ID A0A3B3BJH0_ORYME Unreviewed; 909 AA.
AC A0A3B3BJH0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK2 {ECO:0000313|Ensembl:ENSOMEP00000005369.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000005369.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000005369.1}
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. GRIK2 subfamily. {ECO:0000256|ARBA:ARBA00038119}.
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DR AlphaFoldDB; A0A3B3BJH0; -.
DR STRING; 30732.ENSOMEP00000005369; -.
DR PaxDb; 30732-ENSOMEP00000005369; -.
DR Ensembl; ENSOMET00000007602.1; ENSOMEP00000005369.1; ENSOMEG00000006383.1.
DR GeneTree; ENSGT00940000155610; -.
DR OMA; HVQTKWK; -.
DR Proteomes; UP000261560; Unplaced.
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; cd06382; PBP1_iGluR_Kainate; 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; 1.
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:SF38; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 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 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 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 TRANSMEM 564..583
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 640..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 821..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 433..802
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 443..508
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 909 AA; 102785 MW; BAB07FB67672A437 CRC64;
MKITSHHLTI TSLVLNLRLL PLLLLFLGYT HGMPHVLRFG GIFESIESGP SGAEELAFKF
ALNTINRNRT LLPNTTLTYD IQRINIFDSF EASRKACDQL SLGVAAIFGP SHSSSANAVQ
SICNALGVPH IQTKWKHQVS DNRDSYYVSL FPDFSSLSRA ILDLVHFFKW RTVTVVYDDS
TGLIRLQELI KAPSRYNIRL KIRQLPTETK DAKPLLKEMK KAKEFHVIFD CGHEMAAWIL
KQALAMGMMT EYYHYIFTTL DLFALDMEPY RFSGVNMTGF RILNTENSQV SSIIEKWSME
RLQAPPKPDS GLLDGFMTTD AALMYDAVHV VAVAVQQSQQ ITVSSLQCNR HKPWRFGGRF
INLIKEAHWD GLTGRVLFNK SNGLRTDFDL DVISLKEEGL EKIGTWDPPS GLNMTESHKS
KTSNITDSLA NKSLRVSTIL EEPYVMFKKS DKPLYGNDRF EGYCIDLLRE LSGILGFRYE
VRLVEDGKYG ALDENTGQWN GMVRELMDHK ADLAVAPLAI TYVREKVIDF SKPFMTLGIS
ILYRKPNGTN PGVFSFLNPL SPDIWMYILL ACLGVSCVLF VIARFSPYEW YNPHPCNPDS
DVVENNFTLL NSFWFGVGAL MQQGSELMPK ALSTRIVGGI WWFFTLIIIS SYTANLAAFL
TVERMESPID SADDLAKQTK IPYGVVEDGA TMTFFKKTKI STYDKMWEFM NSRRQSVMVK
NVEEGIQRVL TSDYAFLMES TTIEFVTQRN CNLTQIGGLI DSRAYGVGTP MGSPYRDKIT
IAILQLQEEG KLHMMKEKWW RGNGCPEEES KEASALGVQN IGGIFIVLAA GLVLSVFVAV
GEVLYKSKQN AQLEKRSFCS AMMDELRVSL KCQRRLKQKP QPPVIVKTEE VINMHTFNDR
RLPGKETMA
//
