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GRIN1 glutamate ionotropic receptor NMDA type subunit 1 [ Homo sapiens (human) ]

Gene ID: 2902, updated on 9-Jul-2021

Summary

Official Symbol
GRIN1provided by HGNC
Official Full Name
glutamate ionotropic receptor NMDA type subunit 1provided by HGNC
Primary source
HGNC:HGNC:4584
See related
Ensembl:ENSG00000176884 MIM:138249
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
NR1; MRD8; GluN1; NMDA1; NDHMSD; NDHMSR; NMD-R1; NMDAR1
Summary
The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits. Alternatively spliced transcript variants have been described. [provided by RefSeq, Jul 2008]
Expression
Restricted expression toward brain (RPKM 50.5) See more
Orthologs
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Genomic context

See GRIN1 in Genome Data Viewer
Location:
9q34.3
Exon count:
22
Annotation release Status Assembly Chr Location
109.20210514 current GRCh38.p13 (GCF_000001405.39) 9 NC_000009.12 (137139092..137168759)
105.20201022 previous assembly GRCh37.p13 (GCF_000001405.25) 9 NC_000009.11 (140033606..140063208)

Chromosome 9 - NC_000009.12Genomic Context describing neighboring genes Neighboring gene mannosidase alpha class 1B member 1 Neighboring gene dipeptidyl peptidase 7 Neighboring gene uncharacterized LOC105376328 Neighboring gene microRNA 3621 Neighboring gene leucine rich repeat containing 26 Neighboring gene transmembrane protein 210

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env HIV-1 gp120-induced dephosphorylation of KV2.1 is dependent on NMDA receptor-mediated activation of protein phosphatase 2B or calcineurin PubMed
env HIV-1 gp120 activates forward trafficking and surface clustering of NMDA receptors in membrane microdomains by a PKA-dependent phosphorylation of the NR1 C-terminal Ser897, followed by a PKC-dependent phosphorylation of Ser896 PubMed
env HIV-1 gp120-induced synapse loss requires sequential activation of CXCR4, IL-1beta receptor, and NMDA receptor PubMed
env HIV-1 gp120 activates NMDA receptor directly and phosphorylates JNK through a gp120-mediated apoptotic pathway in human neuroblastoma cells PubMed
env HIV-1 clade B gp120 significantly downregulates NMDA receptor gene and protein expression and levels of glutamine compared to clade C gp120 PubMed
env HIV-1 gp120-mediated human cell death involves the NMDA receptor complex; antagonists of the NMDA receptor reverse the gp120-mediated effects PubMed
env HIV-1 gp120 causes an activation of phospholipase A2, resulting in the increased release of arachidonic acid, which may sensitize the NMDA receptor PubMed
env HIV-1 gp120 binds to cells expressing epsilon1/zeta1 or epsilon2/zeta1 combined NMDA receptor subunits, but not to cells expressing a single epsilon1, epsilon2, or zeta1 NMDA receptor subunit PubMed
Tat tat The gene expression of GRIN1 is significantly upregulated in both clade B and clade C Tat treated SK-N-MC neuroblastoma cells PubMed
tat Ca(2+) influx through the NMDA receptor is necessary for HIV-1 Tat-induced synapse loss PubMed
tat HIV-1 Tat-induced dendritic swellings that act in striatal neurons are regulated by NMDA and AMPA receptor-related events PubMed
tat HIV-1 Tat upregulates the expression of NMDARs for the apoptosis of retinal pigmen epithelium (RPE) cells. Silencing of NMDARs by siRNA abolishes Tat-induced RPE apoptosis PubMed
tat HIV-1 Tat-induced activation of spermine oxidase (SMO) activity involves NMDAR stimulation in human neuroblastoma PubMed
tat HIV-1 Tat and methamphetamine inhibit the normal conjunction of signaling between D1 and NMDA receptors, resulting in neural dysfunction and death PubMed
tat HIV-1 Tat interacts with NMDA receptors in primary neuronal-glial cultures and in hippocampal slice cultures PubMed
tat Tat treatment causes activation of neuronal nitric oxide synthase (nNOS) through association with NMDA receptors PubMed
tat HIV-1 Tat treatment induces the formation of complexes involving the low-density lipoprotein receptor-related protein (LRP), postsynaptic density protein-95 (PSD-95), and N-methyl-d-aspartic acid (NMDA) receptors at the neuron surface PubMed
tat HIV-1 Tat-induced NMDA receptor activation is clade dependent. The Cys 30-Cys 31 motif in Tat is critical for the NMDA receptor activation PubMed
tat HIV-1 Tat upregulates expression of NMDA receptor 1 in mixed cultures of human neurons and astrocytes PubMed
tat HIV-1 Tat induces apoptosis of neurons and neurotoxicity through the activation of both NMDA and non-NMDA receptors PubMed

Go to the HIV-1, Human Interaction Database

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
contributes_to NMDA glutamate receptor activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
contributes_to NMDA glutamate receptor activity IDA
Inferred from Direct Assay
more info
PubMed 
enables NMDA glutamate receptor activity IDA
Inferred from Direct Assay
more info
PubMed 
enables NMDA glutamate receptor activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables NMDA glutamate receptor activity ISS
Inferred from Sequence or Structural Similarity
more info
 
enables NMDA glutamate receptor activity TAS
Traceable Author Statement
more info
PubMed 
enables amyloid-beta binding ISS
Inferred from Sequence or Structural Similarity
more info
 
contributes_to calcium channel activity IDA
Inferred from Direct Assay
more info
PubMed 
enables calcium ion binding ISS
Inferred from Sequence or Structural Similarity
more info
 
enables calmodulin binding ISS
Inferred from Sequence or Structural Similarity
more info
 
enables glutamate binding IDA
Inferred from Direct Assay
more info
PubMed 
enables glutamate-gated calcium ion channel activity IDA
Inferred from Direct Assay
more info
PubMed 
enables glycine binding IDA
Inferred from Direct Assay
more info
PubMed 
enables glycine binding IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables ligand-gated ion channel activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables neurotransmitter binding ISS
Inferred from Sequence or Structural Similarity
more info
 
enables protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables protein-containing complex binding ISS
Inferred from Sequence or Structural Similarity
more info
 
enables signaling receptor activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Process Evidence Code Pubs
involved_in brain development NAS
Non-traceable Author Statement
more info
PubMed 
involved_in calcium ion homeostasis ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in calcium ion transmembrane import into cytosol IDA
Inferred from Direct Assay
more info
PubMed 
involved_in calcium-mediated signaling IEA
Inferred from Electronic Annotation
more info
 
involved_in cation transport IDA
Inferred from Direct Assay
more info
PubMed 
NOT involved_in cellular response to amyloid-beta IGI
Inferred from Genetic Interaction
more info
PubMed 
involved_in chemical synaptic transmission IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in excitatory chemical synaptic transmission NAS
Non-traceable Author Statement
more info
PubMed 
involved_in excitatory postsynaptic potential ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in ionotropic glutamate receptor signaling pathway IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in ionotropic glutamate receptor signaling pathway IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in ionotropic glutamate receptor signaling pathway ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in positive regulation of calcium ion transport into cytosol ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in positive regulation of cysteine-type endopeptidase activity ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
involved_in positive regulation of excitatory postsynaptic potential ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in positive regulation of reactive oxygen species biosynthetic process ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in positive regulation of transcription by RNA polymerase II ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in propylene metabolic process ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in protein heterotetramerization ISS
Inferred from Sequence or Structural Similarity
more info
 
involved_in regulation of membrane potential IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in regulation of membrane potential IDA
Inferred from Direct Assay
more info
PubMed 
involved_in regulation of synaptic plasticity NAS
Non-traceable Author Statement
more info
PubMed 
involved_in response to ethanol IDA
Inferred from Direct Assay
more info
PubMed 
involved_in response to glycine IDA
Inferred from Direct Assay
more info
PubMed 
involved_in visual learning ISS
Inferred from Sequence or Structural Similarity
more info
 
Component Evidence Code Pubs
part_of NMDA selective glutamate receptor complex IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
part_of NMDA selective glutamate receptor complex IDA
Inferred from Direct Assay
more info
PubMed 
part_of NMDA selective glutamate receptor complex TAS
Traceable Author Statement
more info
PubMed 
located_in cell surface ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
located_in cytoplasm ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
located_in dendrite IDA
Inferred from Direct Assay
more info
PubMed 
located_in dendritic spine ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
 
located_in excitatory synapse ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in integral component of plasma membrane IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in neuron projection IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in neuron projection ISS
Inferred from Sequence or Structural Similarity
more info
 
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
PubMed 
located_in plasma membrane TAS
Traceable Author Statement
more info
 
located_in postsynaptic density ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in postsynaptic membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
is_active_in synapse IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in synapse ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in synaptic cleft ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in synaptic membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in synaptic vesicle ISS
Inferred from Sequence or Structural Similarity
more info
 
located_in terminal bouton ISS
Inferred from Sequence or Structural Similarity
more info
 

General protein information

Preferred Names
glutamate receptor ionotropic, NMDA 1
Names
N-methyl-D-aspartate receptor channel, subunit zeta-1
N-methyl-D-aspartate receptor subunit NR1
glutamate [NMDA] receptor subunit zeta-1
glutamate receptor, ionotropic, N-methyl D-aspartate 1
putative NMDtranscript(altAcc_e2)

NCBI Reference Sequences (RefSeq)

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_011507.1 RefSeqGene

    Range
    4998..34600
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_000832.7NP_000823.4  glutamate receptor ionotropic, NMDA 1 isoform GluN1-4a precursor

    See identical proteins and their annotated locations for NP_000823.4

    Status: REVIEWED

    Description
    Transcript Variant: This variant (GluN1-4a, also known as NR1-1) lacks an alternate in-frame exon and uses an alternate splice site in the 3' coding region, compared to variant GluN1-1a. The resulting protein (isoform GluN1-4a, also known as isoform NR1-1) is shorter and has a different C-terminus, compared to isoform GluN1-1a.
    Source sequence(s)
    AL929554, L13266
    Consensus CDS
    CCDS43910.1
    UniProtKB/Swiss-Prot
    Q05586
    Related
    ENSP00000360614.4, ENST00000371559.8
    Conserved Domains (3) summary
    cd13719
    Location:395799
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25383
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:835863
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  2. NM_001185090.2NP_001172019.1  glutamate receptor ionotropic, NMDA 1 isoform GluN1-3b precursor

    See identical proteins and their annotated locations for NP_001172019.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (GluN1-3b, also known as NR1-4) contains an alternate coding segment and uses a different splice site in the 3' coding region, compared to variant GluN1-1a. The resulting protein (isoform GluN1-3b, also known as isoform NR1-4) is longer and has a distinct C-terminus when it is compared to isoform GluN1-1a. This variant has also been named isoform 4b or NMDAR1-4b.
    Source sequence(s)
    AB208999, AF015731, AL929554, BU728516, L13268
    Consensus CDS
    CCDS55354.1
    UniProtKB/Swiss-Prot
    Q05586
    UniProtKB/TrEMBL
    Q59GW0
    Related
    ENSP00000360608.3, ENST00000371553.7
    Conserved Domains (3) summary
    cd13719
    Location:416820
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25404
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:856884
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  3. NM_001185091.2NP_001172020.1  glutamate receptor ionotropic, NMDA 1 isoform GluN1-5b precursor

    See identical proteins and their annotated locations for NP_001172020.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (GluN1-5b, also known as 5) contains an alternate coding segment, lacks a different alternate coding segment, and uses a different splice site in the 3' coding region, compared to variant GluN1-1a. The resulting protein (isoform GluN1-5b, also known as isoform 5) is shorter and has a distinct C-terminus when it is compared to isoform GluN1-1a. This variant has also been named isoform 3b or NMDAR1-3b.
    Source sequence(s)
    AB208999, AF015730, AL929554, BU728516, L13268
    Consensus CDS
    CCDS55355.1
    UniProtKB/Swiss-Prot
    Q05586
    UniProtKB/TrEMBL
    Q59GW0
    Related
    ENSP00000360615.3, ENST00000371560.4
    Conserved Domains (3) summary
    cd13719
    Location:416820
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25404
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:856884
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  4. NM_007327.4NP_015566.1  glutamate receptor ionotropic, NMDA 1 isoform GluN1-1a precursor

    See identical proteins and their annotated locations for NP_015566.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (GluN1-1a, also known as NR1-3) represents the longest transcript and encodes protein isoform GluN1-1a (also known as isoform NR1-3).
    Source sequence(s)
    AL929554, D13515
    Consensus CDS
    CCDS7031.1
    UniProtKB/Swiss-Prot
    Q05586
    Related
    ENSP00000360616.3, ENST00000371561.8
    Conserved Domains (3) summary
    cd13719
    Location:395799
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25383
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:835863
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  5. NM_021569.4NP_067544.1  glutamate receptor ionotropic, NMDA 1 isoform GluN1-2a precursor

    See identical proteins and their annotated locations for NP_067544.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (GluN1-2a, also known as NR1-2) lacks an alternate in-frame exon in the 3' coding region, compared to variant GluN1-1a, resulting in a shorter protein (isoform GluN1-2a, also known as isoform NR1-2), compared to isoform GluN1-1a.
    Source sequence(s)
    AL929554, D13515, L13267
    Consensus CDS
    CCDS7032.1
    UniProtKB/Swiss-Prot
    Q05586
    Related
    ENSP00000360605.4, ENST00000371550.8
    Conserved Domains (3) summary
    cd13719
    Location:395799
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25383
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:835863
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit

RefSeqs of Annotated Genomes: Homo sapiens Updated Annotation Release 109.20210514

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000009.12 Reference GRCh38.p13 Primary Assembly

    Range
    137139092..137168759
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005266073.4XP_005266130.1  glutamate receptor ionotropic, NMDA 1 isoform X1

    See identical proteins and their annotated locations for XP_005266130.1

    UniProtKB/Swiss-Prot
    Q05586
    Related
    ENSP00000360601.4, ENST00000371546.8
    Conserved Domains (3) summary
    cd13719
    Location:416820
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25404
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:856884
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  2. XM_005266072.3XP_005266129.1  glutamate receptor ionotropic, NMDA 1 isoform X3

    See identical proteins and their annotated locations for XP_005266129.1

    UniProtKB/TrEMBL
    Q5VSF9
    Related
    ENSP00000360610.4, ENST00000371555.8
    Conserved Domains (3) summary
    cd13719
    Location:416820
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25404
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:856884
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  3. XM_011518583.2XP_011516885.1  glutamate receptor ionotropic, NMDA 1 isoform X4

    See identical proteins and their annotated locations for XP_011516885.1

    Related
    ENST00000471122.5
    Conserved Domains (3) summary
    cd13719
    Location:416820
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25404
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:856884
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
  4. XM_005266071.3XP_005266128.1  glutamate receptor ionotropic, NMDA 1 isoform X2

    See identical proteins and their annotated locations for XP_005266128.1

    UniProtKB/Swiss-Prot
    Q05586
    Conserved Domains (3) summary
    cd13719
    Location:395799
    PBP2_iGluR_NMDA_Nr1; The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily
    cd06379
    Location:25383
    PBP1_iGluR_NMDA_NR1; N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor
    pfam10562
    Location:835863
    CaM_bdg_C0; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit
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