ID A0A060WR00_ONCMY Unreviewed; 748 AA.
AC A0A060WR00;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN ORFNames=GSONMT00013481001 {ECO:0000313|EMBL:CDQ69462.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ69462.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ69462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ69462.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-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; FR904669; CDQ69462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WR00; -.
DR STRING; 8022.A0A060WR00; -.
DR PaxDb; 8022-A0A060WR00; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
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: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:SF151; GLUTAMATE RECEPTOR 3; 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 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:UP000193380};
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 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 458..480
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 680..702
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 247..623
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 257..322
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 748 AA; 83687 MW; 37D53CD109038DAD CRC64;
MESAVANNWQ VTARSVGSIV DPTEYKRIIE EMDRRQEKRF LIDCEVGRIN TILEQVVTLG
KNSRGYHYIL ANLGFANMTL DKVFAGGANI TGFQIINPEN PIVTQFIQRW ERLDEREFPE
AKGTPLKYTS ALTHDAVLVL AEAFRYLRRQ RVDVSRRGSA GDCLANPAVP WSQGIDIERA
LKMVQVQGMT GNIQFDSFGR RSNYSIDVYE MKIGGPKKTG YWNEFEKYVF IVDAQVTNES
SSVENRTIVV TTIMESPYVM YKRNYLSLDG NDRYEGYCVD LAAEIAKHVG IRYKLSVVAD
GKYGARDPET KTWNGMVGEL VYGRADIAVA PLTITLVREE VIDFSKPFMS LGISIMIKKP
QKSKPGVFSF LDPLAYEIWM CIVFAYIGVS VVLFLVSRFS PYEWHLDEND EAKDPQSPPD
PPNDFGIFNS LWFSLGAFMQ QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV
ERMVSPIESA EDLAKQTEIA YGTLDSGSTK EFFRRSKIAV YEKMWSYMKS AEPSVFAKTT
PEGVARVRKS KGKFAFLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGVAT PKGSALRNAV
NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKNSCKP CRIETQHLRQ AEKQMVGECG
TKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMTVALIEF CYKSRAETKR LNLAKNAQNF
KPAPPANTQN FATYREGYNV YGTESVKI
//
