GRIA3_MACFA
ID GRIA3_MACFA Reviewed; 894 AA.
AC Q38PU6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Glutamate receptor 3;
DE Short=GluR-3;
DE AltName: Full=AMPA-selective glutamate receptor 3;
DE AltName: Full=GluR-C;
DE AltName: Full=GluR-K3;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 3;
DE Short=GluA3;
DE Flags: Precursor;
GN Name=GRIA3; Synonyms=GLUR3;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=16943768;
RA Hanna M.C., Calkins D.J.;
RT "Expression and sequences of genes encoding glutamate receptors and
RT transporters in primate retina determined using 3'-end amplification
RT polymerase chain reaction.";
RL Mol. Vis. 12:961-976(2006).
CC -!- FUNCTION: Receptor for glutamate that functions as ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC Binding of the excitatory neurotransmitter L-glutamate induces a
CC conformation change, leading to the opening of the cation channel, and
CC thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist. In the presence
CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is
CC characterized by a delayed accumulation of current flux upon continued
CC application of glutamate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity). Found
CC in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3,
CC CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Interaction with CNIH2 and
CC CNIH3 promotes cell surface expression. {ECO:0000250}.
CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is
CC required for cell surface expression. {ECO:0000250}.
CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-621
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-847 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA3 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
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DR EMBL; DQ159931; ABA47255.1; -; mRNA.
DR AlphaFoldDB; Q38PU6; -.
DR SMR; Q38PU6; -.
DR STRING; 9541.XP_005594555.1; -.
DR eggNOG; KOG1054; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..894
FT /note="Glutamate receptor 3"
FT /id="PRO_0000271754"
FT TOPO_DOM 29..552
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 574..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 603..618
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 619..621
FT /evidence="ECO:0000250"
FT TOPO_DOM 622..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 649..823
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 824..844
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 845..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 508..510
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 686..687
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 737
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 877
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT MOD_RES 887
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT LIPID 621
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 847
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..340
FT /evidence="ECO:0000250"
FT DISULFID 750..805
FT /evidence="ECO:0000250"
SQ SEQUENCE 894 AA; 101011 MW; 715B782DCD2514A2 CRC64;
MARQKKMGQN VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT
NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL
HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA
AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS
RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN
APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM
VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS
ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY
GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS
KPGVFSFLDP LAYEIWMCIV FASIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP
NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER
MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD
GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALGNAVNL
AVLKLNEQGL LDKLKNKWWY DKGECGTGGC GSKDKTSALS LSNVAGVFYI LVGGLGLAMM
VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI
