ID A0A3Q3AQ29_KRYMA Unreviewed; 975 AA.
AC A0A3Q3AQ29;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK3 {ECO:0000313|Ensembl:ENSKMAP00000018445.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000018445.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000018445.1}
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 AlphaFoldDB; A0A3Q3AQ29; -.
DR STRING; 37003.ENSKMAP00000018445; -.
DR Ensembl; ENSKMAT00000018701.1; ENSKMAP00000018445.1; ENSKMAG00000013708.1.
DR GeneTree; ENSGT00940000159465; -.
DR OMA; FMQCEIN; -.
DR OrthoDB; 511851at2759; -.
DR Proteomes; UP000264800; 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: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:UP000264800};
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 563..582
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 639..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 823..844
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 433..801
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 443..507
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 875..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 110067 MW; 70EC9820F7DA6752 CRC64;
MRNTWLSPRS AIWEYWTSLI ACLFWIQYSC GMPHVIRIGG IFEQTDGPVS LVSAEELAFK
FAVNNINRNR TLLPNTTLTY DIQRINIYDS FEASRKACDQ LSLGVVAIFG PSHSSSSNAV
QSICNALEVP HIQVRWKHHP MDNKDTFYAN LYPDYSSLSY AILDLVQFLK WKTATVVYDD
STGLIRLQEL IMAPSRYNIR LKIRQLPLDT QDTRPLLKEM KRSREFRIIF DCSHHMAAQI
LKQAQTMGMM TEYYHYIFTT LDLMAIDLEP YRFCGVNMTG FRILNVDNPQ VASIVEKWSM
ERQIPPKPDS GLLEGIMTTD AALTYDAVHI VSVSYQHAPQ MTVNSLQCHR HKPWRFGGRF
MSFIKESHWD GLTGRLSFNK TTGLRTDFDL DIVSLKEDGL EKVGKWSASG GLNITEVPKR
KGMNITDSLA NRSLVVTSIL EEPYVMLKKS DKALVGNDRF EGFCIDLLKE LANILGFTYE
IRLVPDGKYG SQDDKGQWNG MIRELIEHRA DLAMAPLTIT YTREKFIDFS KPFLNMGISI
LYRKPNSTSN GFFSFLNPMT PDIWVYILLA YLGVSCVLFV IARFSPYEWY DAHPCNPGSD
VVENNFTLLN SFWFGVGSLM QQGSELMPKA LSTRIIGGIW WFFTLIIISS YTANLAAFLT
VERMDSPVDS ADDIAKQTKI EYGVVRDGAT MAFFKKSKVS TFEKMWAFMS SRPRTSLVKS
IEDGIQRVLK SDYALITEST TIDYITRRNC NLTQVGGLID SKGYGIGTPL GSPYRDKITI
AILSMLEDGL LHILKEKWWS GNSCLDEERH ETGPMGIQNL GGIFIVLASG LVVSVFVAIA
EFIYKLRKTA EREQVFVQRH GGRDQTVVHL REAGETQASA SSHGEDGCSD QHARLQRPTT
PRKGQHELQH WDDPCVSMTM CSPQGKNLVS NISGTVPEPR DNGIDGITRY TVNHSDIGTL
TKHGQLKMAA SATQV
//
