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Glutamate [NMDA] receptor subunit 1 (DNMDAR-I) (dNR1)

 NMDA1_DROME             Reviewed;         997 AA.
Q24418;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 143.
RecName: Full=Glutamate [NMDA] receptor subunit 1 {ECO:0000303|PubMed:15823532};
Short=DNMDAR-I {ECO:0000303|PubMed:8508917};
Short=dNR1 {ECO:0000303|PubMed:15823532};
Flags: Precursor;
Name=Nmdar1 {ECO:0000312|EMBL:AAF52016.1,
ECO:0000312|FlyBase:FBgn0010399};
Synonyms=nmr {ECO:0000312|EMBL:CAA50675.1},
NR1 {ECO:0000303|PubMed:15823532}; ORFNames=CG2902;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:CAA50675.1}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=Berlin {ECO:0000312|EMBL:CAA50675.1}, and
Canton-S {ECO:0000312|EMBL:CAA50675.1};
TISSUE=Head {ECO:0000312|EMBL:CAA50675.1};
PubMed=8508917; DOI=10.1016/0014-5793(93)81387-F;
Ultsch A., Schuster C.M., Laube B., Betz H., Schmitt B.;
"Glutamate receptors of Drosophila melanogaster. Primary structure of
a putative NMDA receptor protein expressed in the head of the adult
fly.";
FEBS Lett. 324:171-177(1993).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=11773617; DOI=10.1073/pnas.012318899;
Chiang A.-S., Lin W.-Y., Liu H.-P., Pszczolkowski M.A., Fu T.-F.,
Chiu S.-L., Holbrook G.L.;
"Insect NMDA receptors mediate juvenile hormone biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:37-42(2002).
[3] {ECO:0000312|EMBL:AAF52016.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF52016.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000312|EMBL:AAL48048.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAL48048.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6] {ECO:0000305}
FUNCTION, INTERACTION WITH NMDAR2, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15823532; DOI=10.1016/j.cub.2005.02.059;
Xia S., Miyashita T., Fu T.-F., Lin W.-Y., Wu C.-L., Pyzocha L.,
Lin I.-R., Saitoe M., Tully T., Chiang A.-S.;
"NMDA receptors mediate olfactory learning and memory in Drosophila.";
Curr. Biol. 15:603-615(2005).
[7] {ECO:0000305}
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-693, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head {ECO:0000269|PubMed:17893096};
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
-!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
with high calcium permeability and voltage-dependent sensitivity
to magnesium. Mediated by glycine. This protein plays a key role
in synaptic plasticity, synaptogenesis, excitotoxicity, memory
acquisition and learning. It mediates neuronal functions in
glutamate neurotransmission. Is involved in the cell surface
targeting of NMDA receptors. Plays a role in associative learning
and in long-term memory consolidation.
{ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:15823532}.
-!- SUBUNIT: Forms a heteromeric NMDA channel with Nmdar2.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15823532};
Multi-pass membrane protein {ECO:0000269|PubMed:15823532}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:15823532}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:15823532}.
-!- TISSUE SPECIFICITY: Highly expressed in adult heads: in the brain
and ring gland. Low expression throughout the entire brain is also
seen. Higher expression levels were observed in some scattered
cell bodies and part of their fibers, including those from several
pairs of DPM (dorsal-posterior-medial) neurons surrounding the
calyx, DAL (dorsal-anterior-lateral) and DPL (dorsal-posterior-
lateral) neurons in the lateral protocerebrum (LP), VAL (ventral-
anterior-lateral) neurons in the anterior protocerebrum, and two
pairs of VP (ventral-posterior) neurons in the posterior
protocerebrum. Many cell bodies in the optic lobes show
preferential expression. Punctuate expression is notably detected
in many brain regions including the superior medial protocerebrum.
Weakly expressed in the antennal lobes and central complex.
{ECO:0000269|PubMed:11773617, ECO:0000269|PubMed:15823532,
ECO:0000269|PubMed:8508917}.
-!- DEVELOPMENTAL STAGE: Expression first seen in late embryos. Levels
are low during larval development and increase in late pupae to
persist through to adulthood. {ECO:0000269|PubMed:8508917}.
-!- DISRUPTION PHENOTYPE: Flies exhibit disruption of olfactory
learning. {ECO:0000269|PubMed:15823532}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X71790; CAA50675.1; -; mRNA.
EMBL; AE014297; AAF52016.1; -; Genomic_DNA.
EMBL; AY070577; AAL48048.1; -; mRNA.
PIR; S33754; S33754.
RefSeq; NP_730940.1; NM_169059.2.
UniGene; Dm.3670; -.
ProteinModelPortal; Q24418; -.
BioGrid; 65872; 4.
IntAct; Q24418; 6.
STRING; 7227.FBpp0078410; -.
iPTMnet; Q24418; -.
PaxDb; Q24418; -.
PRIDE; Q24418; -.
EnsemblMetazoa; FBtr0078763; FBpp0078410; FBgn0010399.
GeneID; 40665; -.
KEGG; dme:Dmel_CG2902; -.
UCSC; CG2902-RA; d. melanogaster.
CTD; 40665; -.
FlyBase; FBgn0010399; Nmdar1.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00910000143978; -.
HOGENOM; HOG000184780; -.
InParanoid; Q24418; -.
KO; K05208; -.
OMA; SGFYHIP; -.
OrthoDB; EOG091G0M5H; -.
PhylomeDB; Q24418; -.
Reactome; R-DME-3928662; EPHB-mediated forward signaling.
Reactome; R-DME-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-DME-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-DME-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-DME-5673001; RAF/MAP kinase cascade.
Reactome; R-DME-8849932; Synaptic adhesion-like molecules.
GenomeRNAi; 40665; -.
PRO; PR:Q24418; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0010399; -.
Genevisible; Q24418; DM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
GO; GO:0008328; C:ionotropic glutamate receptor complex; IPI:FlyBase.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0004972; F:NMDA glutamate receptor activity; ISS:FlyBase.
GO; GO:0008306; P:associative learning; IDA:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
GO; GO:0042331; P:phototaxis; IDA:FlyBase.
GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
GO; GO:0050975; P:sensory perception of touch; IMP:FlyBase.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 2.
Pfam; PF10562; CaM_bdg_C0; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
Calcium; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Magnesium; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 997 Glutamate [NMDA] receptor subunit 1.
{ECO:0000255}.
/FTId=PRO_0000363996.
TOPO_DOM 27 573 Extracellular. {ECO:0000255}.
TRANSMEM 574 594 Helical. {ECO:0000255}.
TOPO_DOM 595 651 Cytoplasmic. {ECO:0000255}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TOPO_DOM 673 831 Extracellular. {ECO:0000255}.
TRANSMEM 832 852 Helical. {ECO:0000255}.
TOPO_DOM 853 997 Cytoplasmic. {ECO:0000255}.
REGION 530 532 Glycine binding.
{ECO:0000250|UniProtKB:P35439}.
BINDING 537 537 Glycine. {ECO:0000250|UniProtKB:P35439}.
BINDING 703 703 Glycine. {ECO:0000250|UniProtKB:P35439}.
BINDING 747 747 Glycine. {ECO:0000250|UniProtKB:P35439}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 693 693 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
DISULFID 93 93 Interchain.
{ECO:0000250|UniProtKB:Q05586}.
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


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