ID A0A2K6GRT5_PROCO Unreviewed; 927 AA.
AC A0A2K6GRT5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRIK4 {ECO:0000313|Ensembl:ENSPCOP00000028909.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000028909.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000028909.1}
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; A0A2K6GRT5; -.
DR Ensembl; ENSPCOT00000039844.1; ENSPCOP00000028909.1; ENSPCOG00000027128.1.
DR GeneTree; ENSGT00940000159111; -.
DR Proteomes; UP000233160; 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; cd13724; PBP2_iGluR_kainate_KA1; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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:SF171; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 4; 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:UP000233160};
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 518..537
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 595..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 776..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 388..757
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 398..462
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 833..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 104160 MW; D2ACC0ED6D39DFAB CRC64;
ILDDPMECSR GERLSITLAK NRINRAPERL GKAKVEVDIF ELLRDSEYET AETMCQILPK
GVVAVLGPSS SPASSSIISN ICGEKEVPHF KVAPEEFVKF QFQRFTTLNL HPSNTDISVA
VAGILNFFNC TTACLICAKA ECLLNLEKLL RQFLISKDTL SVRMLDDTRD PTPLLKEIRD
DKTATIIIHA NASMSHTILL KAAELGMVSA YYTYIFTNLE FSLQRMDSLV DDRVNILGFS
IFNQSHAFFQ EFAQSLNQSW QENCDHAPFT GPALSSALLF DAVYAVVTAV QELNRSQEIG
VKPLSCGSAQ IWQHGTSLMN YLRMVELEGL TGHIEFNSKG QRSNYALKIL QFTRNGFRQI
GQWHVAEGLS MDSRLYASNI SDSLFNTTLV VTTILENPYL MLKGNHQEME GNDRYEGFCV
DMLKELAEIL RFNYKIRLVG DGVYGVPEAN GTWTGMVGEL IARKADLAVA GLTITAEREK
VIDFSKPFMT LGISILYRVH MGRKPGYFSF LDPFSPGVWL FMLLAYLAVS CVLFLVARLT
PYEWYSPHPC AQGRCNLLVN QYSLGNSLWF PVGGFMQQGS TIAPRALSTR CVSGVWWAFT
LIIISSYTAN LAAFLTVQRM DVPIESVDDL ADQTAIEYGT IHGGSSMTFF QNSRYQTYQR
MWNYMYSKQP SVFVKSTEEG IARVLNSNYA FLLESTMNEY YRQRNCNLTQ IGGLLDTKGY
GIGMPVGSVF RDEFDLAILQ LQENNRLEIL KRKWWEGGKC PKEEDHRAKG LGMENIGGIF
VVLICGLIVA IFMAMLEFLW TLRHSEATEV SVCQEMVSEL RSIILCQDSI HPRRRRSGVP
QPRPPIPEER RPRGTATLSN GKLCGAGEPD QLAQRLAQEA ALVARGCTHI RVCPECRRFQ
GLRARPSPAR SEESLEWEKT TNSSEPE
//
