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Database: UniProt
Entry: A0A3B3SPA0_9TELE
LinkDB: A0A3B3SPA0_9TELE
Original site: A0A3B3SPA0_9TELE 
ID   A0A3B3SPA0_9TELE        Unreviewed;      1001 AA.
AC   A0A3B3SPA0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000031881.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000031881.1}
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; A0A3B3SPA0; -.
DR   STRING; 1676925.ENSPKIP00000031881; -.
DR   Ensembl; ENSPKIT00000012738.1; ENSPKIP00000031881.1; ENSPKIG00000012197.1.
DR   GeneTree; ENSGT00940000158016; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:UniProt.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd06379; PBP1_iGluR_NMDA_NR1; 1.
DR   CDD; cd13719; PBP2_iGluR_NMDA_Nr1; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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:SF570; GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF01094; ANF_receptor; 2.
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        633..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        702..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        884..908
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          506..866
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          512..578
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          935..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..958
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  112772 MW;  464EC84FF55B22B0 CRC64;
     MLICGRRSCT FLHCAYRSKS KQNGIGNNNV DRVKRVAQQT SAKTAAVSTG HGWIEMRLML
     MAVFLSCSIA RVGCEPKMVN IGAVLSQKRY EQVFKDAVTQ ANQLYGRDKF KLNAISVTHK
     PNAIQMALSV CEDLISNQVY AILVSHPPQS NDHLTPTPVS YTAGFYRIPV MGLTTRMSIY
     SDKSIHLSFL RTVPPYSHQA HVWFDMMREF RWNHIILIVS DDHEGRAAQK RLETLLEERE
     TKNKKRNYEN LDQLSYDNKR GPKAEKVLQF NQETNITALL VEARELEARV IILSASEEDA
     AAVYKSARYL NMTGSGYVWL VGEREMSGKA LSEAPDGLIG LQLINGKNES AHINDAVAVV
     ARSIQELFEK ENITEPPRGC VGNTNIWKTG PLFKRVLMSS KYPEGLTGRV EFNDDGDRKF
     AHYSILNYQK SRLIQVGVYN GTQVVLNNQR KIIWPGGETE KPRGFQMSTR LKIVTIHQEP
     FVYVKPTLLD GTCKEEFTPN GVLIKKVICT GPNETIPGRP IVPQCCYGFC IDLLIKLAMT
     MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLGGL ADMIVAPLTI NNERAQYIEF
     SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL LDRFSPFGRF
     KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF AMIIVASYTA
     NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL STMYRHMEKH
     NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG IGMRKDSPWK
     QNVSLAILSS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML VAGGIAAGIF
     LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQPSSSLE TQDDRKSGRA EPDPKKKASF
     RSISTSLASS IKRRRSSKDT YPPTDITGQL NLSDPSVSTV V
//
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