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Database: UniProt
Entry: A0A3B4CGT3_PYGNA
LinkDB: A0A3B4CGT3_PYGNA
Original site: A0A3B4CGT3_PYGNA 
ID   A0A3B4CGT3_PYGNA        Unreviewed;       909 AA.
AC   A0A3B4CGT3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIK2 {ECO:0000313|Ensembl:ENSPNAP00000010663.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010663.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000010663.1}
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. GRIK2 subfamily. {ECO:0000256|ARBA:ARBA00038119}.
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DR   RefSeq; XP_017563713.1; XM_017708224.1.
DR   RefSeq; XP_017563714.1; XM_017708225.1.
DR   AlphaFoldDB; A0A3B4CGT3; -.
DR   STRING; 42514.ENSPNAP00000010663; -.
DR   Ensembl; ENSPNAT00000035803.1; ENSPNAP00000010663.1; ENSPNAG00000016277.1.
DR   GeneID; 108433570; -.
DR   CTD; 2898; -.
DR   GeneTree; ENSGT00940000155610; -.
DR   OMA; YHRWREV; -.
DR   OrthoDB; 511851at2759; -.
DR   Proteomes; UP000261440; 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   CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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:SF38; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 2; 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   Signal {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..32
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           33..909
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027165919"
FT   TRANSMEM        564..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        640..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        821..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          433..802
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          443..508
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   909 AA;  102834 MW;  B72451F51CF0C713 CRC64;
     MKITSPLITH ARFRCCVRLL LLPLLCVGYS RGMPHVLRFG GIFESIETGP SGAEELAFKF
     ALNTINRNRT LLPNTTLTYD IQRINIHDSF EASRKACDQL SLGVAAIFGP SHSSSANAVQ
     SICNALGVPH IQTKWKHQVS DNRDSFYVSL YPDFSSLSRA ILDLVHFFKW RMVTVVYDDS
     TGLIRLQELI KAPSRYNIRL KIRQLPAETK DAKPLLKEMK RGKEFHVIFD CGHEMAAGIL
     KQALAMGMMT EYYHYIFTTL DLFALDVEPY RYSGVNMSGF RILNTENSQV SSIIEKWSME
     RLQAPPKPDS GLLDGFMTTD AALMYDAVHV VAVAVQQSPQ ITVSSLQCNR HKPWRFGNRF
     MTLIKEAHWD GLTGRINFNK TNGLRTDFDL DVISLKEEGL EKIGTWDPVS GLNMTEHQKG
     KMANVSDSLT NRTLYVSTIL EEPYVMFKKS DKPLHGNDRF EGYCIDLLRE LANILGFVYE
     VRLVEDGKYG AQEESTGQWN GLVRELMDHK ADLAVAPLAI TYVREKVIDF SKPFMTLGIS
     ILYRKPNGTN PGVFSFLNPL SPDIWMYILL AYLGVSCVLF VIARFSPYEW YNPHPCNPDS
     DVVENNFTLL NSFWFGVGAL MQQGSELMPK ALSTRIVGGI WWFFTLIIIS SYTANLAAFL
     TVERMESPID SADDLAKQTK IEYGVVEDGS TMTFFKKTKI STYDKMWEFM SSRRHSVMVK
     SVEEGIQRVL TSDYAFLMES TTIEYVTQRN CNLTQIGGLI DSKAYGVGTP MGSPYRDKIT
     IAILQLQEEG KLHMMKEKWW RGNGCPEEES KEASALGVQN IGGIFIVLAA GLVLSVFVAV
     GEFLYKSKQN AQLEKRSFCS AMVEELRVSL KCQRRLKHKP QPPVMVKTEE VINMHTFNDR
     RLPGKETMA
//
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