ID A0A3B4T444_SERDU Unreviewed; 877 AA.
AC A0A3B4T444;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK2 {ECO:0000313|Ensembl:ENSSDUP00000000845.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000845.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000000845.1}
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 AlphaFoldDB; A0A3B4T444; -.
DR STRING; 41447.ENSSDUP00000000845; -.
DR Ensembl; ENSSDUT00000000890.1; ENSSDUP00000000845.1; ENSSDUG00000000651.1.
DR GeneTree; ENSGT00940000155610; -.
DR Proteomes; UP000261420; 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 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 532..551
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 608..630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 789..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 401..770
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 411..476
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 877 AA; 99151 MW; 4681CF11EC85B364 CRC64;
MPHVLRFGGI FESIESGPSG AEELAFKFAL NTINRNRTLL PNTTLTYDIQ RINIFDSFEA
SRKACDQLSL GVAAIFGPSH SSSANAVQSI CNALGVPHIQ TKWKHQVSDN RDSYYVSLFP
DFSSLSRAIL DLVHFFKWRT VTVVYDDSTG LIRLQELIKA PSRYNIRLKI RQLPTETKDA
KPLLKEMKKA KEFHVIFDCG HEMAAWILKQ ALAMGMMTEY YHYIFTTLDL FALDMEPYRY
SGVNMTGFRI LNTENSQVSS IIEKWSMERL QAPPKPDSGL LDGFMTTDAA LMYDAVHVVA
VAVQQSQQIT VSSLQCNRHK PWRFGGRFIS LIKEAHWDGL TGRVLFNKTN GLRTDFDLDV
ISLKEEGLEK IGTWDPPSGL NMTETHKSKT SNITDSLANK SLRVSTILEE PYVMFKKSDK
PLYGNDRFEG YCIDLLRELS AILGFRYEVR LVEDGKYGAL DESTGQWNGM VRELMDHKAD
LAVAPLAITY VREKVIDFSK PFMTLGISIL YRKPNGTNPG VFSFLNPLSP DIWMYILLAC
LGVSCVLFVI ARFSPYEWYN PHPCNPDSDV VENNFTLLNS FWFGVGALMQ QGSELMPKAL
STRIVGGIWW FFTLIIISSY TANLAAFLTV ERMESPIDSA DDLAKQTKIL YGVVEDGATM
TFFKKTKIST YDKMWEFMNS RRQSVMVKNV DEGIQRVLTS DYAFLMESTT IEFVTQRNCN
LTQIGGLIDS KAYGVGTPMG SPYRDKITIA ILQLQEEGKL HMMKEKWWRG NGCPEEESKE
ASALGVQNIG GIFIVLAAGL VLSVFVAVGE VLYKSKQNAQ LEKRSFCSAM MDELRVSLKC
QRRLKQKPQP PVIVKTEEVI NMHTFNDRRL PGKETMA
//
