ID A0A3P8NPS4_ASTCA Unreviewed; 812 AA.
AC A0A3P8NPS4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
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:ENSACLP00000006806.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000006806.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000006806.1}
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; A0A3P8NPS4; -.
DR Ensembl; ENSACLT00000006958.1; ENSACLP00000006806.1; ENSACLG00000004470.1.
DR GeneTree; ENSGT00940000156123; -.
DR Proteomes; UP000265100; Chromosome 2.
DR Bgee; ENSACLG00000004470; Expressed in camera-type eye and 1 other cell type or tissue.
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; cd13715; PBP2_iGluR_AMPA; 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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF592; 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 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, 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..18
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 19..812
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027154612"
FT TRANSMEM 540..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 624..646
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 413..789
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 423..488
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 812 AA; 91994 MW; ECFACD21EEA040B6 CRC64;
MAQRVVFFLL WLFDRSFAGF PNQINIGGLF MRSTVQEHSA FRFAVQLYNT NQNTTEKPFH
LNYNVDNLES SNSFSVTHAF CSQFSRGVYA IFGFYDKKSM NTLTSFCGAL HTSFVTPSYP
TDNEVQFVIQ MRPALRGAVL SLLSHYKWQK FVYLYDTDRG FSILQAIMEA AVANNWQVTA
RSVSSTTDAA EFKRIIEEMD RRQEKRYVID CEVDRINTIL EQVVTLGKNS RGYHYILANL
GFSNVSLDKV FAGGANISGF QIVNPENPIV QQFIQRWERL DEREFPEARN APLKYTSALT
HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKT VQVQGMTGNI
QFDNYGRRTN YTIDVYEMKT GGPRKIGYWN EYSRFVNIMD LQVSNDSSVE NRTIVVTTIM
EAPYVMYKKN YMHLEGNDRY EGYCVDLASE IAKHVGIKYK LSIVMDGKYG ARDPETKTWN
GMVGELVYGR ADIAIAPLTI TLVREEVIDF SKPFMSLGIS IMIKKPQKSK PGVFSFLDPL
AYEIWMCIVF AYIGVSVVLF LVSRFSPYEW NLEEQDETKD PQTPPDPPND FGIFNSLWFS
LGAFMQQGCD ISPRSLSGRI VGGVWWFFTL IIISSYTANL AAFLTVERMV SPIESAEDLA
KQTEIAYGTL DSGSTKEFFR RSKIAVYEKM WSYMKSAEPS VFVKTTPDGV ARVRKSKGKF
AFLLESTMNE YIEQRKPCDT MKVGGNLDSK GYGVATPKGS ALRNAVNLAV LKLNEQGLLD
KLKNKWWYDK GECGSGGGDS KNSCKPCSIE TQ
//