Grin3a
entrez
191573
canonical
uniprot
Q9R1M7
canonical
ensembl
ENSRNOG00055020470
resolver
ensembl
ENSRNOG00060005622
resolver
ensembl
ENSRNOG00065010818
resolver
genesymbol
Grin3a
resolver
uniprot
O09098
resolver
uniprot
O09155
resolver
uniprot
Q62800
resolver
uniprot
Q63268
resolver
uniprot
Q9Z2H0
resolver
uniprot_entry
NMD3A_RAT
resolver
uniprot_sec
O09098
resolver
uniprot_sec
O09155
resolver
uniprot_sec
Q62800
resolver
uniprot_sec
Q63268
resolver
uniprot_sec
Q9Z2H0
resolver
activity_regulation
ACTIVITY REGULATION: Excitatory glycine receptors are inhibited by D-serine at a concentrion of 10uM. {ECO:0000269|PubMed:11823786}.
uniprot
proteins
amino_acid_sequence
MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTTAPRAASRAQEGGRAGAQRDDPESGTWRPPAPSQGARWLGSALHGRGPPGSRKLGEGAGAETLWPRDALLFAVENLNRVEGLLPYNLSLEVVMAIEAGLGDLPLMPFSSPSSPWSSDPFSFLQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSSVLHIPVLSIVRHEFPRESQNPLHLQLSLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTENNSKFHLESVINITANLSSTKDLLSFLQVQMDNIRNSTPTMVMFGCDMDSIRQIFEMSTQFGLSPPELHWVLGDSQNVEELRTEGLPLGLIAHGKTTQSVFEYYVQDAMELVARAVATATMIQPELALLPSTMNCMDVKTTNLTSGQYLSRFLANTTFRGLSGSIKVKGSTIISSENNFFIWNLQHDPMGKPMWTRLGSWQGGRIVMDSGIWPEQAQRHKTHFQHPNKLHLRVVTLIEHPFVFTREVDDEGLCPAGQLCLDPMTNDSSMLDRLFSSLHSSNDTVPIKFKKCCYGYCIDLLEQLAEDMNFDFDLYIVGDGKYGAWKNGHWTGLVGDLLSGTANMAVTSFSINTARSQVIDFTSPFFSTSLGILVRTRDTAAPIGAFMWPLHWTMWLGIFVALHITAIFLTLYEWKSPFGMTPKGRNRNKVFSFSSALNVCYALLFGRTAAIKPPKCWTGRFLMNLWAIFCMFCLSTYTANLAAVMVGEKIYEELSGIHDPKLHHPSQGFRFGTVRESSAEDYVRQSFPEMHEYMRRYNVPATPDGVQYLKNDPEKLDAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPPNSPLTSNISELISQYKSHGFMDVLHDKWYKVVPCGKRSFAVTETLQMGIKHFSGLFVLLCIGFGLSILTTIGEHIVHRLLLPRIKNKSKLQYWLHTSQRFHRALNTSFVEEKQPRSKTKRVEKSRWRRWTCKTEGDSELSLFPRSNLGPQQLMVWNTSNLSHDNQRKYIFNDEEGQNQLGTQAHQDIPLPQRRRELPASLTTNGKADSLNVTRSSVIQELSELEKQIQVIRQELQLAVSRKTELEEYQKTNRTCES
uniprot
proteins
function
FUNCTION: Component of a non-conventional N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with low calcium permeability and low voltage-dependent block by Mg(2+) (PubMed:11160393, PubMed:11823786, PubMed:11929923, PubMed:18003876). During the development of neural circuits, participates in the synaptic refinement period, restricting spine maturation and growth (PubMed:25009255). Forms glutamatergic receptor complexes with GluN1 and GluN2 subunits which are activated by glycine binding to the GluN1 and GluN3 subunits and L-glutamate binding to GluN2 subunits (PubMed:11929923). Forms excitatory glycinergic receptor complexes with GluN1 alone which are activated by glycine binding to the GluN1 and GluN3 subunits (PubMed:11823786). GluN3A subunit also binds D-serine (PubMed:18636091). Each GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:11160393, PubMed:11929923). By competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting signaling and limiting the maturation and growth of inactive synapses (PubMed:24297929). {ECO:0000269|PubMed:11160393, ECO:0000269|PubMed:11823786, ECO:0000269|PubMed:11929923, ECO:0000269|PubMed:18003876, ECO:0000269|PubMed:18636091, ECO:0000269|PubMed:24297929, ECO:0000269|PubMed:25009255}.
uniprot
proteins
mass_dalton
127607
uniprot
proteins
mutagenesis
MUTAGEN 971..973; /note="YWL->AAA: Endocytosis-deficient. When transfected in pyramidal neurons transfected, increases the rate of spine elimination and reduction in the stability of preexisting spines, compared to the wild-type protein. No effect on spine growth rate."; /evidence="ECO:0000269|PubMed:25009255"; MUTAGEN 1082..1115; /note="Missing: When expressed in pyramidal neurons, increases spine stability and reduces spine elimination."; /evidence="ECO:0000269|PubMed:25009255
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:11160393}.
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR3A/GRIN3A subfamily
uniprot
proteins
pubmed
11160393
uniprot
proteins
pubmed
11588171
uniprot
proteins
pubmed
11823786
uniprot
proteins
pubmed
11929923
uniprot
proteins
pubmed
12391275
uniprot
proteins
pubmed
18003876
uniprot
proteins
pubmed
18636091
uniprot
proteins
pubmed
23972471
uniprot
proteins
pubmed
24297929
uniprot
proteins
pubmed
25009255
uniprot
proteins
pubmed
7472412
uniprot
proteins
pubmed
7472413
uniprot
proteins
pubmed
9891978
uniprot
proteins
sequence_length
1135
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11160393, ECO:0000269|PubMed:11588171}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13224}. Postsynaptic cell membrane {ECO:0000269|PubMed:11588171}. Postsynaptic density {ECO:0000269|PubMed:11588171}. Note=Requires the presence of GRIN1 to be targeted at the plasma membrane. {ECO:0000269|PubMed:11160393}.
uniprot
proteins
transmembrane_region
TRANSMEM 675..694; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q13224"; TRANSMEM 742..761; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q13224"; TRANSMEM 933..948; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q13224
uniprot
proteins