ID   B4DII7_HUMAN            Unreviewed;      1124 AA.
AC   B4DII7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58499.1};
RN   [1] {ECO:0000313|EMBL:BAG58499.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hippocampus {ECO:0000313|EMBL:BAG58499.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00034430};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00036239};
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004156}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034104, ECO:0000256|RuleBase:RU367118}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00034104,
CC       ECO:0000256|RuleBase:RU367118}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. NR2A/GRIN2A subfamily. {ECO:0000256|ARBA:ARBA00060784}.
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DR   EMBL; AK295620; BAG58499.1; -; mRNA.
DR   AlphaFoldDB; B4DII7; -.
DR   SwissPalm; B4DII7; -.
DR   DNASU; 2903; -.
DR   ClinPGx; PA28979; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-ARBA.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005261; F:monoatomic cation channel activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-ARBA.
DR   GO; GO:0007611; P:learning or memory; IEA:UniProtKB-ARBA.
DR   GO; GO:0045471; P:response to ethanol; IEA:UniProtKB-ARBA.
DR   CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 1.
DR   FunFam; 3.40.190.10:FF:000593; Glutamate ionotropic receptor NMDA type subunit 1; 1.
DR   FunFam; 3.40.50.2300:FF:000344; Glutamate ionotropic receptor NMDA type subunit 2A; 1.
DR   FunFam; 3.40.50.2300:FF:000020; Glutamate receptor ionotropic, NMDA 2B, putative; 1.
DR   FunFam; 3.40.190.10:FF:000007; Putative glutamate receptor ionotropic NMDA 2B; 1.
DR   FunFam; 3.40.190.10:FF:000009; Putative glutamate receptor ionotropic NMDA 2B; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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; IPR018884; NMDAR2_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF10565; NMDAR2_C; 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   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU367118};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601508-3};
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}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        400..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        472..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   TRANSMEM        663..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367118"
FT   DOMAIN          274..641
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          282..345
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          840..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         356
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-1"
FT   BINDING         361
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-1"
FT   BINDING         532
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-1"
FT   BINDING         533
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-1"
FT   BINDING         574
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-1"
FT   SITE            505
FT                   /note="Crucial to convey clamshell closure to channel
FT                   opening"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-2"
FT   SITE            538
FT                   /note="Interaction with the cone snail toxin Con-ikot-ikot"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-2"
FT   DISULFID        588..643
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601508-3"
SQ   SEQUENCE   1124 AA;  127609 MW;  183311901E07BF3E CRC64;
     MLKIMQDYDW HVFSLVTTIF PGYREFISFV KTTVDNSFVG WDMQNVITLD TSFEDAKTQV
     QLKKIHSSVI LLYCSKDEAV LILSEARSLG LTGYDFFWIV PSLVSGNTEL IPKEFPSGLI
     SVSYDDWDYS LEARVRDGIG ILTTAASSML EKFSYIPEAK ASCYGQMERP EVPMHTLHPF
     MVNVTWDGKD LSFTEEGYQV HPRLVVIVLN KDREWEKVGK WENHTLSLRH AVWPRYKSFS
     DCEPDDNHLS IVTLEEAPFV IVEDIDPLTE TCVRNTVPCR KFVKINNSTN EGMNVKKCCK
     GFCIDILKKL SRTVKFTYDL YLVTNGKHGK KVNNVWNGMI GEVVYQRAVM AVGSLTINEE
     RSEVVDFSVP FVETGISVMV SRSNGTVSPS AFLEPFSASV WVMMFVMLLI VSAIAVFVFE
     YFSPVGYNRN LAKGKAPHGP SFTIGKAIWL LWGLVFNNSV PVQNPKGTTS KIMVSVWAFF
     AVIFLASYTA NLAAFMIQEE FVDQVTGLSD KKFQRPHDYS PPFRFGTVPN GSTERNIRNN
     YPYMHQYMTK FNQKGVEDAL VSLKTGKLDA FIYDAAVLNY KAGRDEGCKL VTIGSGYIFA
     TTGYGIALQK GSPWKRQIDL ALLQFVGDGE MEELETLWLT GICHNEKNEV MSSQLDIDNM
     AGVFYMLAAA MALSLITFIW EHLFYWKLRF CFTGVCSDRP GLLFSISRGI YSCIHGVHIE
     EKKKSPDFNL TGSQSNMLKL LRSAKNISSM SNMNSSRMDS PKRAADFIQR GSLIMDMVSD
     KGNLMYSDNR SFQGKESIFG DNMNELQTFV ANRQKDNLNN YVFQGQHPLT LNESNPNTVE
     VAVSTESKAN SRPRQLWKKS VDSIRQDSLS QNPVSQRDEA TAENRTHSLK SPRYLPEEMA
     HSDISETSNR ATCHREPDNS KNHKTKDNFK RSVASKYPKD CSEVERTYLK TKSSSPRDKI
     YTIDGEKEPG FHLDPPQFVE NVTLPENVDF PDPYQDPSEN FRKGDSTLPM NRNPLHNEEG
     LSNKDQYKLY SKHFTLKDKG SPHSETSERY RQNSTHCRSC LSNMPTYSGH FTMRSPFKCD
     ACLRMGNLHD IDEDQMLQET GMTNAWLLGD APRTLTNTRC HPRR
//