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Database: UniProt
Entry: A0A3B3R4D6_9TELE
LinkDB: A0A3B3R4D6_9TELE
Original site: A0A3B3R4D6_9TELE 
ID   A0A3B3R4D6_9TELE        Unreviewed;       900 AA.
AC   A0A3B3R4D6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSPKIP00000012790.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000012790.1}
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. NR1/GRIN1 subfamily. {ECO:0000256|ARBA:ARBA00005374}.
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DR   AlphaFoldDB; A0A3B3R4D6; -.
DR   STRING; 1676925.ENSPKIP00000012790; -.
DR   Ensembl; ENSPKIT00000037193.1; ENSPKIP00000012790.1; ENSPKIG00000000455.1.
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:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:UniProt.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
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; 4.
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:SF377; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
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..17
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           18..900
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027148003"
FT   TRANSMEM        578..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        651..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        829..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          451..811
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          457..523
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   900 AA;  101563 MW;  09A1151F2C2A6A01 CRC64;
     MRLYLLAVFF SCSCARGGCE PKIVNIGAVL SQKRYEQVFK DAVSQANQLY GKDKFKMNAI
     SVTHKPNAIQ MALSVCEDLI SNQVYAILVS HPPQSNDHLT PTPVSYTAGF YRIPVMGLTT
     RMSIYSDKSI HLSFLRTVPP YSHQANVWFD LMREFRWSHI ILIVSDDHEG RAAQKRLETL
     LEERETKNKN RNYENLDQLS YDNKRGPKAE KVLLFSQDTN ITAMLKEAKD LEARVFILSA
     SEEDAAAVYK AARQLNMTGS GYVWMVGERE MSGKALSEAP DGLIGLQLIN GKNESAHIND
     AVAVVAQSIQ ELFEKENITE PPRGCVGNTN IWKTGPLFKR VLMSSKFPEG LTGRVEFNDD
     GDRKFAHYNI LNYQKSRLIQ VGLFNGTQVV LNNQKKIIWP GGETEKPRGY QMSTRLKIVT
     IHQEPFVYVK PTLHDGTCRE EYTVNGVLIK KVICTGPNET IPGRPIVPQC CYGFCIDLLI
     KLAMTLNFTY EVHLVADGKF GTQERVNNSN KKEWNGMMGE LLGGQADMIV APLTINNERA
     QYIEFSKPFK YQGLTILVKK EIPRSTLDSF MQPFQSTLWL LVGLSVHVVA VMLYLLDRFS
     PFGRFKVNSE EEEEDALTLS SAMWFSWGVL LNSGIGEGAP RSFSARILGM VWAGFAMIIV
     ASYTANLAAF LVLDRPEERI TGINDPRLRN PSDKFIYATV KQSSVDIYFR RQVELSTMYR
     HMEKHNYESA AEAIQAVRDN KLHAFIWDSA VLEFEASQKC DLVTTGELFF RSGFGIGMRK
     DSPWKQNVSL AILSSHENGF MEDLDKTWVR YQECDSRSNA PATLTFENMA GVFMLVAGGI
     VAGIFLIFIE IAYKRHKDAR RKQMQLAFAA VNVWRKNLQP YPTDITGQLN LSDPSVSTVV
//
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