NMDA1_DROWI
ID NMDA1_DROWI Reviewed; 982 AA.
AC B4MU83;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000250|UniProtKB:Q24418};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000250|UniProtKB:Q24418}; ORFNames=GK23704;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW75672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW75672.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH963852; EDW75672.1; -; Genomic_DNA.
DR RefSeq; XP_002064686.1; XM_002064650.2.
DR AlphaFoldDB; B4MU83; -.
DR SMR; B4MU83; -.
DR STRING; 7260.FBpp0252847; -.
DR EnsemblMetazoa; FBtr0254355; FBpp0252847; FBgn0225666.
DR GeneID; 6641663; -.
DR KEGG; dwi:6641663; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; B4MU83; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; B4MU83; -.
DR Proteomes; UP000007798; 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: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:0008355; P:olfactory learning; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..982
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000364003"
FT TOPO_DOM 17..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 661..819
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 934..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518..520
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 525
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 691
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 735
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 982 AA; 110944 MW; FD990E343E969F63 CRC64;
MAFAVWFLST FVIVAAQRHM ALEHEGTYNI GGVLTNSDSE EHFRTTIAHL NFDQQYVPRK
VTYYEKTIRM DKNPIKTVFN VCNKLIEKRV YAVVVSHEQT SGDLSPAAVS YTSGFYSIPV
IGISSRDAAF SDKNIHVSFL RTVPPYYHQA DVWLEMLSHF SYTKVIIIHS SDTDGRAILG
RFQTTSQTYY DDVDVRATVE MIVEFEPKLT SFSEHLTYMK TAQSRVYLMY ASTEDAQIIF
RDARDHNMTQ EGHVWIVTEQ ALFANNTPEG VLGLQLEHAH SDKGHIRDSV YVLASAIKEM
ISNETIAEAP KDCGDSAVNW ESGKRLFQYL KTRNITGETG QVAFDDNGDR IYAGYDVINI
RENQKQHVVG KFSYDNMRAK MRMKINDSEI IWAGKQKRKP EGIMIPTHLK LLTIEEKPFV
YVRRMGDDEF HCEPNERPCP LFNTTDATAN EFCCSGYCID LLIELAKRIN FTYDLALSPD
GQFGHYILRN NTGATLRKEW TGLIGQLVNE RADMIVAPLT INPERAEYIE FSKPFKYQGI
TILEKKPSRS STLVSFLQPF SNTLWILVMV SVHVVALVLY LLDRFSPFGR FKLSHSDSNE
EKALNLSSAV WFAWGVLLNS GIGEGTPRSF SARVLGMVWA GFAMIIVASY TANLAAFLVL
ERPKTKLSGI NDARLRNTME NLTCATVKGS SVDMYFRRQV ELSNMYRTME ANNYATAEHA
IQDVKKGKLM AFIWDSSRLE YEASKDCELV TAGELFGRSG YGIGLQKGSP WTDAVTLAIL
EFHESGFMEK LDKQWIFHGH VQQNCELFEK TPNTLGLKNM AGVFILVGVG IAGGVGLIII
EVIYKKHQVK KQKRLDIARH AADKWRGTIE KRKTIRASLA MQRQYNVGLN SRAPGTISLA
VDKKRYPRLS QRMGPERAWP GDAAEVLRMR RPYEIGKPGQ SPKVIGGPPH PMLGKTRPQA
QQNLLPPRYS PGYTSDVSHL VV
