ID W5M5Z0_LEPOC Unreviewed; 920 AA.
AC W5M5Z0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK3 {ECO:0000313|Ensembl:ENSLOCP00000003798.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003798.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003798.1}
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 EMBL; AHAT01009510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01009511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01009512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01009513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006631317.1; XM_006631254.2.
DR AlphaFoldDB; W5M5Z0; -.
DR STRING; 7918.ENSLOCP00000003798; -.
DR Ensembl; ENSLOCT00000003805.1; ENSLOCP00000003798.1; ENSLOCG00000003209.1.
DR GeneID; 102686878; -.
DR KEGG; loc:102686878; -.
DR CTD; 2899; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000159465; -.
DR HOGENOM; CLU_007257_1_1_1; -.
DR InParanoid; W5M5Z0; -.
DR OMA; FMQCEIN; -.
DR OrthoDB; 511851at2759; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000003209; Expressed in brain and 2 other cell types or tissues.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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:SF174; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 3; 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:UP000018468};
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 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 822..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 435..803
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 445..509
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 920 AA; 104379 MW; 2DDBD19C2BF453B2 CRC64;
MRNIWLSSRS VILEYWKALI LCLFWIQYSR GMPHVIRIGG IFEQTEGSPG PVVSAEEQAF
KFAVNNINRN RTLLPNTTLT YDIQRINIYD SFEASRKACD QLSLGVVAIF GPSHSSSSNA
VQSICNALEV PHIQVRWKHH PMDNRDTFYA NLYPDYSSLS YAILDLVQFL KWKTATVVYD
DSTGLIRLQE LIMAPSRYNI RLKIRQLPLD TDDTRPLLKE MKRGREFRII FDCSHTMAAQ
ILKQALAMGM MTEYYHYIFT TLDLFALDLE PYRYCGVNMT GFRILNTDNP QVASIVEKWS
MERLQAAPKP ESGLLDGIMT TDAALTYDAV HIVSVSYQRA PQMTVNSLQC HRHKPWRFGG
RFMNFIKESH WEGLTGRLVF NKTSGLRTDF DLDIISLKED GLEKVGKWSP SGGLNITEVP
RPRGVNITDS LSNRSLVITT ILEEPYVMFK KSDKALAGND RFEGFCIDLL KELANILGFM
YEIRLVPDGK YGSQDEKGQW NGMVKELMDH KADLAVAPLT ISYVREKVID FSKPFMTLGI
SILYRKPNGT NNGVFSFLNP LSPDIWMYIL LAYLGVSCVL FVIARFSPYE WYDAHPCNPG
SDIVENNFTL LNSFWFGVGS LMQQGSELMP KALSTRIIGG IWWFFTLIII SSYTANLAAF
LTVERMESPV ETADDLAKQT KIEYGVVKDG ATMTFFKKSK ISTFEKMWAF MSSKQNTALV
KNNEEGIQRV LKADYALLME STTIEYVTQR NCNLTQIGGL IDTKGYGIGT PMGSPYRDKI
SIAILHLLED GKLHVLKEKW WRGNGCPDDD TKEIRALGIQ NIGGIFIVLA AGLVLSVFVA
IGEFIYKLRK TAEREQRSFC SAMANEIRLS FTCERRVKHK PQPPVMVKTD AVINMHTFND
RRLPGKDNMT CNTGMTPVFP
//
