Grin2d
Domain
A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter.
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:1385220). Participates in synaptic plasticity for learning and memory formation (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:1385220, PubMed:7790891). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 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. NR2D/GRIN2D subfamily.
Tissue Specificity
Detected in neonate brain synaptosomes (at protein level).
Cellular localization
- Cell membrane
- Multi-pass membrane protein
- Postsynaptic cell membrane
- Multi-pass membrane protein
Alternative names
GluN2D, Grin2d, Glutamate [NMDA] receptor subunit epsilon-4, N-methyl D-aspartate receptor subtype 2D, NMDAR2D, NR2D