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Database: UniProt
Entry: H2SJS1_TAKRU
LinkDB: H2SJS1_TAKRU
Original site: H2SJS1_TAKRU 
ID   H2SJS1_TAKRU            Unreviewed;      1093 AA.
AC   H2SJS1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN   Name=GRIK5 {ECO:0000313|Ensembl:ENSTRUP00000012654.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000012654.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000012654.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000012654.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; H2SJS1; -.
DR   STRING; 31033.ENSTRUP00000012654; -.
DR   Ensembl; ENSTRUT00000012715.3; ENSTRUP00000012654.3; ENSTRUG00000003234.3.
DR   eggNOG; KOG1052; Eukaryota.
DR   GeneTree; ENSGT00940000158852; -.
DR   InParanoid; H2SJS1; -.
DR   OMA; SQYCNGY; -.
DR   OrthoDB; 511851at2759; -.
DR   TreeFam; TF334668; -.
DR   Proteomes; UP000005226; Chromosome 12.
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; 3.40.50.2300; -; 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: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:UP000005226};
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..27
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   CHAIN           28..1093
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT                   /id="PRO_5027140966"
FT   TRANSMEM        554..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        633..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        813..837
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          425..794
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          435..499
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          988..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1033
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1085
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1093 AA;  121192 MW;  BC5017A61C9BF80B CRC64;
     MPALPALLLS YVFIPLLTVA PLPFAWADTP AALRMAAILD DQSLCGRGER LALALARENA
     NSLMEGSSQS RVEVDIYELK NDSQYTTTDT MCQILPKGVV SVIGPASSPA SSSAVSHICG
     EKEIPHVKIG PEETPKLPYL RFASVTLHPS NEDLSLAIGS ILRSFSYPTT SIICAKAECL
     LRLEELVQSF LISRETLSVR MLDDSLDPTP LLKEIRDDKV ATIIIDANAS VSYRILKKAN
     ELGMMSAFYK YILTTMDFPL LWLDNVVGDQ SNVLGFSMLN SSHVFYLDFI RSLNLSWREG
     CRINPYPGPA LSSALMFDAV HVVVSAVRQL NRSQEIGVRP LSCTSPLIWQ HGTSLMNYLR
     MVEHDGLTGH IEFNSRGQRT NYTLRILERH PGGHKEIGTW FSNNTLVMNS TSLDLNASET
     LANKTLTVTT ILENPYVMRK SNHQDFQGNN QYEGFCVDML RELADILKFS FKIKLVDDGL
     YGAPEPNGSW TGMVGELINR KADLAVAGFT ITSEREKVID FSKPFMNLGI SILYRVHLGR
     KPGYFSFLDP FSPAVWLFML LAYLAVSCVL FLAARLSPYE WYNPHPCLRE RRDILENQYT
     LGNSLWFPVG GFMQQGSEVM PRALSTRCVS GVWWAFTLII ISSYTANLAA FLTVQRMEAP
     IESPDDLADQ TNIQYGTIHG GSTMTFFMNS RYQTYQRMWN YMYSKQPSVF VKSTEEGIAR
     VLNSRYAFLM ESTMNEYYRS LNCNLTQIGG LLDTKGYGIG MPLGSPFRDE ITLGILQLQE
     SNRLEILKRR WWEGGQCLRE EDHRAKGLGM ENIGGIFVVL ICGLIIAVFV AIMEFVWSTR
     RSADTDEVSV CQEMLSEFRN AVCCKKSSRS RRRRPLTGAG VGVLRHPSRL ALAAPRPIRL
     VRDMRFSNGK LYGGAGRLSG TPRGVGGADL GPGPQKLLEE PMCVNATGSA LTPPLPTLVA
     PPMLPRGFLQ GCSHVRICQE CRRIQNLRPT ALTPPPPPPP SSSSSTSSCS RVPASAPHRR
     HGLHHHLHHH RGSMSLPRLP PPSTPSPTDR ADSDGGGTGS PRRASMKPPP PPRPMPPPKT
     PPRPPTDLLG GHN
//
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