GRIA4_MACFA
ID GRIA4_MACFA Reviewed; 902 AA.
AC Q38PU5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Glutamate receptor 4;
DE Short=GluR-4;
DE Short=GluR4;
DE AltName: Full=AMPA-selective glutamate receptor 4;
DE AltName: Full=GluR-D;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 4;
DE Short=GluA4;
DE Flags: Precursor;
GN Name=GRIA4; Synonyms=GLUR4;
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 EPB41L1 via its C-terminus (By similarity).
CC Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2,
CC CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 and
CC PRKCG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein. Cell
CC projection, dendrite. Note=Interaction with CNIH2, CNIH3 and PRKCG
CC 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-611
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-837 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-862 by PRKCG; phosphorylation increases
CC plasma membrane-associated GRI4 expression. {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. GRIA4 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ159932; ABA47256.1; -; mRNA.
DR RefSeq; NP_001306367.1; NM_001319438.1.
DR AlphaFoldDB; Q38PU5; -.
DR SMR; Q38PU5; -.
DR STRING; 9541.XP_005579556.1; -.
DR GeneID; 102122335; -.
DR CTD; 2893; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic 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; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..902
FT /note="Glutamate receptor 4"
FT /id="PRO_0000271755"
FT TOPO_DOM 22..544
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 566..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 593..608
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 609..611
FT /evidence="ECO:0000250"
FT TOPO_DOM 612..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 639..813
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 814..834
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 835..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 500..502
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 676..677
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 727
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 862
FT /note="Phosphoserine; by PKC/PRKCG"
FT /evidence="ECO:0000250|UniProtKB:P19493"
FT LIPID 611
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 837
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..331
FT /evidence="ECO:0000250"
FT DISULFID 740..795
FT /evidence="ECO:0000250"
SQ SEQUENCE 902 AA; 100685 MW; 1B84402B971DAB05 CRC64;
MRIISRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA
PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP
SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH
VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA
NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVIKLMDRWK KLDQREYPGS ETPPKYTSAL
TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN
VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DVPTLGNDTA AIENRTVVVT
TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK
IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL
DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW
FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER MVSPIESAED
LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG
KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSSLGNAVNL AVLKLNEPGL
LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS
RAEAKRMKLT FSEAIRNKAR LSITGSVGEN GRVLTPDCPK AVHAGTAIRQ SSGLAVIASD
LP
