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1.A.10.1.1
AMPA-selective glutamate ionotropic channel receptor (GIC; AMPAR), kainate-subtype, GluR-K1; GluR1; GluR-A; GluA1; Gria1 of 906 aas (preferentially monovalent cation selective). Contributes to amygdala-dependent emotional learning and fear conditioning (Humeau et al., 2007). Transmembrane AMPAR regulatory protein (TARP) gamma-7 (TC#8.A.16.2.5) selectively enhances the synaptic expression of Ca2+-permeable (CP-AMPARs) and suppresses calcium-impermeable (CI-AMPAR) activities (Studniarczyk et al. 2013).  Thus, TARPs modulate the pharmacology and gating of AMPA-type glutamate receptors (Soto et al. 2014).  TARPs interact with the N-terminal domain of the AMPAR and control channel gating; residues in the receptor and the TARP involved in this interaction have been identified (Cais et al. 2014).  The auxilary protein, Shisa9 or CKAMP44 (UniProt acc# B4DS77), has a C-terminal PDZ domain that allows interaction with scaffolding proteins and AMPA glutamate receptors (Karataeva et al. 2014).  The transmembrane domain alone can tetramerize (Gan et al. 2016). The most potent and well-tolerated AMPA receptor inhibitors, used to treat epilepsy, act via a noncompetitive mechanism.  The crystal structures of the rat AMPA-subtype GluA2 receptor in complex with three noncompetitive inhibitors have been solved. The inhibitors bind to a binding site, completely conserved between rat and human, at the interface between the ion channel and linkers connecting it to the ligand-binding domains (Yelshanskaya et al. 2016). The endogenous neuropeptide, cyclopropylglycine, at a physiological concentration of 1 μM, enhances the transmembrane AMPA currents in rat cerebellar Purkinje cells (Gudasheva et al. 2016).

Accession Number:P19490
Protein Name:GluR-K1 aka GRIA1 aka GLUR1
Length:907
Molecular Weight:101579.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate monovalent cations

Cross database links:

Genevestigator: P19490
RefSeq: NP_113796.1   
Entrez Gene ID: 50592   
Pfam: PF01094    PF00060    PF10613   
KEGG: rno:50592   

Gene Ontology

GO:0032279 C:asymmetric synapse
GO:0030054 C:cell junction
GO:0043198 C:dendritic shaft
GO:0043197 C:dendritic spine
GO:0005769 C:early endosome
GO:0005789 C:endoplasmic reticulum membrane
GO:0008328 C:ionotropic glutamate receptor complex
GO:0043025 C:neuronal cell body
GO:0014069 C:postsynaptic density
GO:0045211 C:postsynaptic membrane
GO:0019717 C:synaptosome
GO:0005234 F:extracellular-glutamate-gated ion channel a...
GO:0004970 F:ionotropic glutamate receptor activity
GO:0031489 F:myosin V binding
GO:0030165 F:PDZ domain binding
GO:0042803 F:protein homodimerization activity
GO:0019901 F:protein kinase binding
GO:0031267 F:small GTPase binding
GO:0006811 P:ion transport
GO:0050806 P:positive regulation of synaptic transmission
GO:0031623 P:receptor internalization
GO:0019228 P:regulation of action potential in neuron
GO:0001919 P:regulation of receptor recycling
GO:0048167 P:regulation of synaptic plasticity
GO:0010226 P:response to lithium ion
GO:0035249 P:synaptic transmission, glutamatergic

References (10)

[1] “Cloning by functional expression of a member of the glutamate receptor family.”  Hollmann M.et.al.   2480522
[2] “A family of AMPA-selective glutamate receptors.”  Keinaenen K.et.al.   2166337
[3] “Molecular cloning and functional expression of glutamate receptor subunit genes.”  Boulter J.et.al.   2168579
[4] “Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.”  Sommer B.et.al.   1699275
[5] “Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors.”  Yakel J.L.et.al.   7877986
[6] “Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696.”  Nakazawa K.et.al.   8848293
[7] “Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II.”  Mammen A.L.et.al.   9405465
[8] “SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit.”  Leonard A.S.et.al.   9677374
[9] “Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif.”  Cai C.et.al.   12070168
[10] “Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics.”  Bedoukian M.A.et.al.   16793768
Structure:
2AWW   3SAJ     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 
61:	IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 
121:	FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT 
181:	TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL 
241:	NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 
301:	AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 
361:	RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 
421:	MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 
481:	LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 
541:	MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 
601:	QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 
661:	YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 
721:	TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW 
781:	WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 
841:	GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM 
901:	PLGATGL