ID A0A3B3WZG9_9TELE Unreviewed; 1047 AA.
AC A0A3B3WZG9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000008074.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000008074.1}
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 AlphaFoldDB; A0A3B3WZG9; -.
DR Ensembl; ENSPMET00000003064.1; ENSPMEP00000008074.1; ENSPMEG00000010104.1.
DR Proteomes; UP000261480; Unplaced.
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 Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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:SF364; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3B; 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; 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|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, 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 TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 566..585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 597..621
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 411..738
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 420..474
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 888..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 860..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 888..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 116217 MW; C6B6BEA6FA9D2104 CRC64;
PTHLARSRRT MLLCYPKVFS RYSLISRLIF FLLLPLTLSS SSLCSCLSYL TFLVYVSAAA
KMFLRFFFHL FQNRFHLQMS ARVPPSTLGS LLLAVLQSGN GDRDRGSRGE GRWGGAAVIC
PGWDEGSDGL LTHLQRHSGP AWHLWDIINL TLITGGRERR GEASEERRED QMEEEALNII
SSSFLRSPSP ISSVLLMGSD PECLSSVLRA AQRLAPSLPA LQWIMGYPLS PDSLHTLGGP
LGLLAYGEVG RKPISFYIRD ALQLVGRAVT TATMVKPELA LVQNLVNCYD KPNRHELPSS
GQYLSRFLSN ISFTGSTGLI QVDADVSRVL SSQLFHVWSL KRGALGQPAW VTVGQWTRGR
LELEGGILGL GHRLRVVTLV EHPFVFTREV DEDGLCPAGQ LCLDPKTNRT DIINGLFNLP
GDLRKCCYGY CIDLLEKLAE DMGFTFDLYI VGDGKYGALS GTGRWTGLVG DLLNGTADMA
VTSFSINSAR SRVIDFTSPF YSTSLGILVR SRDTAAPIGA FMWPLHWSMW VGIFVTLHLT
ALFLTLYEWN SPFGMTPHGR NRLRVFSYSS ALNLCYAILF GRTVATKTPK CWTGRFLMNL
WAIFCLLVLS SYTANLAAVM VGEKTFEQVS GIHDDKVRPR ASWQVYNWKV FDVQHSAVVV
WKDPPALDAF IMDKALLDFE VSIDADCKLL TVGKPFAIEG YGIGLPQGSP LTRNVSEFVS
RYKSDGFMDM LHDKWYKVVP CGKRVFAVTE TLQMGIQHFS GLFVLLCMGV GGALLTLAGE
HTFYHLVVPR LRRANTLQYW LHTSQVGEHM GRADRHAHSL LLRPHPTVTS RPVSTLASTG
LVLSPLGNRA TQTSLWEGEL QELQVKIETF RNQLREALAR RAEIQTSLDR ERSGVVRRDT
SLDRERDRQR VQTINTDRSS STLSKLPERD RTSQLQTLNN QQTGRPSQTA GAGTAGLGRT
SQLNTVNSLD RGRATQSRPV VTVTGERTVQ SRTSSLERSQ VNQQGAGNII VQTRNTSSLD
RQKANLSRTL NTLERTKANQ SSVSSGT
//
