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P35438 (NMDZ1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 [NMDA] receptor subunit zeta-1
Alternative name(s):
N-methyl-D-aspartate receptor subunit NR1
Short name=NMD-R1
Gene names
Name:Grin1
Synonyms:Glurz1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 GCOM1. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junction › synapse › postsynaptic cell membrane By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Note: Enriched in post-synaptic plasma membrane and post-synaptic densities By similarity. Ref.5

Post-translational modification

NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 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. Ref.6

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 functionIonic 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. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype. Source: MGI

cerebral cortex development

Inferred from mutant phenotype. Source: MGI

conditioned taste aversion

Inferred from mutant phenotype. Source: MGI

ionotropic glutamate receptor signaling pathway

Inferred from direct assay. Source: MGI

long-term memory

Inferred from mutant phenotype. Source: MGI

male mating behavior

Inferred from mutant phenotype. Source: MGI

negative regulation of neuron apoptosis

Inferred from mutant phenotype. Source: MGI

olfactory learning

Inferred from mutant phenotype. Source: MGI

pons maturation

Inferred from mutant phenotype. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay. Source: MGI

prepulse inhibition

Inferred from mutant phenotype. Source: MGI

regulation of axonogenesis

Inferred from mutant phenotype. Source: MGI

regulation of dendrite morphogenesis

Inferred from mutant phenotype. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype. Source: MGI

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype. Source: MGI

regulation of respiratory gaseous exchange

Inferred from mutant phenotype. Source: MGI

regulation of synapse assembly

Inferred from mutant phenotype. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype. Source: MGI

response to amphetamine

Inferred from mutant phenotype. Source: MGI

response to morphine

Inferred from mutant phenotype. Source: MGI

sensory perception of pain

Inferred from mutant phenotype. Source: MGI

social behavior

Inferred from mutant phenotype. Source: MGI

suckling behavior

Inferred from mutant phenotype. Source: MGI

synaptic transmission, glutamatergic

Inferred from mutant phenotype. Source: MGI

visual learning

Inferred from mutant phenotype. Source: MGI

   Cellular componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from physical interaction. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

growth cone

Non-traceable author statement. Source: UniProtKB

outer membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

postsynaptic density

Inferred from direct assay. Source: MGI

postsynaptic membrane

Inferred from direct assay. Source: MGI

synaptic vesicle

Inferred from direct assay. Source: MGI

synaptosome

Inferred from direct assay. Source: MGI

   Molecular functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay Ref.1. Source: MGI

calcium channel activity

Inferred from direct assay Ref.1. Source: MGI

calcium ion binding

Inferred from direct assay. Source: MGI

calmodulin binding

Inferred from direct assay. Source: MGI

extracellular-glutamate-gated ion channel activity

Inferred from electronic annotation. Source: InterPro

glycine binding

Inferred from mutant phenotype. Source: UniProtKB

receptor binding

Inferred from physical interaction. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q621088EBI-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 [NMDA] receptor subunit zeta-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 Ref.6
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: 1532151] [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: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[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: 15489334] [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: 12008020] [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: 14602821] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3B.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.
Tissue: Brain cortex.
[7]"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: 18849881] [Abstract]
Cited for: INTERACTION WITH GCOM1.
+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.
IPIIPI00118385.
IPI00608056.
PIRS21104.
RefSeqNP_001171127.1. NM_001177656.1.
NP_001171128.1. NM_001177657.1.
NP_032195.1. NM_008169.2.
UniGeneMm.278672.

3D structure databases

ProteinModelPortalP35438.
SMRP35438. Positions 24-394, 397-800.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31577N.
IntActP35438. 123 interactions.
MINTMINT-135802.
STRINGP35438.

PTM databases

PhosphoSiteP35438.

Proteomic databases

PRIDEP35438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028335; ENSMUSP00000028335; ENSMUSG00000026959.
ENSMUST00000114312; ENSMUSP00000109951; ENSMUSG00000026959.
GeneID14810.
KEGGmmu:14810.
UCSCuc008iri.2. mouse.
uc008irk.2. mouse.

Organism-specific databases

CTD2902.
MGIMGI:95819. Grin1.

Phylogenomic databases

HOVERGENHBG052638.
PhylomeDBP35438.

Gene expression databases

ArrayExpressP35438.
BgeeP35438.
CleanExMM_GRIN1.
GenevestigatorP35438.
GermOnlineENSMUSG00000026959. Mus musculus.

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.
IPR001638. SBP_bac_3.
[Graphical view]
KOK05208.
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]
ProtoNetSearch...

Other

NextBio286995.
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: November 16, 2011
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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