ID A0A091XHA8_OPIHO Unreviewed; 832 AA.
AC A0A091XHA8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
DE Flags: Fragment;
GN ORFNames=N306_02779 {ECO:0000313|EMBL:KFR12606.1};
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:KFR12606.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR12606.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR12606.1};
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}. Endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic density membrane
CC {ECO:0000256|ARBA:ARBA00037872}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037872}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA2 subfamily. {ECO:0000256|ARBA:ARBA00037989}.
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 EMBL; KK735119; KFR12606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091XHA8; -.
DR STRING; 30419.A0A091XHA8; -.
DR PhylomeDB; A0A091XHA8; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density 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:SF99; GLUTAMATE RECEPTOR 2; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 557..579
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 747..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 347..722
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 357..422
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR12606.1"
FT NON_TER 832
FT /evidence="ECO:0000313|EMBL:KFR12606.1"
SQ SEQUENCE 832 AA; 92996 MW; E6702F74ADB68061 CRC64;
NCFSFSFLVC SQFSRGVFAI FGFYDKKSVN TITSFCGTLH VSFITPSFPT DGTHPFVIQM
RPDLKGALLS LIEYYQWTKF AYLYDSDRGL STLQAVLDSA AEKKWQVTAI NVGNINNDRK
DETYRSLFQD LEVKKERRVI LDCERDKVND IVDQVITIGK HVKGYHYIIA NLGFTDGDLS
KIQFGGANVS GFQIVDYDDP LVSKFIQRWS TLEEKEYPGA HTSTIKYTSA LTYDAVQVMT
EAFRNLRKQR IEISRRGNAG DCLANPAVPW GHGVEIERAL KQVQVEGLTG NIKFDQNGKR
INFTINVMEL KSTGPRKIGY WSEVDKMVVN PLDGPLGNES SGLENKTIIV TTILESPYVM
MKKNHEMLEG NDRYEGYCVD LATEIAKHCG FKYKLTIVGD GKYGARDADT KIWNGMVGEL
VYGKADIAIA PLTITLVREE VIDFSKPFMS LGISIMIKKP QKSKPGVFSF LDPLAYEIWM
CIVFAYIGVS VVLFLVSRFS PYEWHTEEFE DGRETQTNES TNEFGIFNSL WFSLGAFMQQ
GCDISPRSLS GRIVGGVWWF FTLIIISSYT ANLAAFLTVE RMVSPIESAE DLSKQTEIAY
GTLDSGSTKE FFRRSKIAVF DKMWTYMKSA EPSVFVRTTA EGVARVRKSK GKYAYLLEST
MNEYIEQRKP CDTMKVGGNL DSKGYGIATP KGSSLRNAVN LAVLKLNEQG LLDKLKNKWW
YDKGECGSGG GDSKEKTSAL SLSNVAGVFY ILVGGLGLAM LVALIEFCYK SRAEAKRMKL
TLYDAMRSKA RLSITGSTGE NGRVMTPEFP KAVHAVPYVS PGMGMNVSVT DL
//
