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Glutamate receptor ionotropic, NMDA 2C (GluN2C) (Glutamate [NMDA] receptor subunit epsilon-3) (N-methyl D-aspartate receptor subtype 2C) (NMDAR2C) (NR2C)

 NMDE3_RAT               Reviewed;        1237 AA.
Q00961;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
05-DEC-2018, entry version 157.
RecName: Full=Glutamate receptor ionotropic, NMDA 2C;
Short=GluN2C;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-3;
AltName: Full=N-methyl D-aspartate receptor subtype 2C;
Short=NMDAR2C {ECO:0000303|PubMed:8428958};
Short=NR2C {ECO:0000303|PubMed:1350383};
Flags: Precursor;
Name=Grin2c;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1350383; DOI=10.1126/science.256.5060.1217;
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
Burnashev N., Sakmann B., Seeburg P.H.;
"Heteromeric NMDA receptors: molecular and functional distinction of
subtypes.";
Science 256:1217-1221(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=8428958;
Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H.,
Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
"Molecular characterization of the family of the N-methyl-D-aspartate
receptor subunits.";
J. Biol. Chem. 268:2836-2843(1993).
[3]
INTERACTION WITH DLG4.
PubMed=7569905; DOI=10.1126/science.7569905;
Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
"Domain interaction between NMDA receptor subunits and the
postsynaptic density protein PSD-95.";
Science 269:1737-1740(1995).
[4]
INTERACTION WITH PATJ.
PubMed=9647694; DOI=10.1006/mcne.1998.0679;
Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
"CIPP, a novel multivalent PDZ domain protein, selectively interacts
with Kir4.0 family members, NMDA receptor subunits, neurexins, and
neuroligins.";
Mol. Cell. Neurosci. 11:161-172(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF MET-815.
PubMed=28126851; DOI=10.1124/mol.116.106781;
Chen W., Tankovic A., Burger P.B., Kusumoto H., Traynelis S.F.,
Yuan H.;
"Functional evaluation of a de novo GRIN2A mutation identified in a
patient with profound global developmental delay and refractory
epilepsy.";
Mol. Pharmacol. 91:317-330(2017).
-!- 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+) (PubMed:1350383, PubMed:8428958,
PubMed:28126851). Sensitivity to glutamate and channel kinetics
depend on the subunit composition (Probable). Plays a role in
regulating the balance between excitatory and inhibitory activity
of pyramidal neurons in the prefrontal cortex. Contributes to the
slow phase of excitatory postsynaptic current, long-term synaptic
potentiation, and learning (By similarity).
{ECO:0000250|UniProtKB:Q01098, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:8428958,
ECO:0000305}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1350383,
PubMed:8428958, PubMed:28126851). In vivo, the subunit composition
may depend on the expression levels of the different subunits
(Probable). Interacts with PDZ domains of PATJ and DLG4
(PubMed:7569905, PubMed:9647694). Interacts (via PDZ-binding
motif) with SNX27 (via PDZ domain); the interaction is required
for recycling to the plasma membrane when endocytosed and prevent
degradation in lysosomes (By similarity).
{ECO:0000250|UniProtKB:Q14957, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:7569905,
ECO:0000269|PubMed:8428958, ECO:0000269|PubMed:9647694,
ECO:0000305}.
-!- INTERACTION:
Q63ZW7:Patj (xeno); NbExp=2; IntAct=EBI-631045, EBI-8366894;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:8428958}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q14957}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:Q14957}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q14957}.
-!- TISSUE SPECIFICITY: Detected in cerebellum.
{ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:8428958}.
-!- 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.
{ECO:0000250|UniProtKB:Q00960}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2C/GRIN2C subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA02499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M91563; AAA41713.1; -; mRNA.
EMBL; D13212; BAA02499.1; ALT_INIT; mRNA.
RefSeq; NP_036707.3; NM_012575.3.
RefSeq; XP_006247769.1; XM_006247707.2.
RefSeq; XP_006247771.1; XM_006247709.3.
RefSeq; XP_017452475.1; XM_017596986.1.
RefSeq; XP_017452476.1; XM_017596987.1.
RefSeq; XP_017452477.1; XM_017596988.1.
RefSeq; XP_017452478.1; XM_017596989.1.
RefSeq; XP_017452479.1; XM_017596990.1.
RefSeq; XP_017452480.1; XM_017596991.1.
RefSeq; XP_017452481.1; XM_017596992.1.
UniGene; Rn.9709; -.
ProteinModelPortal; Q00961; -.
BioGrid; 246576; 1.
ComplexPortal; CPX-287; NMDA receptor complex, GluN1-GluN2C.
IntAct; Q00961; 5.
MINT; Q00961; -.
STRING; 10116.ENSRNOP00000004477; -.
BindingDB; Q00961; -.
ChEMBL; CHEMBL401; -.
GuidetoPHARMACOLOGY; 458; -.
iPTMnet; Q00961; -.
PhosphoSitePlus; Q00961; -.
PaxDb; Q00961; -.
PRIDE; Q00961; -.
GeneID; 24411; -.
KEGG; rno:24411; -.
CTD; 2905; -.
RGD; 2739; Grin2c.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
HOVERGEN; HBG052636; -.
InParanoid; Q00961; -.
KO; K05211; -.
PhylomeDB; Q00961; -.
TreeFam; TF314731; -.
PRO; PR:Q00961; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
GO; GO:0005261; F:cation channel activity; IDA:RGD.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central.
GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR018884; NMDAR2_C.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
Pfam; PF10565; NMDAR2_C; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
Calcium; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Magnesium; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1237 Glutamate receptor ionotropic, NMDA 2C.
/FTId=PRO_0000011582.
TOPO_DOM 20 554 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 555 573 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 574 600 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
INTRAMEM 601 620 Discontinuously helical.
{ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 621 627 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 628 643 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 644 814 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 815 834 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 835 1237 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
REGION 509 511 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
REGION 601 620 Pore-forming.
{ECO:0000250|UniProtKB:Q00960}.
REGION 687 688 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
MOTIF 1235 1237 PDZ-binding.
BINDING 511 511 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 516 516 Glutamate.
{ECO:0000250|UniProtKB:Q00959}.
BINDING 729 729 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
SITE 612 612 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000250|UniProtKB:Q01098}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000250|UniProtKB:Q01098}.
MOD_RES 912 912 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 539 539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 82 317 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 426 453 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 433 454 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 743 798 {ECO:0000250|UniProtKB:Q00959}.
MUTAGEN 815 815 M->V: Increased glutamate and glycine
agonist potency.
{ECO:0000269|PubMed:28126851}.
SEQUENCE 1237 AA; 135271 MW; B175993804B337A4 CRC64;
MGGALGPALL LTSLLGAWAR LGAGQGEQAV TVAVVFGSSG PLQTQARTRL TSQNFLDLPL
EIQPLTVGVN NTNPSSILTQ ICGLLGAARV HGIVFEDNVD TEAVAQLLDF VSSQTHVPIL
SISGGSAVVL TPKEPGSAFL QLGVSLEQQL QVLFKVLEEY DWSAFAVITS LHPGHALFLE
GVRAVADASY LSWRLLDVLT LELGPGGPRA RTQRLLRQVD APVLVAYCSR EEAEVLFAEA
AQAGLVGPGH VWLVPNLALG STDAPPAAFP VGLISVVTES WRLSLRQKVR DGVAILALGA
HSYRRQYGTL PAPAGDCRSH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG GYLVRPTMVV
IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS RHLTVATLEE RPFVIVESPD
PGTGGCVPNT VPCRRQSNHT FSSGDLTPYT KLCCKGFCID ILKKLAKVVK FSYDLYLVTN
GKHGKRVRGV WNGMIGEVYY KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVSRSNG
TVSPSAFLEP YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KPGGPSFTIG
KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF MIQEQYIDTV
SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH THMVKFNQRS VEDALTSLKM
GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IAMQKDSHWK RAIDLALLQL
LGDGETQKLE TVWLSGICQN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY
WKLRHSVPNS SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTADSAQ ANVLKMLQAA
RDMVNTADVS SSLDRATRTI ENWGNNRRVP APTASGPRSS TPGPPGQPSP SGWGPPGGGR
TPLARRAPQP PARPATCGPP LPDVSRPSCR HASDARWPVR VGHQGPHVSA SERRALPERS
LLPAHCHYSS FPRAERSGRP YLPLFPEPPE PDDLPLLGPE QLARREAMLR AAWARGPRPR
HASLPSSVAE AFTRSNPLPA RCTGHACACP CPQSRPSCRH LAQAQSLRLP SYPEACVEGV
PAGVATWQPR QHVCLHAHTR LPFCWGTVCR HPPPCTSHSP WLIGTWEPPA HRVRTLGLGT
GYRDSGVLEE VSREACGTQG FPRSCTWRRV SSLESEV


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