ID A0A2K5YKX0_MANLE Unreviewed; 895 AA.
AC A0A2K5YKX0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK1 {ECO:0000313|Ensembl:ENSMLEP00000016219.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000016219.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000016219.1}
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|ARBA:ARBA00034104,
CC ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
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; A0A2K5YKX0; -.
DR Ensembl; ENSMLET00000039685.1; ENSMLEP00000016219.1; ENSMLEG00000032142.1.
DR GeneTree; ENSGT00940000156253; -.
DR Proteomes; UP000233140; 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: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:UP000233140};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 555..574
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 631..653
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 812..836
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 425..793
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 435..499
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 895 AA; 101088 MW; 75CA8224F5929D89 CRC64;
MGHLDGGSET ALRPPSGGIF ETVENEPVNV EELAFKFAVT SINRNRTLMP NTTLTYDIQR
INLFDSFEAS RRACDQLALG VAALFGPSHS SSVSAVQSIC NALEVPHIQT RWKHPSVDNK
DLFYINLYPD YAAISRAILD LVLYYNWKTV TVVYEDSTGL IRLQELIKAP SRYNIKIKIR
QLPSGNKDAK PLLKEMKKGK EFYVIFDCSH ETAAEILKQI LFMGMMTEYY HYFFTTLDLF
ALDLELYRYS GVNMTGFRLL NIDNPHVSSI IEKWSMERLQ APPRPETGLL DGMMTTEAAL
MYDAVYMVAI ASHRASQLTV SSLQCHRHKP WRLGPRFMNL IKEARWDGLT GHITFNKTNG
LRKDFDLDII SLKEEGTEKA AGEVSKHLYK VWKKIGIWNS NSGLNMTDSN KDKSSNITDS
LANRTLIVTT ILEEPYVMYR KSDKPLYGND RFEGYCLDLL KELSNILGFI YDVKLVPDGK
YGAQNDKGEW NGMVKELIDH RADLAVAPLT ITYVREKVID FSKPFMTLGI SILYRKPNGT
NPGVFSFLNP LSPDIWMYVL LACLGVSCVL FVIARFTPYE WYNPHPCNPD SDVVENNFTL
LNSFWFGVGA LMQQGSELMP KALSTRIVGG IWWFFTLIII SSYTANLAAF LTVERMESPI
DSADDLAKQT KIEYGAVRDG STMTFFKKSK ISTYEKMWAF MSSRQQTALV RNSDEGIQRV
LTTDYALLME STSIEYVTQR NCNLTQIGGL IDSKGYGVGT PIGSPYRDKI TIAILQLQEE
GKLHMMKEKW WRGNGCPEED NKEASALGVE NIGGIFIVLA AGLVLSVFVA IGEFIYKSRK
NNDIEQAFCF FYGLQCKQTH PTNSTSGTTL STDLECGKLI REERGIRKQS SVHTV
//
