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1.A.10.1.2
Glutamate receptor 4, GIC, AMPA-subtype, GluR4, GRIA4 or GluR-D (preferentially monovalent cation selective). Binding of the excitatory neurotransmitter, L-glutamate, induces a conformation change, leading to the opening of the cation channel, thereby converting 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, CACNG7 or CACNG8, GluR4 shows resensitization characterized by a delayed accumulation of current flux upon continued application of glutamate (Gill et al. 2008; Birdsey-Benson et al. 2010). De novo variants in GRIA4 lead to intellectual disability with or without seizures, gait abnormalities, problems of social behavior, and other variable features (Martin et al. 2017).

Accession Number:P19493
Protein Name:GluR-D aka GRIA4 aka GLUR4
Length:902
Molecular Weight:100758.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate monoatomic monocation

Cross database links:

RefSeq: NP_001106655.1    NP_058959.2   
Entrez Gene ID: 29629   
Pfam: PF01094    PF00060    PF10613   
KEGG: rno:29629   

Gene Ontology

GO:0030054 C:cell junction
GO:0030425 C:dendrite
GO:0043025 C:neuronal cell body
GO:0014069 C:postsynaptic density
GO:0045211 C:postsynaptic membrane
GO:0043195 C:terminal button
GO:0004971 F:alpha-amino-3-hydroxy-5-methyl-4-isoxazole ...
GO:0005234 F:extracellular-glutamate-gated ion channel a...
GO:0006811 P:ion transport
GO:0051968 P:positive regulation of synaptic transmissio...
GO:0050803 P:regulation of synapse structure and activity

References (7)

[1] “A family of AMPA-selective glutamate receptors.”  Keinaenen K.et.al.   2166337
[2] “Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development.”  Bettler B.et.al.   1977421
[3] “Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.”  Sommer B.et.al.   1699275
[4] “Molecular cloning and development analysis of a new glutamate receptor subunit isoform in cerebellum.”  Gallo V.et.al.   1372042
[5] “Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain.”  Pasternack A.et.al.   12603841
[6] “Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1.”  Xia J.et.al.   10027300
[7] “Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein.”  Coleman S.K.et.al.   12574408
Structure:
3EN3   3EPE   3FAS   3FAT   3KEI   3KFM   4GPA   5FWX     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA 
61:	PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP 
121:	SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH 
181:	VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA 
241:	NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL 
301:	TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN 
361:	VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DMPTLGNDTA AIENRTVVVT 
421:	TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK 
481:	IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL 
541:	DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW 
601:	FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER MVSPIESAED 
661:	LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG 
721:	KFAFLLESTM NEYTEQRKPC DTMKVGGNLD SKGYGVATPK GSSLGNAVNL AVLKLNEQGL 
781:	LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS 
841:	RAEAKRMKLT FSEATRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD 
901:	LP