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Database: UniProt
Entry: A0A3P8UTG8_CYNSE
LinkDB: A0A3P8UTG8_CYNSE
Original site: A0A3P8UTG8_CYNSE 
ID   A0A3P8UTG8_CYNSE        Unreviewed;      1061 AA.
AC   A0A3P8UTG8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRID1 {ECO:0000313|Ensembl:ENSCSEP00000005129.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000005129.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000005129.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000005129.1}
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   RefSeq; XP_016892791.1; XM_017037302.1.
DR   RefSeq; XP_016892792.1; XM_017037303.1.
DR   RefSeq; XP_016892793.1; XM_017037304.1.
DR   RefSeq; XP_016892794.1; XM_017037305.1.
DR   AlphaFoldDB; A0A3P8UTG8; -.
DR   Ensembl; ENSCSET00000005189.1; ENSCSEP00000005129.1; ENSCSEG00000003314.1.
DR   GeneID; 103387089; -.
DR   CTD; 793756; -.
DR   GeneTree; ENSGT00940000155910; -.
DR   InParanoid; A0A3P8UTG8; -.
DR   OrthoDB; 511851at2759; -.
DR   Proteomes; UP000265120; Chromosome 12.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   CDD; cd06392; PBP1_iGluR_delta_1; 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   PANTHER; PTHR18966:SF229; 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   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.
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:UP000265120};
KW   Signal {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..20
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           21..1061
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027134296"
FT   TRANSMEM        564..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        640..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        834..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          439..810
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          449..511
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          883..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  118291 MW;  4A4659C6F1A0C764 CRC64;
     MELLLIYVSL WILQCISTRA DSIIHIGAIF EENAVRDEEI FQLAISDLSL NDDILQSEKI
     THSVKLIEPN NPFQAVQEAC ELMNQGILAL VTSTGCAAAS ALQSLTDAMH IPHLFIQRNA
     EGSPRTACQL NPSPDGESYT LAARPPVRIN DVLLTLVSEL HWRKFIIFYE SDYDIRGLQT
     FMDQASRLGL DVSLQRVDRN VSRVFTDLFS TMQTEELHRY RDTLRRAVLL MSPRGAQVFI
     HQAVETNLAS KDSHWVYANE EVSDPDIMEL VHSSLGRMTI IRQIFPLWRD TNVRCMRNNH
     RISSLLCDPQ EGYLQSLEVS NLYLYDSVLM LANAFYRKLE DRKWHSMASL NCMRKSTKPW
     NGGWSMLDTI QKGRISGLTG QMDFRAEGSN SHVQFEILGT SYSETFGKDV KRLASWDSTR
     GLNGSLKENR IESGMHGVML KIVTVLEEPF VMVAENILGQ PKRYKGFSID VLDALAKLLG
     FKYDIYQVGD GKYGTALPNG SWNGMIGEVI GKRADLAVSA ITITPERESV VDFSKRYLDY
     SVGILMRKTE DKINIFSLLA PFDLAVWACI AAAIPVVGIM IFLLRRIQTA RCQNSTGGHP
     PPSVSTSLQS AIWIVYGAFV QQGSDSVLGT VALRIVMGSW WLFTLIVCSS YTANLAAYLT
     VSRMDNAVRS FQDLSKQVDL VYGTVRDSAV YEYFKAKGTN PLEQDNTFAE LWKTINKNNG
     FENSVTSPTE GIRKVKQGSY AFLWDMAVVE YAALTDDDCT LTVAGNSLST RGYGMALQHG
     SPYRDLFSQK ILELQEKGDL DILKQKWWPK KGRCDVQSYT DAQPEGRSLR LQSFAGVFCI
     LAAGLLLALL VAALETWWNS NQCRREQPKE QVTQDFGMDS VSGPMTYSDI TSTSPAGRRD
     MWTGRERETG KRLRFLTQDK EVNLEQVHQR LNSLLDEDLA HKQLPGQSIE ISALDISSMQ
     PSQSLEALSA RDYSCGPRPI SVTTFLQEGH GTGRTLGAAA GRTLPLPLSS ATMPSIRCKH
     RAPNGGLFRQ SPVKTPMPMA YQPVPGGPIP EGSEPGHGTS I
//
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