ID A0A3P8QTH1_ASTCA Unreviewed; 1015 AA.
AC A0A3P8QTH1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRID1 {ECO:0000313|Ensembl:ENSACLP00000032374.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000032374.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000032374.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000032374.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3P8QTH1; -.
DR Ensembl; ENSACLT00000033136.1; ENSACLP00000032374.1; ENSACLG00000021863.1.
DR GeneTree; ENSGT00940000155910; -.
DR Proteomes; UP000265100; Chromosome 13.
DR Bgee; ENSACLG00000021863; Expressed in brain and 1 other cell type or tissue.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR CDD; cd06392; PBP1_iGluR_delta_1; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
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 InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF229; GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 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|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Signal {ECO:0000256|RuleBase:RU367118};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, 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 SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 21..1015
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027139548"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 640..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 834..858
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 439..810
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 449..511
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 970..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 112911 MW; 3C9E8B23250FAD9A CRC64;
MELLLICLPL WILQCNSAKA DSIIHIGAIF EENAVRDDQI FQLAISDLSL SDDILQSEKI
THSVKLIQPN NPFQAVQEAC ELMNQGILAL VTSTGCAAAS ALQSLTDAMH IPHLFIQRNG
DGAPRTACQL NPSPDGESYT LAARPPVRIS DVLLTLVSEL HWQKFIIFYE SDYDIRGLQT
FMDQASRLGL DVSLQRVDRN VSRVFSDLFN TMRTEELNRY RDTLRRAVLL MSPRGAQVFV
HQAVETNLAS KDSHWVYANE EVSDADIMEL VHSSLGRMTI IRQIFPLWRD TNVRCMRNNH
RISSLLCDPQ EGYLQSLEVS NLYLYDSVLM LANAFYRKLE DRKWHSMASL NCMRKSTKPW
NGGWSMLDTI QKGRISGLTG LMDFRAEGSN SHVQFEILGT SYSETFGKDV KRLATWDSTR
GLNGSLKENR IESGMHGVTL KIVTLLEEPF VMVAENILGQ PKRYKGFSID VLDALAKILG
FKYDIYQVGD GKYGSALPNG SWNGMIGELI GKRADLAVSA ITITPERESV VDFSKRYLDY
SVGILMHKSE EKINIFSLLA PFDLAVWACI AAAIPVVGIM IFLLRRIQAV RCQNNTAGHP
PPTVSTSLQS AIWIVYGAFV QQGSDSILGS VALRIVMGSW WLFTLIVCSS YTANLAAYLT
VSRMDNAVRS FQDLSKQVDL VYGTVRDSAV YEYFRAKGTN PLEQDSTYAE LWKVINKNNG
FENSVSSPSE GIKKAKRESY AFLWDMAVVE YAALTDDDCT LTIAGNSMST RGYGMALQHG
SPYRDIFSQK ILELQEKGDL DILKQKWWPK KGRCDLQSHT EAQPEGRALR LHSFAGVFCI
LAAGLLLALL VAALETWWNS NHCRREQPKE DKEVNLEQVH QRLNSLLDED LAHKQLPGQS
IEISALDIGS MQPSQSLEAL SVRDYPAHRG PPPLSVTTFL QEGHGAGRTL GASAGRTLPL
PLSSATMPSI RCKHRAPNGG LFRQSPVKTP MPMSYQPVPG GPIPEASEAS HGTSI
//
