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NMDA1_DROER
ID   NMDA1_DROER             Reviewed;         997 AA.
AC   B3P2E5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GG10981;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000312|EMBL:EDV47895.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV47895.1};
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; CH954181; EDV47895.1; -; Genomic_DNA.
DR   RefSeq; XP_001978937.1; XM_001978901.2.
DR   RefSeq; XP_015009472.1; XM_015153986.1.
DR   AlphaFoldDB; B3P2E5; -.
DR   SMR; B3P2E5; -.
DR   STRING; 7220.FBpp0129527; -.
DR   EnsemblMetazoa; FBtr0131035; FBpp0129527; FBgn0103284.
DR   EnsemblMetazoa; FBtr0412075; FBpp0370432; FBgn0103284.
DR   GeneID; 6552207; -.
DR   KEGG; der:6552207; -.
DR   eggNOG; KOG4440; Eukaryota.
DR   HOGENOM; CLU_007257_2_0_1; -.
DR   OMA; KPEGFMI; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; B3P2E5; -.
DR   Proteomes; UP000008711; 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; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..997
FT                   /note="Glutamate [NMDA] receptor subunit 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000363994"
FT   TOPO_DOM        27..573
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        595..651
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        652..672
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        673..831
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        832..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        853..997
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          947..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         530..532
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250|UniProtKB:P35439"
FT   BINDING         537
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250|UniProtKB:P35439"
FT   BINDING         703
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250|UniProtKB:P35439"
FT   BINDING         747
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250|UniProtKB:P35439"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q05586"
SQ   SEQUENCE   997 AA;  112356 MW;  A6B51B80AE77D4CD CRC64;
     MAVAEFVFCW PLFELAIVLL VAPIHAAQRH TASDNPSTYN IGGVLSNSDS EEHFSTTIKH
     LNFDQQYVPR KVTYYDKTIR MDKNPIKTVF NVCDKLIENR VYAVVVSHEQ TSGDLSPAAV
     SYTSGFYSIP VIGISSRDAA FSDKNIHVSF LRTVPPYYHQ ADVWLEMLSH FAYTKVIIIH
     SSDTDGRAIL GRFQTTSQTY YDDVDVRATV ELIVEFEPKL ESFTEHLIDM KTAQSRVYLM
     YASTEDAQVI FRDAGEYNMT GEGHVWIVTE QALFSNNTPD GVLGLQLEHA HSDKGHIRDS
     VYVLASAIKE MISNETIAEA PKDCGDSAVN WESGKRLFQY LKSRNITGET GQVAFDDNGD
     RIYAGYDVIN IREQQKKHVV GKFSYDSMRA KMRMRINDSE IIWPGKQRRK PEGIMIPTHL
     KLLTIEEKPF VYVRRMGDDE FRCEPDERPC PLFNNSDATA NEFCCRGYCI DLLIELSKRI
     NFTYDLALSP DGQFGHYILR NSTGAMTLRK EWTGLIGELV NERADMIVAP LTINPERAEY
     IEFSKPFKYQ GITILEKKPS RSSTLVSFLQ PFSNTLWILV MVSVHVVALV LYLLDRFSPF
     GRFKLSHSDS NEEKALNLSS AVWFAWGVLL NSGIGEGTPR SFSARVLGMV WAGFAMIIVA
     SYTANLAAFL VLERPKTKLS GINDARLRNT MENLTCATVK GSSVDMYFRR QVELSNMYRT
     MEANNYATAE QAIQDVKKGK LMAFIWDSSR LEYEASKDCE LVTAGELFGR SGYGIGLQKG
     SPWTDAVTLA ILEFHESGFM EKLDKQWIFH GHVQQNCELF EKTPNTLGLK NMAGVFILVG
     VGIAGGVGLI IIEVIYKKHQ VKKQKRLDIA RHAADKWRGT IEKRKTIRAS LAMQRQYNVG
     LNSTHAPGTI SLAVDKRRYP RLGQRLGPER AWPGDAADVL RIRRPYELGK PGQSPKVMSA
     NQPGMPMPML GKTRPQQSVL PPRYSPGYTS DVSHLVV
 
 
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