NMDA1_DROME
ID NMDA1_DROME Reviewed; 997 AA.
AC Q24418;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000303|PubMed:15823532};
DE Short=DNMDAR-I {ECO:0000303|PubMed:8508917};
DE Short=dNR1 {ECO:0000303|PubMed:15823532};
DE Flags: Precursor;
GN Name=Nmdar1 {ECO:0000312|EMBL:AAF52016.1, ECO:0000312|FlyBase:FBgn0010399};
GN Synonyms=nmr {ECO:0000312|EMBL:CAA50675.1},
GN NR1 {ECO:0000303|PubMed:15823532}; ORFNames=CG2902;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA50675.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Berlin {ECO:0000312|EMBL:CAA50675.1}, and
RC Canton-S {ECO:0000312|EMBL:CAA50675.1};
RC TISSUE=Head {ECO:0000312|EMBL:CAA50675.1};
RX PubMed=8508917; DOI=10.1016/0014-5793(93)81387-f;
RA Ultsch A., Schuster C.M., Laube B., Betz H., Schmitt B.;
RT "Glutamate receptors of Drosophila melanogaster. Primary structure of a
RT putative NMDA receptor protein expressed in the head of the adult fly.";
RL FEBS Lett. 324:171-177(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11773617; DOI=10.1073/pnas.012318899;
RA Chiang A.-S., Lin W.-Y., Liu H.-P., Pszczolkowski M.A., Fu T.-F.,
RA Chiu S.-L., Holbrook G.L.;
RT "Insect NMDA receptors mediate juvenile hormone biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:37-42(2002).
RN [3] {ECO:0000312|EMBL:AAF52016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF52016.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:AAL48048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48048.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH NMDAR2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15823532; DOI=10.1016/j.cub.2005.02.059;
RA Xia S., Miyashita T., Fu T.-F., Lin W.-Y., Wu C.-L., Pyzocha L., Lin I.-R.,
RA Saitoe M., Tully T., Chiang A.-S.;
RT "NMDA receptors mediate olfactory learning and memory in Drosophila.";
RL Curr. Biol. 15:603-615(2005).
RN [7] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-693, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head {ECO:0000269|PubMed:17893096};
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(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. {ECO:0000250|UniProtKB:P35439,
CC ECO:0000269|PubMed:15823532}.
CC -!- SUBUNIT: Forms a heteromeric NMDA channel with Nmdar2.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15823532};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15823532}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:15823532}. Postsynaptic density
CC {ECO:0000269|PubMed:15823532}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult heads: in the brain and
CC ring gland. Low expression throughout the entire brain is also seen.
CC Higher expression levels were observed in some scattered cell bodies
CC and part of their fibers, including those from several pairs of DPM
CC (dorsal-posterior-medial) neurons surrounding the calyx, DAL (dorsal-
CC anterior-lateral) and DPL (dorsal-posterior-lateral) neurons in the
CC lateral protocerebrum (LP), VAL (ventral-anterior-lateral) neurons in
CC the anterior protocerebrum, and two pairs of VP (ventral-posterior)
CC neurons in the posterior protocerebrum. Many cell bodies in the optic
CC lobes show preferential expression. Punctuate expression is notably
CC detected in many brain regions including the superior medial
CC protocerebrum. Weakly expressed in the antennal lobes and central
CC complex. {ECO:0000269|PubMed:11773617, ECO:0000269|PubMed:15823532,
CC ECO:0000269|PubMed:8508917}.
CC -!- DEVELOPMENTAL STAGE: Expression first seen in late embryos. Levels are
CC low during larval development and increase in late pupae to persist
CC through to adulthood. {ECO:0000269|PubMed:8508917}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit disruption of olfactory learning.
CC {ECO:0000269|PubMed:15823532}.
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; X71790; CAA50675.1; -; mRNA.
DR EMBL; AE014297; AAF52016.1; -; Genomic_DNA.
DR EMBL; AY070577; AAL48048.1; -; mRNA.
DR PIR; S33754; S33754.
DR RefSeq; NP_730940.1; NM_169059.2.
DR AlphaFoldDB; Q24418; -.
DR SMR; Q24418; -.
DR BioGRID; 65872; 5.
DR IntAct; Q24418; 6.
DR STRING; 7227.FBpp0078410; -.
DR TCDB; 1.A.10.1.25; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q24418; 8 sites.
DR iPTMnet; Q24418; -.
DR PaxDb; Q24418; -.
DR PRIDE; Q24418; -.
DR EnsemblMetazoa; FBtr0078763; FBpp0078410; FBgn0010399.
DR GeneID; 40665; -.
DR KEGG; dme:Dmel_CG2902; -.
DR UCSC; CG2902-RA; d. melanogaster.
DR CTD; 40665; -.
DR FlyBase; FBgn0010399; Nmdar1.
DR VEuPathDB; VectorBase:FBgn0010399; -.
DR eggNOG; KOG4440; Eukaryota.
DR GeneTree; ENSGT00940000158016; -.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; Q24418; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q24418; -.
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-DME-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-DME-9609736; Assembly and cell surface presentation of NMDA receptors.
DR BioGRID-ORCS; 40665; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40665; -.
DR PRO; PR:Q24418; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010399; Expressed in brain and 9 other tissues.
DR Genevisible; Q24418; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IPI:FlyBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; ISS:FlyBase.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IDA:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0042331; P:phototaxis; IDA:FlyBase.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
DR GO; GO:0050975; P:sensory perception of touch; IMP:FlyBase.
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 1: Evidence at protein level;
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..997
FT /note="Glutamate [NMDA] receptor subunit 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000363996"
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 970..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:0000269|PubMed:17893096"
FT DISULFID 93
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
SQ SEQUENCE 997 AA; 112288 MW; ABBD0614E2DB3731 CRC64;
MAMAEFVFCR PLFGLAIVLL VAPIDAAQRH 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
RLLTIEEKPF VYVRRMGDDE FRCEPDERPC PLFNNSDATA NEFCCRGYCI DLLIELSKRI
NFTYDLALSP DGQFGHYILR NNTGAMTLRK 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 RIRRPYELGN PGQSPKVMAA
NQPGMPMPML GKTRPQQSVL PPRYSPGYTS DVSHLVV
