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1.A.10.1.4
AMPA glutamate receptor 3 (GluR3) (non-selective monovalent cation channel and Ca2+  channel) (Ayalon et al., 2005; Midgett et al., 2012). Regulated by AMPA receptor regulatory proteins (TARPs) including stargazin and CNIH auxiliary subunits (Kim et al., 2010; Straub and Tomita, 2011; Jackson and Nicoll, 2011; Bats et al., 2012; Rigby et al. 2015). The domain architecture of a calcium-permeable AMPA receptor in a ligand-free conformation has been solved (Midgett et al., 2012). The TARP, stargazin, is elevated in the somatosensory cortex of Genetic Absence Epilepsy Rats (Kennard et al. 2011). TARPs alter the conformation of pore-forming subunits and thereby affect antagonist interactions (Cokić and Stein 2008).  The structural basis of AMPAR regulation by TARP gamma2, or stargazin (STZ) involves variable interaction stoichiometries of the AMPAR-TARP complex, with one or two TARP molecules binding one tetrameric AMPAR (Twomey et al. 2016).  The ion channel extracellular collar plays a role in gating and represents a hub for powerful allosteric modulation of AMPA receptor function (Yelshanskaya et al. 2017). The A653T mutation stabilizes the closed configuration of the channel and affects duration of sleep and awake periods in both humans and mice (Davies et al. 2017).

Accession Number:P42263
Protein Name:Glutamate receptor 3 precursor (GluR-3) (GluR-C) (GluR-K3) (Glutamate receptor ionotropic, AMPA 3)
Length:894
Molecular Weight:101157.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate monovalent cations, Ca2+

Cross database links:

Genevestigator: P42263
eggNOG: prNOG16901
HEGENOM: HBG381523
DIP: DIP-46195N
RefSeq: NP_000819.3    NP_015564.4   
Entrez Gene ID: 2892   
Pfam: PF01094    PF00060    PF10613   
Drugbank: Drugbank Link   
OMIM: 300699  phenotype
305915  gene
KEGG: hsa:2892   

Gene Ontology

GO:0030054 C:cell junction
GO:0030666 C:endocytic vesicle membrane
GO:0016021 C:integral to membrane
GO:0045211 C:postsynaptic membrane
GO:0005234 F:extracellular-glutamate-gated ion channel a...
GO:0007215 P:glutamate signaling pathway
GO:0006811 P:ion transport

References (4)

[1] “Human glutamate receptor hGluR3 flip and flop isoforms: cloning and sequencing of the cDNAs and primary structure of the proteins.”  Rampersad V.et.al.   7918660
[2] “Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq.”  Amir R.et.al.   10602120
[3] “The DNA sequence of the human X chromosome.”  Ross M.T.et.al.   15772651
[4] “Mutations in ionotropic AMPA receptor 3 alter channel properties and are associated with moderate cognitive impairment in humans.”  Wu Y.et.al.   17989220
Structure:
5ide     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT 
61:	NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL 
121:	HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA 
181:	AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS 
241:	RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN 
301:	APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM 
361:	VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS 
421:	ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY 
481:	GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS 
541:	KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP 
601:	NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 
661:	MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD 
721:	GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRNAVNL 
781:	AVLKLNEQGL LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM 
841:	VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI