ID A0A087XB16_POEFO Unreviewed; 1130 AA.
AC A0A087XB16;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIN3A {ECO:0000313|Ensembl:ENSPFOP00000002969.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000002969.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000002969.1}
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}.
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; AYCK01009688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01009689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XB16; -.
DR STRING; 48698.ENSPFOP00000002969; -.
DR Ensembl; ENSPFOT00000002973.1; ENSPFOP00000002969.1; ENSPFOG00000002891.1.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000158571; -.
DR OMA; TIVMFGC; -.
DR Proteomes; UP000028760; 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; 2.
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};
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:UP000028760};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367118};
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 SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 29..1130
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027138029"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 721..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 751..774
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 939..961
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 570..915
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 574..627
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 57..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 125929 MW; 58C660E25D954E51 CRC64;
MRINLWSISP SLCLLLCALL FLSPCAHSHP QPCQVLKRIG HTVRVGALHV QPRLVATAPG
SSSEDAEGAL PRDQPLELGK PAKTGAGALG YGNLRTRAAT NNQRGTSRSK SQARQRDGNP
SKEDGVFSPR ESVLLAAEAL NRAMLLPYNL SLEIVMAVGS ALGELPAFSY SSTGIPEDED
PLSFLESVCH TVVVQGVSAM LAFPRNRDEL VKLEFVSLAL QVPVVSVVQR EFPRHSENRL
HFQMAMRTVA APPSQLLYYL LMMNGWWDFS IVLCQEWKIN DFLFLIKNNS RFHLGTLVNL
TTNSSSKSDQ QQGLMRQLEA LREHSSTRGV VTFGCDIREV RRLWTLATRM TLPEFHWVLG
DSQNVAELRT DGLPLGLLAH GMMGSPSLDH YVQDSLEFVA RAVGSAAQEN PTMALIPGTT
NCMDAQQSNG SSGEFLARFL ANTSFEGQSG FISKESQSQN IISEAHHYIW SLQLDPLGQP
TWTRLGRWRR GRVLMDQGAW PSHQGSGSGG DWRRSARLHM RVVTLVEHPF VFTREVDGDG
MCPAGQLCLD PLTNETSVLK GLFQKLAGHN GSVPTELKKC CYGYCIDLLE KLAEDIGFTF
DLYIVGDGKY GGYKNGRWTG LVGDLLSGAA HLAVTSFSIN SARSQVIDFT SPFFSTSLGI
LVRTRDTAAP IGAFMWPLHW SMWLGIFVSL HVTAVFLTLY EWHSPFGMTP RGRNRNRVFS
FSSALNVCYA ILFGRTVAIK PPKCWTGRLL MNLWAIFCLF CLSTYTANLA AVMVGEKTYE
QLSGIHDPKL HHPSQGFRFA TVRESSAEDY VKKSFPEMHE YMRRYNVPAT PDGIHHLKAD
PQKLDAFIMD KALLDYEVSI DADCKTLTVG KPFAIEGYGI GLPQNSPLTS NFSELVSQYK
SDGFMDMLHD KWYKVVPCGK RSFAVTETLQ MGIKHFSGLF VMLCVGVALS LLTTIAEHIV
YKLVIPRVKE PRSKYWLHTS QRLHRALNSV FIDDKLPSVT KPEKRCNEGN NQSASWNPAE
SSHCNRRRFL PQDIQNDLEH PSSQDLPPPP PPSPRPHPHT LPLLEKHMPI VTTSNGRSDL
TLGQVGQNPL VQELSELEGQ ITAIKLQLQS AMRRKRELER YQTENQQTNQ
//