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Database: UniProt
Entry: G3R6H4_GORGO
LinkDB: G3R6H4_GORGO
Original site: G3R6H4_GORGO 
ID   G3R6H4_GORGO            Unreviewed;       963 AA.
AC   G3R6H4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000010928.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000010928.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000010928.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000010928.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Receptor for glutamate that functions as a 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       {ECO:0000256|RuleBase:RU367118}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
CC       Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|RuleBase:RU367118}.
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DR   EMBL; CABD030110514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030110515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030110516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030110517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030110518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030110519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9593.ENSGGOP00000010928; -.
DR   Ensembl; ENSGGOT00000011252.3; ENSGGOP00000010928.3; ENSGGOG00000011208.3.
DR   eggNOG; KOG1053; Eukaryota.
DR   GeneTree; ENSGT00940000161021; -.
DR   HOGENOM; CLU_002039_0_1_1; -.
DR   InParanoid; G3R6H4; -.
DR   OMA; NCGDLQP; -.
DR   TreeFam; TF314731; -.
DR   Proteomes; UP000001519; Chromosome 19.
DR   Bgee; ENSGGOG00000011208; Expressed in testis and 1 other cell type or tissue.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR   GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0051205; P:protein insertion into membrane; IEA:Ensembl.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd13720; PBP2_iGluR_NMDA_Nr3; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   PANTHER; PTHR18966:SF364; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3B; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU367118};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW   ECO:0000256|RuleBase:RU367118};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW   Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Synapse {ECO:0000256|RuleBase:RU367118};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367118};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367118};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}.
FT   TRANSMEM        510..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        549..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        579..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        755..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          393..727
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          394..457
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          98..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   963 AA;  104387 MW;  DCA5168D83E20E26 CRC64;
     LLPRAPLARA RARAALARAA LAPRLPHNLS LELVVAAPPA RDPASLTRGL CQALVPPGVA
     ALLAFPEARP ELLQLHFLAA ATETPVLSLL RREARAPLGA PVRGTPGVRT RGTRGGGGSP
     GDGRSQDGGA GTTQRRGIPG RWTGPRDQGW GRPGCPRSKE TRTXXXERPC RPLPSALVMG
     TPPLWPLPLP CPGPFPPSPQ TLPWSLGPPG PHPALGGWAG GQAVSLLTLG VQFRGLQVWI
     SLLPVQPKRA LLPAPVNCGD LQPAGPESPG RFLARFLANT SFQGRTGPVW VTGSSQVHMS
     RHFKVWSLRR DPRGAPAWAT VGSWRDGQLD LEPGGASARP PPPQGAQVRP KLRVVTLLEH
     PFVFARDPDE DGQCPAGQLC LDPGTNDSAT LDALFAALAN GSVPRALRKC CYGYCIDLLE
     RLAEDTPFDF ELYIVGDGKY GALRDGRWTG LVGDLLAGRA HMAVTSFSIN SARSQVVDFT
     SPFFSTSLGI MVRARDTASP IGAFMWPLHW SMWLGIFAAL HLTALFLTVC EWCSPYGLTP
     RGRNRSTVFS YSSALNLCYA ILFGRTVSSK TPKCPTGRLL MNLWAIFCLL VLSSYTANLA
     AVMVGDKSFE ELSGIHDPKL HHPAQGFRFG TVWESSAEAY IKKSFPDMHA HMRRHSAPTT
     PHGVAMLTSD PPKLNAFIMD KSLLDYEVSI DADCKLLTVG KPFAIEGYGI GLPQNSPLTS
     NLSELPRGLP LRDLAGLLLC CPQTLQMSIY HFSGLFVLLC LGLGSALLSS LGEHAFFRLA
     LPRIRKRSRL QYWLHTSQKI HRALNTEPPE GSKKETAEAE PTGPEVEQQQ QQDQPTAPEG
     WKRARWAVDK ERRVRFLLEP AVVVAPEADA EAEAAPREGP VWPCSNGRPP AARPTGAPQP
     GELQELDRRI EVARERLRQA LVRRGELLAQ LGDSTRHRPR RLLQARAAPA EAPPHSGRPG
     SQE
//
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