GRIN3B
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+) (By similarity). 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 (By similarity). Forms excitatory glycinergic receptor complexes with GluN1 alone which are activated by glycine binding to the GluN1 and GluN3 subunits. GluN3B subunit also binds D-serine and, in the absence of glycine, activates glycinergic receptor complexes, but with lower efficacy than glycine (By similarity). Each GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (By similarity).
Sequence Similarities
Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR3B/GRIN3B subfamily.
Cellular localization
- Cell membrane
- Multi-pass membrane protein
- Postsynaptic cell membrane
- Requires the presence of GRIN1 to be targeted at the plasma membrane.
Alternative names
GluN3B, N-methyl-D-aspartate receptor subtype 3B, NMDAR3B, NR3B, GRIN3B