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Protein

Glutamate [NMDA] receptor subunit 1

Gene

Nmdar1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei537 – 5371GlycineBy similarity
Binding sitei703 – 7031GlycineBy similarity
Binding sitei747 – 7471GlycineBy similarity

GO - Molecular functioni

  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • NMDA glutamate receptor activity Source: FlyBase

GO - Biological processi

  • associative learning Source: FlyBase
  • calcium ion homeostasis Source: UniProtKB
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • ionotropic glutamate receptor signaling pathway Source: UniProtKB
  • long-term memory Source: FlyBase
  • medium-term memory Source: FlyBase
  • olfactory learning Source: FlyBase
  • phototaxis Source: FlyBase
  • regulation of membrane potential Source: UniProtKB
  • sensory perception of touch Source: FlyBase
  • synaptic transmission Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Magnesium

Enzyme and pathway databases

ReactomeiR-DME-3928662. EPHB-mediated forward signaling.
R-DME-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-DME-442729. CREB phosphorylation through the activation of CaMKII.
R-DME-8849932. SALM protein interactions at the synapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate [NMDA] receptor subunit 11 Publication
Short name:
DNMDAR-I1 Publication
Short name:
dNR11 Publication
Gene namesi
Name:Nmdar1Imported
Synonyms:nmrImported, NR11 Publication
ORF Names:CG2902
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010399. Nmdar1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 573547ExtracellularSequence analysisAdd
BLAST
Transmembranei574 – 59421HelicalSequence analysisAdd
BLAST
Topological domaini595 – 65157CytoplasmicSequence analysisAdd
BLAST
Transmembranei652 – 67221HelicalSequence analysisAdd
BLAST
Topological domaini673 – 831159ExtracellularSequence analysisAdd
BLAST
Transmembranei832 – 85221HelicalSequence analysisAdd
BLAST
Topological domaini853 – 997145CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of membrane Source: FlyBase
  • ionotropic glutamate receptor complex Source: FlyBase
  • NMDA selective glutamate receptor complex Source: UniProtKB
  • postsynaptic density Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Flies exhibit disruption of olfactory learning.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 997971Glutamate [NMDA] receptor subunit 1Sequence analysisPRO_0000363996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi93 – 93InterchainBy similarity
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence analysis
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence analysis
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence analysis
Glycosylationi693 – 6931N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ24418.
PRIDEiQ24418.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

Expression first seen in late embryos. Levels are low during larval development and increase in late pupae to persist through to adulthood.1 Publication

Gene expression databases

BgeeiQ24418.
GenevisibleiQ24418. DM.

Interactioni

Subunit structurei

Forms a heteromeric NMDA channel with Nmdar2.

Protein-protein interaction databases

IntActiQ24418. 6 interactions.
STRINGi7227.FBpp0078410.

Structurei

3D structure databases

ProteinModelPortaliQ24418.
SMRiQ24418. Positions 35-857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni530 – 5323Glycine bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000184780.
InParanoidiQ24418.
KOiK05208.
OMAiPCPLFNA.
OrthoDBiEOG79GT5V.
PhylomeDBiQ24418.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q24418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMAEFVFCR PLFGLAIVLL VAPIDAAQRH TASDNPSTYN IGGVLSNSDS
60 70 80 90 100
EEHFSTTIKH LNFDQQYVPR KVTYYDKTIR MDKNPIKTVF NVCDKLIENR
110 120 130 140 150
VYAVVVSHEQ TSGDLSPAAV SYTSGFYSIP VIGISSRDAA FSDKNIHVSF
160 170 180 190 200
LRTVPPYYHQ ADVWLEMLSH FAYTKVIIIH SSDTDGRAIL GRFQTTSQTY
210 220 230 240 250
YDDVDVRATV ELIVEFEPKL ESFTEHLIDM KTAQSRVYLM YASTEDAQVI
260 270 280 290 300
FRDAGEYNMT GEGHVWIVTE QALFSNNTPD GVLGLQLEHA HSDKGHIRDS
310 320 330 340 350
VYVLASAIKE MISNETIAEA PKDCGDSAVN WESGKRLFQY LKSRNITGET
360 370 380 390 400
GQVAFDDNGD RIYAGYDVIN IREQQKKHVV GKFSYDSMRA KMRMRINDSE
410 420 430 440 450
IIWPGKQRRK PEGIMIPTHL RLLTIEEKPF VYVRRMGDDE FRCEPDERPC
460 470 480 490 500
PLFNNSDATA NEFCCRGYCI DLLIELSKRI NFTYDLALSP DGQFGHYILR
510 520 530 540 550
NNTGAMTLRK EWTGLIGELV NERADMIVAP LTINPERAEY IEFSKPFKYQ
560 570 580 590 600
GITILEKKPS RSSTLVSFLQ PFSNTLWILV MVSVHVVALV LYLLDRFSPF
610 620 630 640 650
GRFKLSHSDS NEEKALNLSS AVWFAWGVLL NSGIGEGTPR SFSARVLGMV
660 670 680 690 700
WAGFAMIIVA SYTANLAAFL VLERPKTKLS GINDARLRNT MENLTCATVK
710 720 730 740 750
GSSVDMYFRR QVELSNMYRT MEANNYATAE QAIQDVKKGK LMAFIWDSSR
760 770 780 790 800
LEYEASKDCE LVTAGELFGR SGYGIGLQKG SPWTDAVTLA ILEFHESGFM
810 820 830 840 850
EKLDKQWIFH GHVQQNCELF EKTPNTLGLK NMAGVFILVG VGIAGGVGLI
860 870 880 890 900
IIEVIYKKHQ VKKQKRLDIA RHAADKWRGT IEKRKTIRAS LAMQRQYNVG
910 920 930 940 950
LNSTHAPGTI SLAVDKRRYP RLGQRLGPER AWPGDAADVL RIRRPYELGN
960 970 980 990
PGQSPKVMAA NQPGMPMPML GKTRPQQSVL PPRYSPGYTS DVSHLVV
Length:997
Mass (Da):112,288
Last modified:November 1, 1996 - v1
Checksum:iABBD0614E2DB3731
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71790 mRNA. Translation: CAA50675.1.
AE014297 Genomic DNA. Translation: AAF52016.1.
AY070577 mRNA. Translation: AAL48048.1.
PIRiS33754.
RefSeqiNP_730940.1. NM_169059.2.
UniGeneiDm.3670.

Genome annotation databases

EnsemblMetazoaiFBtr0078763; FBpp0078410; FBgn0010399.
GeneIDi40665.
KEGGidme:Dmel_CG2902.
UCSCiCG2902-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71790 mRNA. Translation: CAA50675.1.
AE014297 Genomic DNA. Translation: AAF52016.1.
AY070577 mRNA. Translation: AAL48048.1.
PIRiS33754.
RefSeqiNP_730940.1. NM_169059.2.
UniGeneiDm.3670.

3D structure databases

ProteinModelPortaliQ24418.
SMRiQ24418. Positions 35-857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ24418. 6 interactions.
STRINGi7227.FBpp0078410.

Proteomic databases

PaxDbiQ24418.
PRIDEiQ24418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078763; FBpp0078410; FBgn0010399.
GeneIDi40665.
KEGGidme:Dmel_CG2902.
UCSCiCG2902-RA. d. melanogaster.

Organism-specific databases

CTDi40665.
FlyBaseiFBgn0010399. Nmdar1.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000184780.
InParanoidiQ24418.
KOiK05208.
OMAiPCPLFNA.
OrthoDBiEOG79GT5V.
PhylomeDBiQ24418.

Enzyme and pathway databases

ReactomeiR-DME-3928662. EPHB-mediated forward signaling.
R-DME-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-DME-442729. CREB phosphorylation through the activation of CaMKII.
R-DME-8849932. SALM protein interactions at the synapse.

Miscellaneous databases

GenomeRNAii40665.
PROiQ24418.

Gene expression databases

BgeeiQ24418.
GenevisibleiQ24418. DM.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glutamate receptors of Drosophila melanogaster. Primary structure of a putative NMDA receptor protein expressed in the head of the adult fly."
    Ultsch A., Schuster C.M., Laube B., Betz H., Schmitt B.
    FEBS Lett. 324:171-177(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: BerlinImported and Canton-SImported.
    Tissue: HeadImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  3. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    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.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Embryo1 Publication.
  6. "NMDA receptors mediate olfactory learning and memory in Drosophila."
    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.
    Curr. Biol. 15:603-615(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NMDAR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  7. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-693, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head1 Publication.

Entry informationi

Entry nameiNMDA1_DROME
AccessioniPrimary (citable) accession number: Q24418
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.