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P35438 (NMDZ1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, NMDA 1

Short name=GluN1
Alternative name(s):
Glutamate [NMDA] receptor subunit zeta-1
N-methyl-D-aspartate receptor subunit NR1
Short name=NMD-R1
Gene names
Name:Grin1
Synonyms:Glurz1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Modulated 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 By similarity.

Subunit structure

Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B); disulfide-linked. Found in a complex with GRIN2A or GRIN2B and GRIN3B. Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB. Interacts with DLG4 and MPDZ By similarity. Interacts with LRFN1 and LRFN2 By similarity. Interacts with MYZAP. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Note: Enriched in postsynaptic plasma membrane and postsynaptic densities By similarity. Ref.5

Post-translational modification

NMDA is probably regulated by C-terminal phosphorylation of an isoform ofNR1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity By similarity.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 10481908PubMed 10818139. Source: MGI

associative learning

Inferred from mutant phenotype PubMed 12040087PubMed 12718863PubMed 21813695. Source: MGI

calcium ion homeostasis

Inferred from direct assay PubMed 7907365. Source: MGI

calcium ion transmembrane transport

Inferred from direct assay PubMed 1374164Ref.1. Source: GOC

calcium ion transport

Inferred from direct assay Ref.1. Source: MGI

cation transport

Inferred from genetic interaction PubMed 7531804. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 8060614. Source: MGI

cellular response to manganese ion

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from mutant phenotype PubMed 10963597PubMed 12657691. Source: MGI

conditioned taste aversion

Inferred from mutant phenotype PubMed 16101757. Source: MGI

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay PubMed 16025111. Source: MGI

learning

Inferred from mutant phenotype PubMed 17015831. Source: MGI

learning or memory

Inferred from mutant phenotype PubMed 17004940. Source: MGI

long-term memory

Inferred from mutant phenotype PubMed 15003177. Source: MGI

male mating behavior

Inferred from mutant phenotype PubMed 10481908. Source: MGI

memory

Inferred from mutant phenotype PubMed 10700255PubMed 10719900PubMed 17556551. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17077143. Source: MGI

neuromuscular process

Inferred from mutant phenotype PubMed 8313466. Source: MGI

olfactory learning

Inferred from mutant phenotype PubMed 10700255PubMed 11248114. Source: MGI

pons maturation

Inferred from mutant phenotype PubMed 8313466. Source: MGI

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 17803966. Source: MGI

positive regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7907365. Source: MGI

prepulse inhibition

Inferred from mutant phenotype PubMed 15265649. Source: MGI

propylene metabolic process

Inferred from direct assay PubMed 21795692. Source: BHF-UCL

protein tetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of axonogenesis

Inferred from mutant phenotype PubMed 15745956. Source: MGI

regulation of cell communication

Inferred from mutant phenotype PubMed 16299502. Source: MGI

regulation of dendrite morphogenesis

Inferred from mutant phenotype PubMed 15745956. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 15003177. Source: MGI

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 10818139PubMed 17015831PubMed 17313573. Source: MGI

regulation of membrane potential

Inferred from direct assay Ref.1. Source: MGI

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 16906136. Source: MGI

regulation of neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 15576450. Source: MGI

regulation of respiratory gaseous exchange

Inferred from mutant phenotype PubMed 10777815. Source: MGI

regulation of synapse assembly

Inferred from mutant phenotype PubMed 12657691. Source: MGI

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 15003177PubMed 8980238PubMed 8980239PubMed 9246451. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype PubMed 8313466PubMed 8713451. Source: MGI

response to amphetamine

Inferred from mutant phenotype PubMed 15467708PubMed 16638606. Source: MGI

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to fungicide

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from mutant phenotype PubMed 18423864. Source: MGI

rhythmic process

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from mutant phenotype PubMed 12832526. Source: MGI

social behavior

Inferred from mutant phenotype PubMed 10481908. Source: MGI

startle response

Inferred from mutant phenotype PubMed 10818139. Source: MGI

suckling behavior

Inferred from mutant phenotype PubMed 10777815PubMed 8313466PubMed 8713451. Source: MGI

synaptic transmission

Traceable author statement PubMed 10846156. Source: MGI

synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 10963597PubMed 8313466. Source: MGI

visual learning

Inferred from mutant phenotype PubMed 10818139PubMed 16611824PubMed 17313573PubMed 8980238PubMed 9246451. Source: MGI

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from physical interaction PubMed 9003035. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 12414093. Source: MGI

dendrite

Inferred from direct assay PubMed 23395379. Source: MGI

dendrite membrane

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from direct assay PubMed 15663482. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 16814779. Source: MGI

excitatory synapse

Inferred from electronic annotation. Source: Ensembl

growth cone

Non-traceable author statement PubMed 10480904. Source: UniProtKB

membrane

Inferred from direct assay PubMed 10846156PubMed 17093100PubMed 8840015PubMed 9003035. Source: MGI

neuronal postsynaptic density

Inferred from direct assay PubMed 24069373. Source: MGI

postsynaptic density

Inferred from direct assay PubMed 15317856PubMed 15748150. Source: MGI

postsynaptic membrane

Inferred from direct assay PubMed 11754836PubMed 12890763PubMed 15317856. Source: MGI

synapse

Inferred from direct assay PubMed 14645471PubMed 16025111PubMed 16710293PubMed 21734292. Source: MGI

synaptic cleft

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Inferred from direct assay PubMed 10846156. Source: MGI

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay PubMed 1374164PubMed 1377365PubMed 1385220Ref.1. Source: MGI

calcium channel activity

Inferred from direct assay PubMed 1374164Ref.1. Source: MGI

calcium ion binding

Inferred from direct assay PubMed 15663482. Source: MGI

calmodulin binding

Inferred from direct assay PubMed 15663482. Source: MGI

cation channel activity

Inferred from genetic interaction PubMed 7531804. Source: MGI

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glutamate binding

Inferred from electronic annotation. Source: Ensembl

glycine binding

Inferred from mutant phenotype PubMed 12586454. Source: UniProtKB

neurotransmitter binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10862698PubMed 16332682PubMed 16601687PubMed 16635246PubMed 19455133. Source: IntAct

receptor binding

Inferred from physical interaction PubMed 11754835. Source: MGI

voltage-gated cation channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q6210810EBI-400084,EBI-300895
Lrp8Q924X64EBI-400084,EBI-432319

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35438-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35438-2)

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 938920Glutamate receptor ionotropic, NMDA 1
PRO_0000011588

Regions

Topological domain19 – 559541Extracellular Potential
Transmembrane560 – 58021Helical; Potential
Topological domain581 – 63656Cytoplasmic Potential
Transmembrane637 – 65721Helical; Potential
Topological domain658 – 812155Extracellular Potential
Transmembrane813 – 83321Helical; Potential
Topological domain834 – 938105Cytoplasmic Potential
Region516 – 5183Glycine binding By similarity

Sites

Binding site5231Glycine By similarity
Binding site6881Glycine By similarity
Binding site7321Glycine By similarity

Amino acid modifications

Modified residue8891Phosphoserine; by PKC By similarity
Modified residue8901Phosphoserine By similarity
Modified residue8961Phosphoserine; by PKC By similarity
Modified residue8971Phosphoserine; by PKC By similarity
Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Disulfide bond79Interchain By similarity

Natural variations

Alternative sequence864 – 88522DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform 2.
VSP_014222
Alternative sequence886 – 93853Missing in isoform 2.
VSP_014223
Natural variant9361R → T.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C610632DD3E06171

FASTA938105,481
        10         20         30         40         50         60 
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL 

        70         80         90        100        110        120 
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG 

       130        140        150        160        170        180 
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL 

       190        200        210        220        230        240 
ETLLEERESK AEKVLQFDPG TKNVTALLME ARDLEARVII LSASEDDAAT VYRAAAMLNM 

       250        260        270        280        290        300 
TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN 

       310        320        330        340        350        360 
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK 

       370        380        390        400        410        420 
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC 

       430        440        450        460        470        480 
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCV DLLIKLARTM NFTYEVHLVA 

       490        500        510        520        530        540 
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI 

       550        560        570        580        590        600 
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA 

       610        620        630        640        650        660 
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP 

       670        680        690        700        710        720 
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA 

       730        740        750        760        770        780 
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH 

       790        800        810        820        830        840 
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH 

       850        860        870        880        890        900 
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT 

       910        920        930 
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES 

« Hide

Isoform 2 [UniParc].

Checksum: 283AA14096E81558
Show »

FASTA88599,423

References

« Hide 'large scale' references
[1]"Cloning, expression and modulation of a mouse NMDA receptor subunit."
Yamazaki M., Mori H., Araki K., Mori K.J., Mishina M.
FEBS Lett. 300:39-45(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Eye.
[4]"Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability."
Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.
Brain Res. Mol. Brain Res. 100:43-52(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3B.
[5]"Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors."
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.
J. Neurosci. 23:10064-10073(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3B.
[6]"GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and reduces N-methyl D-aspartate toxicity."
Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R., Yang J.
NeuroReport 19:1721-1726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYZAP.
[7]"Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome."
Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S., Cai L., Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G., Mobley W.C., Zhang D., Gage F.H., Ranscht B. expand/collapse author list , Zhang Y.W., Lipton S.A., Hong W., Xu H.
Nat. Med. 19:473-480(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10028 mRNA. Translation: BAA00920.1.
AL732309 Genomic DNA. Translation: CAM14685.1.
AL732309 Genomic DNA. Translation: CAM14688.1.
BC039157 mRNA. Translation: AAH39157.1.
CCDSCCDS15764.1. [P35438-1]
CCDS50528.1. [P35438-2]
PIRS21104.
RefSeqNP_001171127.1. NM_001177656.2.
NP_001171128.1. NM_001177657.2. [P35438-2]
NP_032195.1. NM_008169.3. [P35438-1]
UniGeneMm.278672.

3D structure databases

ProteinModelPortalP35438.
SMRP35438. Positions 24-838.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200067. 82 interactions.
DIPDIP-31577N.
IntActP35438. 124 interactions.
MINTMINT-135802.

Chemistry

BindingDBP35438.
GuidetoPHARMACOLOGY455.

PTM databases

PhosphoSiteP35438.

Proteomic databases

MaxQBP35438.
PaxDbP35438.
PRIDEP35438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028335; ENSMUSP00000028335; ENSMUSG00000026959. [P35438-1]
ENSMUST00000114312; ENSMUSP00000109951; ENSMUSG00000026959. [P35438-2]
GeneID14810.
KEGGmmu:14810.
UCSCuc008iri.2. mouse. [P35438-2]
uc008irk.2. mouse. [P35438-1]

Organism-specific databases

CTD2902.
MGIMGI:95819. Grin1.

Phylogenomic databases

eggNOGNOG282132.
GeneTreeENSGT00740000115410.
HOGENOMHOG000231491.
HOVERGENHBG052638.
KOK05208.
TreeFamTF351405.

Gene expression databases

BgeeP35438.
CleanExMM_GRIN1.
GenevestigatorP35438.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR018882. CaM-bd_C0_NMDA_rcpt_NR1.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF10562. CaM_bdg_C0. 1 hit.
PF00060. Lig_chan. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

NextBio286995.
PROP35438.
SOURCESearch...

Entry information

Entry nameNMDZ1_MOUSE
AccessionPrimary (citable) accession number: P35438
Secondary accession number(s): A2AI15, A2AI18, Q8CFS4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot