896-6273(90)90212-X; PubMed=1699567 [NCBI, ExPASy, EBI, Israel, Japan]
Nakanishi N., Schneider N.A., Axel R.;
"A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties.";
Neuron 5:569-581(1990).
[4]
ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
TISSUE=Brain;
PubMed=1699275 [NCBI, ExPASy, EBI, Israel, Japan]
Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.;
"Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.";
Science 249:1580-1585(1990).
[5]
INTERACTION WITH PRKCABP.
DOI=10.1016/S0896-6273(00)80689-3; PubMed=10027300 [NCBI, ExPASy, EBI, Israel, Japan]
Xia J., Zhang X., Staudinger J., Huganir R.L.;
"Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1.";
Neuron 22:179-187(1999).
[6]
INTERACTION WITH GRIP1.
TISSUE=Hippocampus;
DOI=10.1038/386279a0; PubMed=9069286 [NCBI, ExPASy, EBI, Israel, Japan]
Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.;
"GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors.";
Nature 386:279-284(1997).
[7]
INTERACTION WITH GRIP2.
PubMed=10414981 [NCBI, ExPASy, EBI, Israel, Japan]
Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., Standaert D.G., Weinberg R., Sheng M.;
"Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo.";
J. Neurosci. 19:6528-6537(1999).
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.
  • SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2.
  • INTERACTION:
    P18708:NSF (xeno); NbExp=1; IntAct=EBI-77764, EBI-925742;
    Q9EP80:Pick1; NbExp=4; IntAct=EBI-77764, EBI-77728;
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameFlop
    Isoform IDP19492-1
    This is the isoform sequence displayed in this entry.
    NameFlip
    Isoform IDP19492-2
    Features which should be applied to build the isoform sequence: VSP_000119, VSP_000120, VSP_000121, VSP_000122.
  • PTM: 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).
  • 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.
  • SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10) family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M36420; AAA41245.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54656; CAA38466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38062; AAA63480.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M85036; AAA41241.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C40170; C40170.
RefSeq NP_001106213.1; -.
NP_116785.2; -.
UniGene Rn.13679
3D structure databases
HSSP P19491; 1FTK. [HSSP ENTRY / PDB]
SMR P19492; 416-530, 657-800.
ModBase P19492.
Protein-protein interaction databases
IntAct P19492; -.
PTM databases
PhosphoSite P19492; -.
Organism-specific databases
RGD 70958; Gria3.
Gene expression databases
ArrayExpress P19492; -.
GermOnline ENSRNOG00000007682; Rattus norvegicus.
Ontologies
GO
GO:0043197; Cellular component: dendritic spine (inferred from direct assay from UniProtKB).
GO:0008328; Cellular component: ionotropic glutamate receptor complex (traceable author statement from UniProtKB).
GO:0014069; Cellular component: postsynaptic density (inferred from direct assay from UniProtKB).
GO:0030165; Molecular function: PDZ domain binding (inferred from physical interaction from UniProtKB).
GO:0001919; Biological process: regulation of receptor recycling (inferred from mutant phenotype from UniProtKB).
GO:0010226; Biological process: response to lithium ion (inferred from expression pattern from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001828; ANF_lig_bd_rcpt.
IPR015683; Glutamate_receptor-rel.
IPR001320; Iontro_glu_rcpt.
IPR001508; NMDA_rcpt.
Graphical view of domain structure.
PANTHER PTHR18966; Glut_Rec_Related; 1.
Pfam PF01094; ANF_receptor; 1.
PF00060; Lig_chan; 1.
Pfam graphical view of domain structure.
PRINTS PR00177; NMDARECEPTOR.
SMART SM00079; PBPe; 1.
SMART graphical view of domain structure.
BLOCKS P19492.
Genome annotation databases
Ensembl ENSRNOG00000007682; Rattus norvegicus. [Contig view]
GeneID 29628; -.
KEGG rno:29628; -.
Phylogenomic databases
HOVERGEN P19492; -.
Other
ProtoNet P19492.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell junction; Cell membrane; Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22     Potential. 
CHAIN   23   888  866     Glutamate receptor 3. PRO_0000011537
TOPO_DOM   23   546  524     Extracellular (Potential). 
TRANSMEM   547   567  21     Potential. 
TOPO_DOM   568   629  62     Cytoplasmic (Potential). 
TRANSMEM   630   650  21     Potential. 
TOPO_DOM   651   817  167     Extracellular (Potential). 
TRANSMEM   818   838  21     Potential. 
TOPO_DOM   839   888  50     Cytoplasmic (Potential). 
REGION   502   504  3     Glutamate binding (By similarity). 
REGION   680   681  2     Glutamate binding (By similarity). 
BINDING   509   509        Glutamate (By similarity). 
BINDING   731   731        Glutamate (By similarity). 
MOD_RES   871   871        Phosphotyrosine (By similarity). 
MOD_RES   881   881        Phosphotyrosine (By similarity). 
LIPID   615   615        S-palmitoyl cysteine (By similarity). 
LIPID   841   841        S-palmitoyl cysteine (By similarity). 
CARBOHYD   57    57        N-linked (GlcNAc...) (Potential). 
CARBOHYD   260   260        N-linked (GlcNAc...) (Potential). 
CARBOHYD   374   374        N-linked (GlcNAc...) (Potential). 
CARBOHYD   409   409        N-linked (GlcNAc...) (Potential). 
CARBOHYD   416   416        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   770   771        NA -> TP (in isoform Flip). VSP_000119
VAR_SEQ   780   780        N -> S (in isoform Flip). VSP_000120
VAR_SEQ   784   784        L -> I (in isoform Flip). VSP_000121
VAR_SEQ   801   805        SGGGD -> AKDSG (in isoform Flip). VSP_000122
CONFLICT   517   518        KP -> NA (in Ref. 2). 
Sequence information
Length: 888 AA [This is the length of the unprocessed precursor] Molecular weight: 100373 Da [This is the MW of the unprocessed precursor] CRC64: 2981616375661703 [This is a checksum on the sequence]
        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 GAILSLLSYY KWEKFVYLYD TERGFSVLQA IMEAAVQNNW 

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

       250        260        270        280        290        300 
LANLGFTDIL 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 ATPKGSALGN AVNLAVLKLN 

       790        800        810        820        830        840 
EQGLLDKLKN KWWYDKGECG SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF 

       850        860        870        880 
CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI 

P19492 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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