NMDA1_DROVI
ID NMDA1_DROVI Reviewed; 984 AA.
AC B4LZB5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000250|UniProtKB:Q24418};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000250|UniProtKB:Q24418}; ORFNames=GJ24560;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW68150.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW68150.1};
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; CH940650; EDW68150.1; -; Genomic_DNA.
DR RefSeq; XP_002054630.1; XM_002054594.2.
DR RefSeq; XP_015027744.1; XM_015172258.1.
DR AlphaFoldDB; B4LZB5; -.
DR SMR; B4LZB5; -.
DR STRING; 7244.FBpp0238977; -.
DR EnsemblMetazoa; FBtr0240485; FBpp0238977; FBgn0211640.
DR EnsemblMetazoa; FBtr0444757; FBpp0401071; FBgn0211640.
DR GeneID; 6630672; -.
DR KEGG; dvi:6630672; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; B4LZB5; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; B4LZB5; -.
DR Proteomes; UP000008792; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..984
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000364002"
FT TOPO_DOM 25..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 947..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527..529
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 534
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 700
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 744
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 984 AA; 110817 MW; 5020A2101FCE7995 CRC64;
MAAAFAYRWL LCAAGIVNVL PIGAQRHTAS DNPSTYNIGG VLSNSESELH FHTTIAHLNF
DQQYVPRKVT YYDKTIRMDK NPIKTVFNVC DKLIEKRVYA VVVSHEQTSG DLSPAAVSYT
SGFYSIPVIG ISSRDAAFSD KNIHVSFLRT VPPYYHQADV WLELLSHFLY TKVIIIHSSD
TDGRAILGRF QTTSQTYYDD VDVRATVELI VEFEPKLESF TEHLIDMKTA QSRVYLMYAS
TEDAQVIFRD AGEYNMTGEG HVWIVTEQAL HANNTPDGVL GLQLEHAHSD KGHIRDSVYV
LASAIKEMIS NETIAEAPKD CGDSAVNWES GKRLFQYLKS RNITGETGQV AFDDNGDRIY
AGYDVINIRE HQKQHLVGKF SYDSLRAKMR MRINDSEIIW GGKQKRKPEG IMIPTHLKVL
TIEEKPFVYV RRMGDDEFRC EPDERPCPLF NASDATTNEF CCRGYCIDLL IELSKRINFT
YDLALSPDGQ FGHYILRNNT GAMTLRKEWT GLIGELVNER ADMIVAPLTI NPERAEYIEF
SKPFKYQGIT ILEKKPSRSS TLVSFLQPFS NTLWILVMVS VHVVALVLYL LDRFSPFGRF
KLSHSDSNEE KALNLSSAVW FAWGVLLNSG IGEGTPRSFS ARVLGMVWAG FAMIIVASYT
ANLAAFLVLE RPKTKLSGIN DARLRNTMEN LTCATVKGSS VDMYFRRQVE LSNMYRTMES
NNYVTAEQAI QDVKKGKLMA FIWDSSRLEY EASKDCELVT AGELFGRSGY GVGLQKGSPW
TDAVTLTILE FHESGFMEKL DKQWIFHGHV QQNCELFEKT PNTLGLKNMA GVFILVGVGI
AGGVGLIIIE VIYKKHQVKK QKRLDIARHA ADKWRGTIEK RKTIRASLAM QRQYNVGLMA
RQPPGTISLA VDKRRYPRLG QRLGPERAWP GDAADVLRTR RPYDLTKSGL VPPALGLGKT
RPQQNPLPPR YSPGYTSDVS HLVV
