ID A0A091MWZ2_APAVI Unreviewed; 488 AA.
AC A0A091MWZ2;
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=N311_05012 {ECO:0000313|EMBL:KFP81806.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP81806.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP81806.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP81806.1};
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; KL372976; KFP81806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MWZ2; -.
DR Proteomes; UP000054244; 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; cd13685; PBP2_iGluR_non_NMDA_like; 1.
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 PANTHER; PTHR18966:SF417; GLUTAMATE RECEPTOR-RELATED; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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; 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|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Signal {ECO:0000256|RuleBase:RU367118};
KW Synapse {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..23
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 24..488
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027161724"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 50..404
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 60..116
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT NON_TER 488
FT /evidence="ECO:0000313|EMBL:KFP81806.1"
SQ SEQUENCE 488 AA; 54442 MW; 98113A907672AAD2 CRC64;
MDKGLHFMFF VITTMLLLRE SSQTGEKNDA EIPAVSKSDF GLLYKEGRPT LTVTTILEDP
YVMVRSAELE GYCIDLLTAL AAMLHFSYRV KVVGDGQYGA LSPGGNWTGM VGEILRQEAD
IAVAPLTVTS AREEVVSFTT PFLQTGIGIL LRKDTVSQEM SFFHFLAPFS KETWTGLLFA
YVLTCICLFL VARLSPCEWN EPKNEENHFT FLNSLWFGAG ALALQGVTPR PKALSVRVVA
AVWWLFTIAL LAAYIANFTA LLSSGSEQLP IQTFEDLVKQ RNLEFGTLDG SSTFYFFKNS
KNPIHQMIYE YMDKRRDHVL VKTYQEAVQR VMESNYAFIG ESISQDLAAA RHCNLIRAPE
VIGARGFGIA TPQASPWTKK LSIAVLKLRE SGDLDYLRNK WWETSCLHKS RDRWSPLQPQ
ALGGLFLTLA IGLALGVIAA VVELSNKCRH AAGHVKKSCC SVFTEELCTR LRIKDNSRQS
QETSGRAN
//
