NMDA1_DROPS
ID NMDA1_DROPS Reviewed; 1004 AA.
AC Q296F7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000250|UniProtKB:Q24418};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000250|UniProtKB:Q24418}; ORFNames=GA15505;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL28500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CM000070; EAL28500.1; -; Genomic_DNA.
DR RefSeq; XP_001359355.1; XM_001359318.2.
DR AlphaFoldDB; Q296F7; -.
DR SMR; Q296F7; -.
DR STRING; 7237.FBpp0284416; -.
DR EnsemblMetazoa; FBtr0285978; FBpp0284416; FBgn0075522.
DR GeneID; 4802433; -.
DR KEGG; dpo:Dpse_GA15505; -.
DR eggNOG; KOG4440; Eukaryota.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; Q296F7; -.
DR OMA; KPEGFMI; -.
DR PhylomeDB; Q296F7; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0075522; Expressed in insect adult head.
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..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1004
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000363999"
FT TOPO_DOM 40..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..843
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 980..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542..544
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 549
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 715
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 759
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 1004 AA; 112855 MW; C07DDC5E120A0497 CRC64;
MAGTDSPAAA RFVYRCLLFA PAIVVGLLLP LTLPPIAAAQ RHTASDNPST YNIGGVLSNS
ESETYFHTII SHLNFDQQYV PRKVTYYDKT IRMDKNPIKT VFNVCDKLIE NRVYAVVVSH
EQTSGDLSPA AVSYTSGFYS IPVIGISSRD AAFSDKNIHV SFLRTVPPYY HQADVWLEML
SHFAYTKVII IHSSDTDGRA ILGRFQTTSQ TYYDDVDVRA TVELIVEFEP KLESFTEHLI
DMKTAQSRVY LMYASTEDAQ VIFRDAGEYN MTGEGHVWIV TEQALFANNT PDGVLGLQLE
HAHSDKGHIR DSVYVLASAI KEMISNETIA EAPKDCGDSA VNWESGKRLF QYLKSRNITG
ETGQVAFDDN GDRIYAGYDV INIREHQKKH VVGKFSYDSM RAKMRMNIND SEIIWPGKQN
RKPEGIMIPT HLKVLTIEEK PFVYVRRMGD DEFRCEPDER PCPLFNATDS TANEYCCRGY
CIDLLIELSK RINFTYDLAL SPDGQFGHYL LRNNTGAMTL RKEWTGLMGE LVNERADMIV
APLTINPERA EYIEFSKPFK YQGITILEKK PSRSSTLVSF LQPFSNTLWI LVMVSVHVVA
LVLYLLDRFS PFGRFKLSHS DSNEEKALNL SSAVWFAWGV LLNSGIGEGT PRSFSARVLG
MVWAGFAMII VASYTANLAA FLVLERPKTK LSGINDARLR NTMENLTCAT VKGSSVDMYF
RRQVELSNMY RTMEANNYAT AEQAIQDVKK GKLMAFIWDS SRLEYEASKD CELVTAGELF
GRSGYGVGLQ KGSPWTDSVT LAILEFHESG FMEKLDKQWI FHGHVQQNCE LFEKTPNTLG
LKNMAGVFIL VGVGIAGGVG LIIIEVIYKK HQVKKQKRLD IARHAADKWR GTIEKRKTIR
ASLAMQRQYN VGLNSTHPPG TISLAVDKRR YPRLGQRLGP ERAWPGDAAD VLRTRRPYEL
GKPGQSPKVM VATPAMLGRT RPQQNILPPR YSPGYTSDVS HLVV
