GRIA1_MACFA
ID GRIA1_MACFA Reviewed; 906 AA.
AC Q38PU8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Glutamate receptor 1;
DE Short=GluR-1;
DE AltName: Full=AMPA-selective glutamate receptor 1;
DE AltName: Full=GluR-A;
DE AltName: Full=GluR-K1;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 1;
DE Short=GluA1;
DE Flags: Precursor;
GN Name=GRIA1; Synonyms=GLUR1;
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: Ionotropic glutamate receptor. L-glutamate acts as an
CC excitatory neurotransmitter at many synapses in the central nervous
CC system. Binding of the excitatory neurotransmitter L-glutamate induces
CC a conformation change, leading to the opening of the cation channel,
CC and 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 (By similarity). Tetramers may be formed by the
CC dimerization of dimers (By similarity). Found in a complex with GRIA2,
CC GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and
CC CACNG8 (By similarity). Interacts with HIP1 and RASGRF2. Interacts with
CC SYNDIG1 and GRIA2 (By similarity). Interacts with DLG1 (via C-
CC terminus). Interacts with LRFN1. Interacts with PRKG2. Interacts with
CC CNIH2 and CACNG2. Interacts with CACNG5. Interacts (via C-terminus)
CC with PDLIM4 (via LIM domain); this interaction as well as the
CC interaction of PDLIM4 with alpha-actinin is required for their
CC colocalization in early endosomes (By similarity). Interacts with SNX27
CC (via PDZ domain); the interaction is required for recycling to the
CC plasma membrane when endocytosed and prevent degradation in lysosomes.
CC Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain) (By
CC similarity). Interacts with CACNG3; associates GRIA1 with the adapter
CC protein complex 4 (AP-4) to target GRIA1 to the somatodendritic
CC compartment of neurons (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818,
CC ECO:0000250|UniProtKB:P42261}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23818};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P23818}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P19490}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23818}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P23818}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19490}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19490}. Presynapse
CC {ECO:0000250|UniProtKB:P23818}. Synapse {ECO:0000250|UniProtKB:P23818}.
CC Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface
CC expression. Colocalizes with PDLIM4 in early endosomes. Displays a
CC somatodendritic localization and is excluded from axons in neurons (By
CC similarity). Localized to cone photoreceptor pedicles (By similarity).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818}.
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-603
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-829 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-645. Phosphorylated at Ser-710 by PKC.
CC Phosphorylated at Ser-849 by PKC, PKA and CAMK2. Phosphorylated at Ser-
CC 863 by PKC, PKA and PRKG2 (By similarity). Phosphorylation of Ser-863
CC is reduced by induction of long-term depression and increased by
CC induction of long-term potentiation (By similarity).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818}.
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. GRIA1 subfamily. {ECO:0000305}.
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DR EMBL; DQ159929; ABA47253.1; -; mRNA.
DR RefSeq; NP_001306365.1; NM_001319436.1.
DR AlphaFoldDB; Q38PU8; -.
DR SMR; Q38PU8; -.
DR STRING; 9541.XP_005558388.1; -.
DR GeneID; 102123558; -.
DR CTD; 2890; -.
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:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
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; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW Endosome; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..906
FT /note="Glutamate receptor 1"
FT /id="PRO_0000271752"
FT TOPO_DOM 19..536
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 558..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 585..600
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 601..603
FT /evidence="ECO:0000250"
FT TOPO_DOM 604..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 631..805
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 806..826
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 827..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 861..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 903..906
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 492..494
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 668..669
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT LIPID 603
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 829
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..323
FT /evidence="ECO:0000250"
FT DISULFID 732..787
FT /evidence="ECO:0000250"
SQ SEQUENCE 906 AA; 101520 MW; 03EA1E0268F0C58F CRC64;
MQHIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ
FVLQLRPELQ DALISIIDHY KWQKFVYIYD ADRGLSVLQK VLDTAAEKNW QVTAVNILTT
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIIKLE KNGIGYHYIL ANLGFMDIDL
NKFKESGANV TGFQLVNYTD TIPAKIMQQW KNSDARDHTR VDWKRPKYTS ALTYDGVKVM
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW
WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK
GFCLIPQQSI NEAIRTSTLP RNSGAGASSA GSGENGRVVS HDFPKSMQSI PCMSHSSGMP
LGATGL
