ID G1KAD4_ANOCA Unreviewed; 967 AA.
AC G1KAD4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK1 {ECO:0000313|Ensembl:ENSACAP00000002113.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002113.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002113.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002113.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002113.3}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003219092.2; XM_003219044.2.
DR AlphaFoldDB; G1KAD4; -.
DR STRING; 28377.ENSACAP00000002113; -.
DR Ensembl; ENSACAT00000002170.4; ENSACAP00000002113.3; ENSACAG00000002026.4.
DR GeneID; 100552386; -.
DR KEGG; acs:100552386; -.
DR CTD; 2897; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000156253; -.
DR HOGENOM; CLU_007257_1_1_1; -.
DR OrthoDB; 511851at2759; -.
DR TreeFam; TF334668; -.
DR Proteomes; UP000001646; Chromosome 3.
DR Bgee; ENSACAG00000002026; Expressed in testis and 5 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:SF36; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 1; 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:UP000001646};
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 627..649
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 699..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 884..908
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 497..865
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 507..571
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 108984 MW; A18214C417259221 CRC64;
MHECEELEEE EEEEEEEEEE EEEASGGRRQ HGAPQGLLRA PGCCQRCRRP SPRQPAMGVG
AGGWPGRSGG LLFFLLLFLG LAIVPQSAPQ VLRIGGIFET MENEPLNVEE LAFKFAVTNI
NRNTTLTYDI QRINLFDSFE ASRRACDQLA LGVAALFGPS HSSSVSAVQS ICNALEVPHI
QTRWKHPTVD NKDSFYINLY PDYAAISRAV LDLVLHYNWK IVTVVYEDST GLIRLQELIK
APSRYNIKIK IRQLPSGNKD ARPLLKEMKK GKEFYVIFDC SHDTAAEILK QILSMGMMTE
YYHYFFTTLD LFALDLEPYR YSGVNMTGFR LLNIDNVYVS SVIEKWSMER LQAPPKPETG
LLDGMMTTEA ALIYDAVYMV AVASQRASQM TVSSLQCHRH KPWRFGPRFM NLIKEARWDG
LTGRITFNKT DGLRKDFDLD IISLKEEGTE KAAGEVTNHL YKVWKKIGVW NSNSGLNMTD
SNKDRSTNIT DSLANRTLIV TTILEDPYVM YKKSDKPLYG NDRFEGYCLD LLKELSNILG
FIYEVKLVSD GKYGAQNDKG EWNGMVKELI DHKADLAVAP LTITYVREKV IDFSKPFMTL
GISILYRKPN GTNPGVFSFL NPLSPDIWMY VLLACLGVSC VLFVIARFTP YEWYNPHPCN
PDSDVVENNF TLLNSFWFGV GALMQQGSEL MPKALSTRIV GGIWWFFTLI IISSYTANLA
AFLTVERMES PIDSADDLAK QTKIEYGAVR DGSTMTFFKK SKISTYEKMW AFMSSRQQTA
LVKNNDEGIQ RVLTTDYALL MESTSIEYVT QRNCNLTQIG GLIDSKGYGV GTPIGSPYRD
KITIAILQLQ EEGKLHMMKE KWWRGNGCPE EDSKEASALG VENIGGIFIV LAAGLVLSVF
VAIGEFIYKS RKNSDIEQAF CFFYGLQCKQ THPSNSTSGT TLSTELDCGK LIREERGIRT
QPSIHTV
//
