Recombinant Human Glutamate receptor ionotropic, NMDA 1 (GRIN1), Truncated

Uniprot Id

Q05586

Target Species

Human

Target Name

GRIN1

Target Full Name

Glutamate receptor ionotropic, NMDA 1

Target Function

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition.

Target Involvement

Neurodevelopmental disorder with or without hyperkinetic movements and seizures, autosomal dominant (NDHMSD)

Target Subcellular Location

Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, postsynaptic density.

Target Protein Families

Glutamate-gated ion channel (TC 1.A.10.1) family, NR1/GRIN1 subfamily

Target Research Area

Neuroscience

Target Synonyms

GluN1; Glutamate [NMDA] receptor subunit zeta-1; Glutamate receptor ionotropic N methyl D aspartate 1; Glutamate receptor ionotropic, N-methyl-D aspartate, subunit 1; glutamate receptor ionotropic, NMDA 1; Grin1; MRD8; N methyl D aspartate receptor; N methyl D aspartate receptor channel subunit zeta 1; N methyl D aspartate receptor subunit NR1; N-methyl-D-aspartate receptor subunit NR1; NMD-R1; NMDA 1; NMDA R1; NMDA receptor 1; NMDA1; NMDAR; NMDZ1_HUMAN; NR1

Target Background

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.