NMDA1_DROGR
ID NMDA1_DROGR Reviewed; 982 AA.
AC B4JHV0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000250|UniProtKB:Q24418};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000250|UniProtKB:Q24418}; ORFNames=GH18993;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV92858.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV92858.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC high calcium permeability and voltage-dependent sensitivity to
CC magnesium. Mediated by glycine. This protein plays a key role in
CC synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition
CC and learning. It mediates neuronal functions in glutamate
CC neurotransmission. Is involved in the cell surface targeting of NMDA
CC receptors. Plays a role in associative learning and in long-term memory
CC consolidation (By similarity). {ECO:0000250|UniProtKB:P35439,
CC ECO:0000250|UniProtKB:Q24418}.
CC -!- SUBUNIT: Forms a heteromeric NMDA channel with Nmdar2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q24418};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q24418}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q24418}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q24418}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; CH916369; EDV92858.1; -; Genomic_DNA.
DR RefSeq; XP_001989796.1; XM_001989760.1.
DR AlphaFoldDB; B4JHV0; -.
DR SMR; B4JHV0; -.
DR STRING; 7222.FBpp0152899; -.
DR EnsemblMetazoa; FBtr0154407; FBpp0152899; FBgn0126460.
DR GeneID; 6563892; -.
DR KEGG; dgr:6563892; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; B4JHV0; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; B4JHV0; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IEA:EnsemblMetazoa.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:EnsemblMetazoa.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0072375; P:medium-term memory; IEA:EnsemblMetazoa.
DR GO; GO:0008355; P:olfactory learning; ISS:UniProtKB.
DR GO; GO:0042331; P:phototaxis; IEA:EnsemblMetazoa.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR GO; GO:0050975; P:sensory perception of touch; IEA:EnsemblMetazoa.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 2.
DR Pfam; PF10562; CaM_bdg_C0; 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; SSF53822; 1.
PE 3: Inferred from homology;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..982
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000363995"
FT TOPO_DOM 23..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 948..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 525..527
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 532
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 698
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 742
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 982 AA; 110569 MW; 2DD7E61741C7F996 CRC64;
MRVAFIYRWL LCGAAIVNVL VAQRHTASDN PSTYNIGGVL SNSDSEEHFR TTIAHLNFDQ
QYVPRKVTYY DKTIRMDKNP IKTVFNVCDK LIEKRVYAVV VSHEQTSGDL SPAAVSYTSG
FYSIPVIGIS SRDAAFSDKN IHVSFLRTVP PYYHQADVWL EMLSHFLYTK VIIIHSSDTD
GRAILGRFQT TSQTYYDDVD VRATVELIVE FEPKLESFTE HLIDMKTAQS RVYLMYASTE
DAQVIFRDAG EYNMTGEGHV WIVTEQALHA NNTPDGVLGL QLEHAHSDKG HIRDSVYVLA
SAIKEMISNE TIAEAPKDCG DSAVNWESGK RLFQYLKSRN ITGETGQVAF DDNGDRIYAG
YDVINIREHQ KQHVVGKFSY DSPRGKMRMR INDSEIIWGG KQKRKPEGIM IPTHLKLLTI
EEKPFVYVRR MGDDEFRCEP DERPCPLFNA SGATANEFCC RGYCIDLLIE LSKRINFTYD
LALSPDGQFG HYILRNNSGA MTLRKEWTGL IGELVNERAD MIVAPLTINP ERAEYIEFSK
PFKYQGITIL EKKPSRSSTL VSFLQPFSNT LWILVMVSVH VVALVLYLLD RFSPFGRFKL
SHSDSNEEKA LNLSSAVWFA WGVLLNSGIG EGTPRSFSAR VLGMVWAGFA MIIVASYTAN
LAAFLVLERP KTKLSGINDA RLRNTMENLT CATVKGSSVD MYFRRQVELS NMYRTMESNN
YVTAEQAIQD VKKGKLMAFI WDSSRLEYEA SKDCELVTAG ELFGRSGYGI GLQKGSPWTD
AVTLAILEFH ESGFMEKLDK QWIFHGHVQQ NCELFEKTPN TLGLKNMAGV FILVGVGIAG
GVGLIIIEVI YKKHQVKKQK RLDIARHAAD KWRGTIEKRK TIRASLAMQR QYNVGLMATH
APGTISLAVD KRRYPRLGQR LGPERAWPGD GADVLRIRRP YDLGKGGLTA SQLGLGKTRP
QQNPLPPRYS PGYTSDVSHL VV
