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Database: UniProt
Entry: A0A087XB16_POEFO
LinkDB: A0A087XB16_POEFO
Original site: A0A087XB16_POEFO 
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}.
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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
//
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