ID A0A3B4DNG0_PYGNA Unreviewed; 1034 AA.
AC A0A3B4DNG0;
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=GRIK5 {ECO:0000313|Ensembl:ENSPNAP00000025000.1};
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:ENSPNAP00000025000.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000025000.1}
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. {ECO:0000256|RuleBase:RU367118}.
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DR AlphaFoldDB; A0A3B4DNG0; -.
DR Ensembl; ENSPNAT00000008712.1; ENSPNAP00000025000.1; ENSPNAG00000009981.1.
DR GeneTree; ENSGT00940000158852; -.
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; cd06394; PBP1_iGluR_Kainate_KA1_2; 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: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 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 541..560
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 620..641
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 800..824
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 418..781
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 428..492
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 896..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 115377 MW; 8CC39867FB6899F0 CRC64;
MILPALRLKA DIWPWICNWV LSHCVPHPAA ILDDQSACGR GERLALALAR ENINSMMEGP
ARARVEVDIF ELQRDSQYET TDTMCQILPK GVVSVIGPAS SPASGSTVSH ICGEKEIPHI
KIGPEETPRL PYLRFASVTL YPSNEDLSLA IGAILRSFSY PTASLICAKA ECLLRLEELV
RHFLISRDTL SVRMLDDTLD PTPLLKEIRD DKVATIIIDA NASVSILILK KASELGMTSA
FYKYILTTMD FPLLRLDDVV DEQSNIVGFS MLNSSHPFYL EFIRSLNLSW REGCDLSPYP
GPALSSALMF DAVHVVVGAV RELNRSQEIG VKPLSCTSSL IWQHGTSLMN YLRMVEYDGL
TGRVEFNSKG QRTNYTLRIL EKFRGGHKEI GIWYSNNTLA MNSTSLDINT SHTLANKTLI
VTTILEDPYV MRKENYQDFE GNDQYEGFCV DMLRELSDIL KFSFKIKLVD DGLYGAPEPN
GSWTGMVGEL INRKADLAVA EREKVIDFSK PFMTLGISIL YRVHIGRKPG YFSFLDPFSP
AVWLFMLLAY LAVSCVLFLA ARLSPYEWYN PHPCLRERRD LLENQYTLGN SLWFPVGGFM
QQGSEIMPRA LSTRCVSGVW WAFTLIIISS YTANLAAFLT VQRMEVPIES ADDLADQTNI
QYGTIHGGST MTFFMNSRYQ TYQRMWNYMY SKQPSVFVKS TEEGIARVLN SKYAFLLEST
MNEYHRRHNC NLTQIGGLLD TKGYGIGMPL GSPFRDEITL GVLQLQENNR LEILKRRWWE
GGECPKEEDH RAKGLGMENI GGIFVVLICG LIIAVFVAIM EFVWSTRRSA ETDEVSVCQE
MMTEFRNAIS CKKSSRLRRR RPLSSHGILR HPTRLPLGAP RPVRLVREMR LSNGKLYSGS
GPGPLAGAAA GPRLLEDPLG ANMPSTPPPA PLAPMLPPAP PRGCTHVRVC QECRRIQSLR
SASSSCSRIP PLASATSSLP RLPPPPPPSS SNTNTDSEGG GSTSPRRPKP KPTPPPRPVP
PTKTPTTDLL CKQD
//