Grin1
entrez
24408
canonical
uniprot
P35439
canonical
ensembl
ENSRNOG00000011726
resolver
ensembl
ENSRNOG00055000504
resolver
ensembl
ENSRNOG00060031665
resolver
ensembl
ENSRNOG00065025127
resolver
ensp
ENSRNOP00000029227
resolver
ensp
ENSRNOP00000043301
resolver
ensp
ENSRNOP00000049198
resolver
enst
ENSRNOT00000037725
resolver
genesymbol
Grin1
resolver
genesymbol_syn
NMDAR1
resolver
genesymbol_syn
Nmdar1
resolver
uniprot
A0ACM8Q1Y1
resolver
uniprot
A6JT36
resolver
uniprot
Q62646
resolver
uniprot
Q62648
resolver
uniprot_entry
A0ACM8Q1Y1_RAT
resolver
uniprot_entry
A6JT36_RAT
resolver
uniprot_entry
NMDZ1_RAT
resolver
uniprot_sec
Q62646
resolver
uniprot_sec
Q62648
resolver
activity_regulation
ACTIVITY REGULATION: NMDA glutamate receptor activity is potentiated by Zn2(+) in a dose-dependent fashion (PubMed:7684237). The potentiating effect of Zn2(+) is at submicromolar concentrations and its inhibitory action is at high micromolar to millimolar concentrations (PubMed:7684237). Excitatory glycine receptors are inhibited by D-serine at 100uM (PubMed:11823786). {ECO:0000269|PubMed:11823786, ECO:0000269|PubMed:7684237}.
uniprot
proteins
amino_acid_sequence
MSTMHLLTFALLFSCSFARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYNWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEARELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGIIGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES
uniprot
proteins
function
FUNCTION: Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:1350383, PubMed:1388270, PubMed:1834949, PubMed:8428958). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:11823786, PubMed:1350383, PubMed:1388270, PubMed:15996549, PubMed:18177891, PubMed:1834949, PubMed:24876489, PubMed:27135925, PubMed:27618671, PubMed:28384476, PubMed:28468946, PubMed:8428958). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (By similarity). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:10436042, PubMed:11160393, PubMed:11929923, PubMed:28384476, PubMed:9463421). Forms excitatory glycinergic receptor complexes with GluN3 alone which are activated by glycine binding to the GluN1 and GluN3 subunits (PubMed:11823786, PubMed:11929923, PubMed:12391275). {ECO:0000250|UniProtKB:P35438, ECO:0000250|UniProtKB:Q05586, ECO:0000269|PubMed:10436042, ECO:0000269|PubMed:11160393, ECO:0000269|PubMed:11823786, ECO:0000269|PubMed:11929923, ECO:0000269|PubMed:12391275, ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549, ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949, ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:8428958, ECO:0000269|PubMed:9463421}.
uniprot
proteins
mass_dalton
105509
uniprot
proteins
post_translational_modification
PTM: NMDA is probably regulated by C-terminal phosphorylation of an isoform of NR1 by PKC (PubMed:11588171, PubMed:15936117). Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB) (PubMed:11588171). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity (PubMed:11588171). {ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:15936117}.; PTM: Ubiquitinated via 'Lys-48'-linked ubiquitin chains by the E3 ubiquitin ligase complex, at least composed of CUL3, KCTD13 and RBX1; leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q05586}.
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR1/GRIN1 subfamily
uniprot
proteins
pubmed
10436042
uniprot
proteins
pubmed
11160393
uniprot
proteins
pubmed
11588171
uniprot
proteins
pubmed
11823786
uniprot
proteins
pubmed
11929923
uniprot
proteins
pubmed
12391275
uniprot
proteins
pubmed
12805203
uniprot
proteins
pubmed
1350383
uniprot
proteins
pubmed
1352681
uniprot
proteins
pubmed
1386026
uniprot
proteins
pubmed
1388270
uniprot
proteins
pubmed
15312654
uniprot
proteins
pubmed
15936117
uniprot
proteins
pubmed
15996549
uniprot
proteins
pubmed
16281028
uniprot
proteins
pubmed
16495444
uniprot
proteins
pubmed
16630835
uniprot
proteins
pubmed
18177891
uniprot
proteins
pubmed
1834949
uniprot
proteins
pubmed
18849881
uniprot
proteins
pubmed
21389213
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24090084
uniprot
proteins
pubmed
24876489
uniprot
proteins
pubmed
26041915
uniprot
proteins
pubmed
26912815
uniprot
proteins
pubmed
27135925
uniprot
proteins
pubmed
27458189
uniprot
proteins
pubmed
27618671
uniprot
proteins
pubmed
28384476
uniprot
proteins
pubmed
28468946
uniprot
proteins
pubmed
7684237
uniprot
proteins
pubmed
8399301
uniprot
proteins
pubmed
8428958
uniprot
proteins
pubmed
9463421
uniprot
proteins
sequence_length
938
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549, ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949, ECO:0000269|PubMed:21389213, ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:8428958}; Multi-pass membrane protein {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Postsynaptic cell membrane {ECO:0000269|PubMed:26041915}. Synaptic cell membrane {ECO:0000269|PubMed:15312654}. Postsynaptic density membrane {ECO:0000269|PubMed:26041915}. Note=Synaptic cell membrane targeting is dependent of GRIN2B/GluN2B subunit (By similarity). Association with GRIN3A occurs in the endoplasmic reticulum (PubMed:11160393). {ECO:0000250|UniProtKB:P35438, ECO:0000269|PubMed:11160393}.
uniprot
proteins
transmembrane_region
TRANSMEM 560..580; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489"; TRANSMEM 631..647; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489"; TRANSMEM 813..833; /note="Helical"; /evidence="ECO:0000269|PubMed:24876489
uniprot
proteins