ID A0A3Q1F7X9_9TELE Unreviewed; 882 AA.
AC A0A3Q1F7X9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000012384.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000012384.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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 AlphaFoldDB; A0A3Q1F7X9; -.
DR Ensembl; ENSAPOT00000031989.1; ENSAPOP00000012384.1; ENSAPOG00000015132.1.
DR GeneTree; ENSGT00940000156123; -.
DR InParanoid; A0A3Q1F7X9; -.
DR OrthoDB; 511851at2759; -.
DR Proteomes; UP000257200; 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; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..882
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027153674"
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 TRANSMEM 814..836
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 882 AA; 99719 MW; D75524FA9883EC1B CRC64;
MAQRVVFFLL WLLDRSFAGF PNQINIGGLF MRSTVQEHSA FRFAVQLYNT NQNTTEKPFH
LNYNVDNLES SNSFSVTHAF CSQFSRGVYA IFGFYDKKSM NTLTSFCGAL HTSFVTPSYP
TDNEVQFVIQ MRPALRGAVL SLLSHYKWQK FVYLYDTDRG FSILQAIMEA AVANNWQVTA
RSVSSTTDAA EFKRIIEEMD RRQEKQYVID CEVDRINTIL EQVVTLGKNS RGYHYILANL
GFSNVSLDKV FAGGANISGF QIVNPENPIV QQFMQRWERL DEREFPEARN APLKYTSALT
HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKT VQVLGMTGNI
QFDNYGRRTN YTIDVYEMKT GGPRKIGYWN EYSRFVNIMD PQVSNDSSVE NRTIVVTTIM
EAPYVMYKKN YMHLEGNDRY EGYCVDLATE IAKHVGIKYK LSIVMDGKYG ARDPETKAWN
GMVGELVYGR ADIAVAPLTI 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 ALRTPVNLAV LKLSEQGILD
KLKNKWWYDK GECGTKDSGS KDKTSALSLS NVAGVFYILV GGLGLAMMVA LIEFCYKSRQ
ETKRLKLAKN AQNFKPAPPT NTQNFATYRE GYNVYGTESV KI
//