ID A0A091WYP1_OPIHO Unreviewed; 879 AA.
AC A0A091WYP1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
DE Flags: Fragment;
GN ORFNames=N306_01130 {ECO:0000313|EMBL:KFR06446.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR06446.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR06446.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR06446.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK734338; KFR06446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091WYP1; -.
DR STRING; 30419.A0A091WYP1; -.
DR PhylomeDB; A0A091WYP1; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
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; cd13720; PBP2_iGluR_NMDA_Nr3; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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:SF397; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3A; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367118}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053605};
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 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 483..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 513..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 701..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 320..677
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 336..389
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 813..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..871
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR06446.1"
FT NON_TER 879
FT /evidence="ECO:0000313|EMBL:KFR06446.1"
SQ SEQUENCE 879 AA; 99746 MW; 47FC970478A17700 CRC64;
NPLHLQMSLE NSLSSDADVT FSILAMNNWY NFSLMLCQEE WNITDFLFLT QQSSKFHLGS
IINITANLTS ASDLLNYLQF YLEGIKDTVS TMVMFGCDME KTRRIFEITT QFGVMPPELH
WIIGDSQNVE ELRTEGLPLG LIAHGKTTQS VFEHYVQDAM ELVARAVAAA TMIQPELALI
PSTMNCMDTD ERKIPSGQYL SKFLANTTFD GLSGHIKVKG SSIISSENNF FIWNLQHDPV
GNPMWTRLGS WQEGKIVMDY GIWPEQAQRR KNHMQHPTRL HLRVVTLIEH PFVFTRDVDE
EGLCPAGQLC LDPLTNDSAV LDNLFEILQG GNDTVPIELK KCCYGYCIDL LEKLAEDMNF
EFDLYIVGDG KYGAWKNGHW TGLVGDLLAG TAHMAVTSFS INTARSQVID FTSPFFSTSL
GILVRTRDTA APIGAFMWPL HWTMWLGIFV ALHITAIFLT LYEWKSPFGM TPKGRNRNKV
FSFSSALNVC YAILFGRTAA IKPPKCWTGR FLMNLWAIFC LFCLSTYTAN LAAVMVGEKI
YEELSGIHDP KLHHPSQGFR FGTVRESSAE DYVRQSFPEM HEYMRRYNVP TTPDGVADLK
HDPEKLDAFI MDKALLDYEV SIDADCKLLT VGKPFAIEGY GIGLPPNSPL TSNISELISQ
YKSHGFMDVL HDKWYKVVPC GKRSFAVTET LQMGIKHFSG LFVMLCIGFG LSILTTIGEH
IVYRLVLPRI KKKPKMKYWL HTSQRLHRAL NSSFIEDKRQ PKTKRVEKRS HVGNSQHAVW
NTASLGNCHR KKYICTDEGQ NEVTIQPHQD IPLPQVRRDT PASLTTNGKA ESRSIARTSV
MQELKELEKQ IEIIKQELQL AMDRKSELEE YQRTNRTAE
//
