ID A0A3P9QEK0_POERE Unreviewed; 891 AA.
AC A0A3P9QEK0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIA2 {ECO:0000313|Ensembl:ENSPREP00000032581.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000032581.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000032581.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000032581.1};
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}. Endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic density membrane
CC {ECO:0000256|ARBA:ARBA00037872}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037872}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA2 subfamily. {ECO:0000256|ARBA:ARBA00037989}.
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 RefSeq; XP_008417219.1; XM_008418997.2.
DR AlphaFoldDB; A0A3P9QEK0; -.
DR Ensembl; ENSPRET00000032950.1; ENSPREP00000032581.1; ENSPREG00000022050.1.
DR GeneID; 103470494; -.
DR GeneTree; ENSGT00940000156950; -.
DR OrthoDB; 511851at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000022050; Expressed in head.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR CDD; cd13715; PBP2_iGluR_AMPA; 1.
DR Gene3D; 1.10.287.70; -; 2.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF99; GLUTAMATE RECEPTOR 2; 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 Pfam; PF00497; SBP_bac_3; 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.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367118};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 26..891
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027162713"
FT TRANSMEM 542..564
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 625..647
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 815..837
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 415..790
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 425..490
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 891 AA; 99801 MW; 9CF54AD038E943D4 CRC64;
MACRRPDSTM KLLLVMTFLF RQAFSGSPSV QIGGLFPRGA DQEYSAFRVG MVQFGMADFR
LTPHIDNLEV ANSFAVTNCF CSQFSRGVYA IFGFYDKKSV NTITSFCETL HVSFITPSFP
AEGMNQFVLQ MRPDIKGPLV ALVEYYKWEK FAYLYDSDRG LSTLQVILDT AAEKEWVVTA
INVGDLKDES KDEAYRSLFQ DLEIRKERRI ILDCEQDKVK DIMEQVITIG KHVKGHHYII
ANLGFLDGDI SKIQYGGANV SGFQIVDFDN PVVAKFDQRW EALEEKEYPG ADTRIRYTSA
LTYDAVNVMT EAFRFLHKQR IDMSRRGNSG DCLANPAVPW AQGVEIERAL KQVQVNGLTG
NIQFNQHGKR TNYSVAVMEL KNSGPLKIGT WSEAHKFEAD KQDINNDTTG IENKTVIVTT
ILEAPYVMLK KNADELQGND RYEGYCVDLA AEIAKHCGIR YKLRIVGDGK YGARDAETKI
WNGMVGELVY GKADIAVAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWTLEEPEDG ALPLTTESTN EFGIFNSLWF
SLGAFMRQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
AKQTEIAYGT LDSGSTKEFF RRSKIALFDK MWQYMKSAEP SVFVKKTSEG VQRVRKSKGK
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKQ SPLRNAVNLA VLKLNEQGLL
DKLKNKWWYD KGECGSGGGE SKEKTSALSL SNVAGVFYIL VGGLGLAMMV ALVEFCYKSR
AEAKKMKMKF TDAMRSKARL SITGSTSENG RVPVAYLRPG LPMSLSMTDL S
//