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Details on Person UniProt:P35438 Grin1
| Class:Id | ReferenceGeneProduct:96441 |
|---|---|
| _chainChangeLog | signal peptide:1-18 added on Sat February 7 2015;chain:19-938 added on Sat February 7 2015 |
| _displayName | UniProt:P35438 Grin1 |
| _timestamp | 2026-02-20 21:42:12 |
| chain | signal peptide:1-18 chain:19-938 |
| checksum | C610632DD3E06171 |
| comment | 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:12008020, PubMed:12860921, PubMed:14602821, PubMed:1532151, PubMed:8060614, PubMed:9049108). 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:12008020, PubMed:1532151, PubMed:7790891, PubMed:8060614). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (PubMed:12860921). 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:12008020, PubMed:14602821).CATALYTIC ACTIVITY Ca(2+)(in) = Ca(2+)(out)CATALYTIC ACTIVITY Na(+)(in) = Na(+)(out)CATALYTIC ACTIVITY K(+)(in) = K(+)(out)SUBUNIT Heterotetramer; the NMDAR subunits are modular and harbor tiered domains that function in concert to regulate opening and closing of the cation-selective ion channel pore (PubMed:12008020, PubMed:14602821). Forms heterotetrameric channels composed of two GluN1/zeta subunits (GRIN1), and two identical GluN2/epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) or GluN3 subunits (GRIN3A or GRIN3B) (in vitro) (PubMed:12008020, PubMed:14602821). Can also form heterotetrameric channels that contain at least two GluN1 subunits and at least two different GluN2 subunits (or a combination of one GluN2 and one GluN3 subunits) (in vitro) (PubMed:12008020, PubMed:14602821). In vivo, the subunit composition may vary in function of the expression levels of the different subunits (By similarity). Found in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB (By similarity). Found in a complex with GRIN2A or GRIN2B and GRIN3B (By similarity). Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (PubMed:23524343). Interacts with DLG4 and MPDZ. Interacts with LRFN1 and LRFN2 (By similarity). Interacts with MYZAP (PubMed:18849881). Found in a complex with DLG4 and PRR7 (By similarity). Found in a complex with GRIN2B and PRR7. Interacts with PRR7; the interaction is reduced following NMDA receptor activity (By similarity).INTERACTION Synaptic cell membrane targeting is dependent of GRIN2B/GluN2B subunit (PubMed:26041915). Association with GRIN3A occurs in the endoplasmic reticulum (By similarity).ALTERNATIVE PRODUCTS Detected in brain (at protein level). Detected in brain.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.DOMAIN The extracellular N-terminal domain (NTD) is a site of allosteric regulation to modulate overall receptor function.DOMAIN The ligand-binding domain (LBD) binds to glycine (GluN1 and GluN3 subunits) and glutamate (GluN2 subunits) and control opening of the channel gate.DOMAIN The transmembrane domain (TMD) harbors the channel gate and pore.PTM NMDA is probably regulated by C-terminal phosphorylation of an isoform of GRIN1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity.DISRUPTION PHENOTYPE Mutant mice are born at the expected Mendelian rate, appear grossly normal and have apparently normal brain structure, but the pups do not feed and all die during the first day after birth. Cerebellum granule cells and hippocampus pyramidal neurons from mutants lack NMDA-induced Ca(2+)influx and membrane currents, contrary to wild-type.SIMILARITY Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily. |
| description | recommendedName: fullName evidence="20"Glutamate receptor ionotropic, NMDA 1 shortName: GluN1 alternativeName: Glutamate [NMDA] receptor subunit zeta-1 alternativeName: N-methyl-D-aspartate receptor subunit NR1 shortName: NMD-R1 |
| geneName | Grin1 Glurz1 |
| identifier | P35438 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Calcium Cell membrane Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Magnesium Membrane Metal-binding Phosphoprotein Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport Zinc |
| modified | [InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10 [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 [InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12 [InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39 [InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18 [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 [InstanceEdit:423310] Kanapin, AA [InstanceEdit:435478] Kanapin, AA [InstanceEdit:435871] Kanapin, AA [InstanceEdit:447347] Kanapin, AA [InstanceEdit:525883] Kanapin, AA [InstanceEdit:613449] Kanapin, AA [InstanceEdit:797602] Kanapin, AA [InstanceEdit:937368] Yung, CK [InstanceEdit:1042053] Yung, CK [InstanceEdit:1220657] Yung, CK [InstanceEdit:1300696] Yung, CK [InstanceEdit:1301627] Yung, CK [InstanceEdit:1551960] Weiser, JD [InstanceEdit:1995863] Weiser, JD [InstanceEdit:2132304] Weiser, JD [InstanceEdit:2265580] Weiser, JD [InstanceEdit:3132113] Weiser, JD [InstanceEdit:3445779] Weiser, JD [InstanceEdit:4341137] Weiser, JD [InstanceEdit:5433710] Weiser, JD [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9657908] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9715482] Weiser, JD [InstanceEdit:9796772] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | Grin1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | NMDZ1_MOUSE A2AI15 A2AI18 Q8CFS4 |
| sequenceLength | 938 |
| species | [Species:48892] Mus musculus |
| (isoformParent) | [ReferenceIsoform:239757] UniProt:P35438-2 Grin1 [Mus musculus] [ReferenceIsoform:403818] UniProt:P35438-1 Grin1 [Mus musculus] |
| (referenceEntity) | [EntityWithAccessionedSequence:3928395] Grin1 [plasma membrane] [Mus musculus] [EntityWithAccessionedSequence:9610359] Grin1 [endoplasmic reticulum membrane] [Mus musculus] [EntityWithAccessionedSequence:9610566] Grin1 [transport vesicle membrane] [Mus musculus] |
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No pathways have been reviewed or authored by UniProt:P35438 Grin1 (96441)
