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Database: UniProt
Entry: A0A087XJW8_POEFO
LinkDB: A0A087XJW8_POEFO
Original site: A0A087XJW8_POEFO 
ID   A0A087XJW8_POEFO        Unreviewed;      1105 AA.
AC   A0A087XJW8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIK5 {ECO:0000313|Ensembl:ENSPFOP00000006071.2};
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:ENSPFOP00000006071.2, 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:ENSPFOP00000006071.2}
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; AYCK01022090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01022091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016521153.1; XM_016665667.1.
DR   AlphaFoldDB; A0A087XJW8; -.
DR   STRING; 48698.ENSPFOP00000006071; -.
DR   Ensembl; ENSPFOT00000006081.2; ENSPFOP00000006071.2; ENSPFOG00000005765.2.
DR   GeneID; 103130107; -.
DR   KEGG; pfor:103130107; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   GeneTree; ENSGT00940000158852; -.
DR   OMA; TSANIWQ; -.
DR   OrthoDB; 511851at2759; -.
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; cd06394; PBP1_iGluR_Kainate_KA1_2; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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   PANTHER; PTHR18966:SF351; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 5; 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   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   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        552..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        633..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        814..838
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          426..795
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          436..500
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          931..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..971
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1093
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  122079 MW;  FEA4FC4C97CA2438 CRC64;
     MPALPALLLS IYVVVLLLTM APLFFSQANT LSAVRMAAIL DDQSVCGRGE RLALALAREN
     INNQMEDSAQ ARVEVDVYEL QKDSQYDTTD TMCQILPKGV VSVIGPASSP ASGSTISHIC
     GEKEIPHVKI GPEETPKLPY LRFASVTLYP SNEDLSLAIG SILQSFGYPT ASLICAKAEC
     LLRLEELVRH FLISRETLSV RMLDESLDPT PLLKEIRDDK VATIIIDANA SISYHILRKA
     NELGMMSAFY KYILTTMDFP LLQLDDVVGD QSNIVGFSML NISHPFYLDF IRSLNLSWKE
     GCNINPYPGP ALSSALMFDA VHVVVSAVRE LNRSQEIGVK PLSCTSPLIW QHGTSLMNYL
     RMVEYDGLTG HIEFNSKGQR TNYTLKILEK HPAGHKEIGT WYSNNTLAMN STSLDLNASE
     TLANKSLIVT TILENPYVMR KSNYQDFQGN DQYEGFCVDM LRELADILKF SFKIKLVDDG
     LYGAPEPNGS WTGMVGELIN RKADLAVAGF TITSEREKVI DFSKPFMTLG ISILYQVHLA
     RKPGYFSFLD PFSPAVWLFM LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ERRDILENQY
     TLGNSLWFPV GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV
     PIESPDDLAD QTNIQYGTIH GGSTMTFFMN SRYQTYQRMW NYMKSKQPSV FVKSTEEGIA
     RVLNSKYAFL MESTMNEYYR SLNCNLTQIG GLLDTKGYGI GMPLGSPYRD EITLGILQLQ
     ESNRLEILKR RWWEGGQCPK EEDHRAKGLG MENIGGIFVV LICGLIVAVF VAIMEFVWST
     RRTAETGEVS VCQEMLTEFR NAVSCKKSSR ARRRRPLSSA GGGVLRHPSR LALAGPRPIR
     LVREMRLSNG KLYSGTGPLT GGLAGLGAGM ATGPDLGPGP QRLLDDPLGV NSASSNPPAP
     PPMPAFEAPP APPRSFLQSC SHVRICQECR RIQSLRPATL TPPPPPPPSS SSSASSCSRI
     PPSLAMSGHH HRHNPHHPLH YHHGSMSLPR LPPPPPPIST DRADSDGGTT SPLRATNRPA
     PPPRPPPTKA PTYPPTDLLG GHNCA
//
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