Grin2c
entrez
24411
canonical
uniprot
Q00961
canonical
ensembl
ENSRNOG00000003280
resolver
ensp
ENSRNOP00000004477
resolver
enst
ENSRNOT00000004477
resolver
genesymbol
Grin2c
resolver
uniprot
A0A0G2JSH8
resolver
uniprot_entry
A0A0G2JSH8_RAT
resolver
uniprot_entry
NMDE3_RAT
resolver
amino_acid_sequence
MGGALGPALLLTSLLGAWARLGAGQGEQAVTVAVVFGSSGPLQTQARTRLTSQNFLDLPLEIQPLTVGVNNTNPSSILTQICGLLGAARVHGIVFEDNVDTEAVAQLLDFVSSQTHVPILSISGGSAVVLTPKEPGSAFLQLGVSLEQQLQVLFKVLEEYDWSAFAVITSLHPGHALFLEGVRAVADASYLSWRLLDVLTLELGPGGPRARTQRLLRQVDAPVLVAYCSREEAEVLFAEAAQAGLVGPGHVWLVPNLALGSTDAPPAAFPVGLISVVTESWRLSLRQKVRDGVAILALGAHSYRRQYGTLPAPAGDCRSHPGPVSPAREAFYRHLLNVTWEGRDFSFSPGGYLVRPTMVVIALNRHRLWEMVGRWDHGVLYMKYPVWPRYSTSLQPVVDSRHLTVATLEERPFVIVESPDPGTGGCVPNTVPCRRQSNHTFSSGDLTPYTKLCCKGFCIDILKKLAKVVKFSYDLYLVTNGKHGKRVRGVWNGMIGEVYYKRADMAIGSLTINEERSEIIDFSVPFVETGISVMVSRSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAITVFMFEYFSPVSYNQNLTKGKKPGGPSFTIGKSVWLLWALVFNNSVPIENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEQYIDTVSGLSDKKFQRPQDQYPPFRFGTVPNGSTERNIRSNYRDMHTHMVKFNQRSVEDALTSLKMGKLDAFIYDAAVLNYMAGKDEGCKLVTIGSGKVFATTGYGIAMQKDSHWKRAIDLALLQLLGDGETQKLETVWLSGICQNEKNEVMSSKLDIDNMAGVFYMLLVAMGLALLVFAWEHLVYWKLRHSVPNSSQLDFLLAFSRGIYSCFNGVQSLPSPARPPSPDLTADSAQANVLKMLQAARDMVNTADVSSSLDRATRTIENWGNNRRVPAPTASGPRSSTPGPPGQPSPSGWGPPGGGRTPLARRAPQPPARPATCGPPLPDVSRPSCRHASDARWPVRVGHQGPHVSASERRALPERSLLPAHCHYSSFPRAERSGRPYLPLFPEPPEPDDLPLLGPEQLARREAMLRAAWARGPRPRHASLPSSVAEAFTRSNPLPARCTGHACACPCPQSRPSCRHLAQAQSLRLPSYPEACVEGVPAGVATWQPRQHVCLHAHTRLPFCWGTVCRHPPPCTSHSPWLIGTWEPPAHRVRTLGLGTGYRDSGVLEEVSREACGTQGFPRSCTWRRVSSLESEV
uniprot
proteins
function
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:1350383, PubMed:8428958). Participates in synaptic plasticity for learning and memory formation by contributing to the slow phase of excitatory postsynaptic current and long-term synaptic potentiation (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:1350383, PubMed:28095420, PubMed:28126851, PubMed:8428958). NMDARs mediate simultaneously the potassium 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 (PubMed:1350383, PubMed:8428958, PubMed:9463421). {ECO:0000250|UniProtKB:P35438, ECO:0000250|UniProtKB:Q01098, ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:28095420, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:8428958, ECO:0000269|PubMed:9463421}.
uniprot
proteins
mass_dalton
135271
uniprot
proteins
mutagenesis
MUTAGEN 550; /note="P->R: Changed NMDA glutamate receptor activity characterized by increased glutamate and glycine potency."; /evidence="ECO:0000269|PubMed:28095420"; MUTAGEN 815; /note="M->V: Increased NMDA glutamate receptor activity characterized by increased glutamate and glycine potency."; /evidence="ECO:0000269|PubMed:28126851
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
protein_family
NR2C/GRIN2C subfamily
uniprot
proteins
pubmed
1350383
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
28095420
uniprot
proteins
pubmed
28126851
uniprot
proteins
pubmed
36959261
uniprot
proteins
pubmed
7569905
uniprot
proteins
pubmed
8428958
uniprot
proteins
pubmed
9463421
uniprot
proteins
pubmed
9647694
uniprot
proteins
sequence_length
1237
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:8428958}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14957}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q14957}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14957}.
uniprot
proteins
transmembrane_region
TRANSMEM 555..575; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q14957"; TRANSMEM 623..644; /note="Helical"; /evidence="ECO:0000269|PubMed:36959261, ECO:0007744|PDB:7YFI"; TRANSMEM 814..833; /note="Helical"; /evidence="ECO:0000269|PubMed:36959261, ECO:0007744|PDB:7YFI
uniprot
proteins