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P35439 (NMDZ1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. 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:Nmdar1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Mediated by glycine. 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. Ref.18

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 By similarity. Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB. Found in a complex with GRIN2A or GRIN2B and GRIN3B. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes By similarity. Interacts with DLG4 and MPDZ. Interacts with LRFN1 and LRFN2. Interacts with MYZAP. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17

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.

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. Ref.7 Ref.12

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
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to manganese ion

Inferred from expression pattern PubMed 19643132. Source: RGD

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

conditioned taste aversion

Inferred from electronic annotation. Source: Ensembl

ionotropic glutamate receptor signaling pathway

Inferred from direct assay PubMed 16477151. Source: RGD

learning or memory

Traceable author statement PubMed 12535174. Source: RGD

long-term memory

Inferred from electronic annotation. Source: Ensembl

male mating behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

olfactory learning

Inferred from electronic annotation. Source: Ensembl

pons maturation

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell death

Inferred from direct assay PubMed 20168047. Source: RGD

positive regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 12930820. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

propylene metabolic process

Inferred from electronic annotation. Source: Ensembl

protein tetramerization

Inferred from direct assay PubMed 22493736. Source: RGD

regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of ion transmembrane transport

Inferred from mutant phenotype PubMed 17050728. Source: GOC

regulation of long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from expression pattern PubMed 19918184. Source: RGD

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from expression pattern PubMed 19761817. Source: RGD

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to fungicide

Inferred from expression pattern PubMed 19591855. Source: RGD

response to morphine

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from expression pattern PubMed 19322657. Source: RGD

rhythmic process

Inferred from direct assay PubMed 16477151. Source: RGD

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from electronic annotation. Source: Ensembl

suckling behavior

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 16477151PubMed 17050728PubMed 22493736. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

dendrite membrane

Inferred from direct assay PubMed 15620359. Source: BHF-UCL

dendritic spine

Inferred from direct assay PubMed 17207780. Source: RGD

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

excitatory synapse

Inferred from direct assay PubMed 19730411. Source: BHF-UCL

postsynaptic density

Inferred from direct assay PubMed 17207780PubMed 21314939. Source: RGD

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from direct assay PubMed 15681343PubMed 15978582PubMed 17003121. Source: MGI

synaptic cleft

Inferred from direct assay PubMed 17207780. Source: RGD

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from direct assay PubMed 19666514. Source: RGD

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay PubMed 16477151PubMed 22098737. Source: RGD

calcium channel activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction PubMed 15069201. Source: RGD

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glutamate binding

Inferred from direct assay PubMed 8011339. Source: UniProtKB

glutamate receptor binding

Inferred from physical interaction PubMed 19298817. Source: RGD

glycine binding

Inferred from direct assay PubMed 8011339. Source: UniProtKB

ionotropic glutamate receptor activity

Inferred from direct assay PubMed 16477151. Source: RGD

neurotransmitter binding

Inferred from direct assay PubMed 16477151. Source: RGD

protein binding

Inferred from physical interaction Ref.13. Source: IntAct

protein dimerization activity

Inferred from direct assay PubMed 22493736. Source: RGD

protein heterodimerization activity

Inferred from direct assay PubMed 21544205. Source: RGD

receptor binding

Inferred from physical interaction PubMed 12408866. Source: RGD

voltage-gated cation channel activity

Inferred from mutant phenotype PubMed 17050728. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4P310164EBI-877897,EBI-375655
Lrfn2Q460M52EBI-877897,EBI-877185
Lrfn2Q80TG92EBI-877923,EBI-877092From a different organism.
Pdzk1Q9JJ403EBI-877897,EBI-7713572

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P35439-1)

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 B (identifier: P35439-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
Isoform C (identifier: P35439-3)

Also known as: NMDAR1-2a subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     864-900: Missing.
Isoform D (identifier: P35439-4)

The sequence of this isoform differs from the canonical sequence as follows:
     901-938: STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES → QYHPTDITGPLNLSDPSVSTVV
Isoform E (identifier: P35439-5)

The sequence of this isoform differs from the canonical sequence as follows:
     864-885: DRKSGRAEPDPKKKATFRAITS → QYHPTDITGPLNLSDPSVSTVV
     886-938: Missing.
Isoform F (identifier: P35439-6)

Also known as: NMDAR1-2b subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     864-900: Missing.
Isoform G (identifier: P35439-7)

Also known as: NMDAR1-4b subunit;

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: K → KSKKRNYENLDQLSYDNKRGPK
     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_0000011589

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

Sites

Binding site5231Glycine
Binding site6881Glycine
Binding site7321Glycine

Amino acid modifications

Modified residue8891Phosphoserine; by PKC By similarity
Modified residue8901Phosphoserine; by PKC Ref.12
Modified residue8961Phosphoserine; by PKC By similarity
Modified residue8971Phosphoserine; by PKC Ref.7
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 sequence1901K → KSKKRNYENLDQLSYDNKRG PK in isoform B, isoform F and isoform G.
VSP_000140
Alternative sequence864 – 90037Missing in isoform F and isoform C.
VSP_000141
Alternative sequence864 – 88522DRKSG…RAITS → QYHPTDITGPLNLSDPSVST VV in isoform E and isoform G.
VSP_000142
Alternative sequence886 – 93853Missing in isoform E and isoform G.
VSP_000143
Alternative sequence901 – 93838STGGG…RHRES → QYHPTDITGPLNLSDPSVST VV in isoform D.
VSP_000144

Secondary structure

............................................................................................................................. 938
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 1994. Version 1.
Checksum: 613D36E38F05BC73

FASTA938105,509
        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 ARELEARVII 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 VPQCCYGFCI 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 B [UniParc].

Checksum: D965531F6C38EDDD
Show »

FASTA959108,045
Isoform C (NMDAR1-2a subunit) [UniParc].

Checksum: A320F3585664F652
Show »

FASTA901101,345
Isoform D [UniParc].

Checksum: E31E00296E49D08D
Show »

FASTA922103,615
Isoform E [UniParc].

Checksum: 6DAA83EFC08C30D8
Show »

FASTA88599,451
Isoform F (NMDAR1-2b subunit) [UniParc].

Checksum: 847CEED410182B5C
Show »

FASTA922103,881
Isoform G (NMDAR1-4b subunit) [UniParc].

Checksum: 1872055038F790FF
Show »

FASTA906101,987

References

[1]"Molecular cloning and characterization of the rat NMDA receptor."
Moriyoshi K., Masu M., Ishii T., Shigemoto R., Mizuno N., Nakanishi S.
Nature 354:31-37(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Brain.
[2]"Alternative splicing generates functionally distinct N-methyl-D-aspartate receptors."
Nakanishi N., Axel R., Shneider N.A.
Proc. Natl. Acad. Sci. U.S.A. 89:8552-8556(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor."
Hollmann M., Boulter J., Maron C., Beasley L., Sullivan J., Pecht G., Heinemann S.F.
Neuron 10:943-954(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Forebrain.
[4]"Cloning and analysis of the 5' flanking sequence of the rat N-methyl-D-aspartate receptor 1 (NMDAR1) gene."
Bai G., Kusiak J.W.
Biochim. Biophys. Acta 1152:197-200(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
Strain: Sprague-Dawley.
Tissue: Liver.
[5]"Structures and properties of seven isoforms of the NMDA receptor generated by alternative splicing."
Sugihara H., Moriyoshi K., Ishii T., Masu M., Nakanishi S.
Biochem. Biophys. Res. Commun. 185:826-832(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
Tissue: Brain.
[6]"Combinatorial RNA splicing alters the surface charge on the NMDA receptor."
Anantharam V., Panchal R., Wilson A., Koltchin V.V., Treistman S.N., Bayley H.
FEBS Lett. 305:27-30(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
Tissue: Brain.
[7]"An NMDA receptor signaling complex with protein phosphatase 2A."
Chan S.F., Sucher N.J.
J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-897, DEPHOSPHORYLATION BY PPP2CB, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B; GRIN3A AND PPP2CB.
[8]"Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors."
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F.
J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[9]"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits."
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.
Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[10]"Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons."
Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V., Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J., Lipton S.A.
J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
[11]"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation."
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.
Neuron 43:563-574(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPDZ AND DLG4.
[12]"Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms."
Sanchez-Perez A.M., Felipo V.
Neurochem. Int. 47:84-91(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-890.
[13]"A novel family of adhesion-like molecules that interacts with the NMDA receptor."
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN2.
[14]"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN1.
[15]"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.
[16]"Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core."
Furukawa H., Gouaux E.
EMBO J. 22:2873-2885(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS AND ANTAGONIST.
[17]"Subunit arrangement and function in NMDA receptors."
Furukawa H., Singh S.K., Mancusso R., Gouaux E.
Nature 438:185-192(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 394-800 IN COMPLEX WITH GRIN2A; GLYCINE AND GLUTAMATE, SUBUNIT.
[18]"Mechanism of partial agonist action at the NR1 subunit of NMDA receptors."
Inanobe A., Furukawa H., Gouaux E.
Neuron 47:71-84(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONISTS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63255 mRNA. Translation: CAA44914.1.
AY157515 Genomic DNA. Translation: AAA16366.1.
U08261 mRNA. Translation: AAB50926.1.
U08262 mRNA. Translation: AAB50927.1.
U08263 mRNA. Translation: AAB50928.1.
U08264 mRNA. Translation: AAB50929.1.
U08265 mRNA. Translation: AAB50930.1.
U08267 mRNA. Translation: AAB50932.1.
U08268 mRNA. Translation: AAB50933.1.
S39217 mRNA. Translation: AAB22431.1.
S39218 mRNA. Translation: AAB22432.1.
S39219 mRNA. Translation: AAB22433.1.
S39220 mRNA. Translation: AAB22434.1.
S39221 mRNA. Translation: AAB22435.1.
X65227 mRNA. Translation: CAA46335.1.
PIRJN0336.
JN0337.
JN0338.
JN0339.
JN0340.
JN0341.
JN0342.
S19710.
RefSeqNP_001257531.1. NM_001270602.1. [P35439-2]
NP_001257532.1. NM_001270603.1. [P35439-6]
NP_001257534.1. NM_001270605.1. [P35439-3]
NP_001257537.1. NM_001270608.1. [P35439-7]
NP_001257539.1. NM_001270610.1. [P35439-5]
NP_001274352.1. NM_001287423.1. [P35439-4]
NP_058706.1. NM_017010.2. [P35439-1]
UniGeneRn.9840.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PB7X-ray1.35A394-544[»]
A663-800[»]
1PB8X-ray1.45A394-544[»]
A663-800[»]
1PB9X-ray1.60A394-544[»]
A663-800[»]
1PBQX-ray1.90A/B394-800[»]
1Y1MX-ray1.80A/B394-544[»]
A/B663-800[»]
1Y1ZX-ray1.50A394-544[»]
A663-800[»]
1Y20X-ray1.40A394-544[»]
A663-800[»]
2A5TX-ray2.00A394-544[»]
3Q41X-ray3.40A/B/C21-393[»]
4KCCX-ray1.89A394-544[»]
A663-800[»]
4KFQX-ray2.20A/B394-544[»]
A/B663-800[»]
4NF4X-ray2.00A394-544[»]
A663-800[»]
4NF5X-ray1.90A394-544[»]
A663-800[»]
4NF6X-ray2.10A394-544[»]
A663-800[»]
4NF8X-ray1.86A394-544[»]
A663-800[»]
ProteinModelPortalP35439.
SMRP35439. Positions 396-800.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246573. 7 interactions.
DIPDIP-674N.
IntActP35439. 11 interactions.
MINTMINT-101336.

Chemistry

BindingDBP35439.
ChEMBLCHEMBL2096680.
GuidetoPHARMACOLOGY455.

PTM databases

PhosphoSiteP35439.

Proteomic databases

PaxDbP35439.
PRIDEP35439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726. [P35439-2]
ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
GeneID24408.
KEGGrno:24408.
UCSCRGD:2736. rat. [P35439-1]

Organism-specific databases

CTD2902.
RGD2736. Grin1.

Phylogenomic databases

eggNOGNOG282132.
GeneTreeENSGT00740000115410.
HOGENOMHOG000231491.
HOVERGENHBG052638.
KOK05208.
OMAWNHVILL.
OrthoDBEOG79GT5V.
PhylomeDBP35439.
TreeFamTF351405.

Gene expression databases

ArrayExpressP35439.
GenevestigatorP35439.

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

EvolutionaryTraceP35439.
NextBio603223.
PROP35439.

Entry information

Entry nameNMDZ1_RAT
AccessionPrimary (citable) accession number: P35439
Secondary accession number(s): Q62646
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 162 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references