ID C7G3L9_PANTR Unreviewed; 1009 AA.
AC C7G3L9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=GRID1 {ECO:0000313|EMBL:BAI22778.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAI22778.1};
RN [1] {ECO:0000313|EMBL:BAI22778.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19737383; DOI=10.1186/1471-2148-9-224;
RA Goto H., Watanabe K., Araragi N., Kageyama R., Tanaka K., Kuroki Y.,
RA Toyoda A., Hattori M., Sakaki Y., Fujiyama A., Fukumaki Y., Shibata H.;
RT "The identification and functional implications of human-specific "fixed"
RT amino acid substitutions in the glutamate receptor family.";
RL BMC Evol. Biol. 9:224-224(2009).
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 EMBL; AB514212; BAI22778.1; -; Genomic_DNA.
DR RefSeq; XP_016774266.1; XM_016918777.1.
DR AlphaFoldDB; C7G3L9; -.
DR GeneID; 100612556; -.
DR KEGG; ptr:100612556; -.
DR CTD; 2894; -.
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 GO; GO:0007215; P:glutamate receptor signaling pathway; IEA:UniProt.
DR CDD; cd06392; PBP1_iGluR_delta_1; 1.
DR CDD; cd13730; PBP2_iGluR_delta_1; 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; 2.
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:SF108; GLUTAMATE RECEPTOR IONOTROPIC, DELTA-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 Signal {ECO:0000256|ARBA:ARBA00022729, 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 SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT CHAIN 21..1009
FT /note="Glutamate receptor"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT /id="PRO_5027137886"
FT TRANSMEM 563..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 637..658
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 831..855
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT DOMAIN 438..807
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 448..510
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 930..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 112129 MW; 83C1BA470149F978 CRC64;
MEALTLWLLP WICQCVSVRA DSIIHIGAIF EENAAKDDRV FQLAVSDLSL NDDILQSEKI
TYSIKVIEAN NPFQAVQEAC DLMTQGILAL VTSTGCASAN ALQSLTDAMH IPHLFVQRNP
GGSPRTACHL NPSPDGEAYT LASRPPVRLN DVMLRLVTEL RWQKFVMFYD SEYDIRGLQS
FLDQASRLGL DVSLQKVDKN ISHVFTSLFT TMKTEELNRY RDTLRRAILL LSPQGAHSFI
NEAVETNLAS KDSHWVFVNE EISDPEILDL VHSALGRMTV VRQIFPSAKD NQKCMRNNHR
ISSLLCDPQE GYLQMLQISN LYLYDSVLML ANAFHRKLED RKWHSMASLN CIRKSTKPWN
GGRSMLDTIK KGHITGLTGV MEFREDSSNP YVQFEILGTT YSETFGKDMR KLATWDSEKG
LNGSLQERPM GSRLQGLTLK VVTVLEEPFV MVAENILGQP KRYKGFSIDV LDALAKALGF
KYEIYQAPDG RYGHQLHNTS WNGMIGELIS KRADLAISAI TITPERESVV DFSKRYMDYS
VGILIKKPEE KISIFSLFAP FDFAVWACIA AAIPVVGVLI FVLNRIQAVR AQSAAQPRPS
ASATLHSAIW IVYGAFVQQG GESSVNSVAM RIVMGSWWLF TLIVCSSYTA NLAAFLTVSR
MDNPIRTFQD LSKQVEMSYG TVRDSAVYEY FRAKGTNPLE QDSTFAELWR TISKNGGADN
CVSSPSEGIR KAKKGNYAFL WDVAVVEYAA LTDDDCSVTV IGNSISSKGY GIALQHGSPY
RDLFSQRILE LQDTGDLDVL KQKWWPHMGR CDLTSHASAQ ADGKSLKLHS FAGVFCILAI
GLLLACLVAA LELWWNSNRC HQETPKEDKE VNLEQVHRRM NSLMDEDIAH KQISPASIEL
SALEMGGLAP TQTLEPTREY QNTQLSVSTF LPEQSSHGTS RTLSSGPSSN LPLPLSSSAT
MPSMQCKHRS PNGGLFRQSP VKTPIPMSFQ PVPGGVLPEA LDTSHGTSI
//
