ID A0A3B4VI75_SERDU Unreviewed; 891 AA.
AC A0A3B4VI75;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000030294.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000030294.1}
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; A0A3B4VI75; -.
DR Ensembl; ENSSDUT00000030818.1; ENSSDUP00000030294.1; ENSSDUG00000021812.1.
DR GeneTree; ENSGT00940000155677; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR CDD; cd13727; PBP2_iGluR_AMPA_GluR4; 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:SF100; GLUTAMATE RECEPTOR 4; 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 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|ARBA:ARBA00022729};
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 530..552
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 614..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 805..827
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 403..779
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 413..478
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 891 AA; 99770 MW; 4F3625B0C3360BCA CRC64;
MLLIRPVCPP PSPLCSGGLF IRNTDQEYTA FRLAIFLHNT SPNASEAPFN LVPHVDNIET
ANSFAVTNAF CSQYSRGVFA IFGLYDKRSV HTLTSFCSAL HISLITPSFP TEGESQFTLQ
LRPSIRGALL SLLDHYDWNK FVFLYDTDRG YAILQAIMEK AGQNNWQVSA ICVENFNDAN
YRRLLEDLDR RQEKKFVIDL EAERLQNMLE QIVSVGKHVK GYHYIMANLG FKDINLERFM
HGGANVTGFQ LVDFSNPMVI KLMQRWNKLD QREYPGSDAP PKYTSALTYD GVMVMAEAFR
NLRRQKVDIS RRGNAGDCLA NPAAPWNQGI DMERTLKQVR LQGLTGNVQF DHYGRRVNYT
MDVFELKNNG PRRIGYWNDA DKLVLIQDSP LLPNDTSGME NRTVVVTTIM EGPYVMLKKN
WEMYEGNDQY EGYCVDLASE IAKHIGIKYK ISIVPDGKYG ARDPETKIWN GMVGELVYGK
AEIAVAPLTI TLVREEVIDF SKPFMSLGIS IMIKKPQKSK PGVFSFLDPL AYEIWMCIVF
AYIGVSVVLF LVSRFSPYEW HTEEPEEGTD GPPSDQPPNE FGIFNSLWFS LGAFMQQGCD
ISPRSLSGRI VGGVWWFFTL IIISSYTANL AAFLTVERMV SPIESAEDLA KQTDIAYGTL
DSGSTKEFFR RSKIAVYEKM WGYMKSAEPT VFTKTTAEGV ARVRKSKGKY AFLLESTMNE
YTEQRKPCDT MKVGGNLDSK GYGVATPKGS QLRSAVNLAV LKLNEQGLLD KLKNKWWYDK
GECGSGGGGE KDKSSQALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR NEAKRMKLTF
TEAMRNKARL SITGSVGENG RVLTPDCPKA VHTGPPLRQS SGLALVSSEL P
//