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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_MOUSE             Reviewed;        1239 AA.
Q01098;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
28-MAR-2018, entry version 162.
RecName: Full=Glutamate receptor ionotropic, NMDA 2C;
Short=GluN2C;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-3 {ECO:0000303|PubMed:1377365};
AltName: Full=N-methyl D-aspartate receptor subtype 2C;
Short=NMDAR2C;
Short=NR2C {ECO:0000303|PubMed:8987814};
Flags: Precursor;
Name=Grin2c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND TISSUE SPECIFICITY.
PubMed=1377365; DOI=10.1038/358036a0;
Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
"Molecular diversity of the NMDA receptor channel.";
Nature 358:36-41(1992).
[2]
SEQUENCE REVISION.
Kashiwabuchi N.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[3]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8987814;
Kadotani H., Hirano T., Masugi M., Nakamura K., Nakao K., Katsuki M.,
Nakanishi S.;
"Motor discoordination results from combined gene disruption of the
NMDA receptor NR2A and NR2C subunits, but not from single disruption
of the NR2A or NR2C subunit.";
J. Neurosci. 16:7859-7867(1996).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-881, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=27922130; DOI=10.1038/srep38321;
Gupta S.C., Ravikrishnan A., Liu J., Mao Z., Pavuluri R.,
Hillman B.G., Gandhi P.J., Stairs D.J., Li M., Ugale R.R.,
Monaghan D.T., Dravid S.M.;
"The NMDA receptor GluN2C subunit controls cortical excitatory-
inhibitory balance, neuronal oscillations and cognitive function.";
Sci. Rep. 6:38321-38321(2016).
-!- 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:1377365). Sensitivity to glutamate
and channel kinetics depend on the subunit composition
(PubMed:1377365). Plays a role in regulating the balance between
excitatory and inhibitory activity of pyramidal neurons in the
prefrontal cortex (PubMed:27922130). Contributes to the slow phase
of excitatory postsynaptic current, long-term synaptic
potentiation, and learning (PubMed:8987814).
{ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:27922130,
ECO:0000269|PubMed:8987814}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1377365). Can also
form heterotetrameric channels that contain at least one zeta
subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or
GRIN3B (By similarity). In vivo, the subunit composition may
depend on the expression levels of the different subunits
(Probable). Interacts with PDZ domains of PATJ and DLG4 (By
similarity). 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:Q00961,
ECO:0000250|UniProtKB:Q14957, ECO:0000269|PubMed:1377365,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1377365};
Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse,
postsynaptic cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level)
(PubMed:8987814). Detected in the granule cell layer of the
cerebellum (PubMed:1377365). {ECO:0000269|PubMed:1377365,
ECO:0000269|PubMed:8987814}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mutant mice appear grossly normal
(PubMed:8987814). Mossy fiber granule cells from mutant mice
present a decrease of the slow component of the excitatory
postsynaptic current (PubMed:8987814). Pyramidal neurons in the
prefrontal cortex display a reduced dendritic spine density
(PubMed:27922130). Besides, the prefrontal cortex has an altered
pattern of excitatory and inhibitory synapses (PubMed:27922130).
Pyramidal neurons in the prefrontal cortex display a reduced
frequency of miniature excitatory postsynaptic currents (mEPSC),
together with an increased frequency of miniature inhibitory
postsynaptic currents (mIPSC), indicative of a shift in the
balance between excitatory and inhibitory membrane currents
(PubMed:27922130). The slow component of the excitatory
postsynaptic current is nearly abolished in mossy fiber cells from
mice lacking both Grin2a and Grin2c (PubMed:8987814). Mice lacking
both Grin2a and Grin2c display subtle motor deficits; they have no
visible phenotype when performing simple tasks, but have decreased
ability to walk across a narrow wooden bar, and are unable to stay
on a rapidly rotating rod (PubMed:8987814).
{ECO:0000269|PubMed:27922130, ECO:0000269|PubMed:8987814}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2C/GRIN2C subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D10694; BAA01536.1; -; mRNA.
CCDS; CCDS25624.1; -.
PIR; I49705; I49705.
RefSeq; NP_034480.2; NM_010350.2.
UniGene; Mm.39090; -.
ProteinModelPortal; Q01098; -.
BioGrid; 200070; 6.
IntAct; Q01098; 2.
MINT; Q01098; -.
STRING; 10090.ENSMUSP00000003351; -.
ChEMBL; CHEMBL3832634; -.
iPTMnet; Q01098; -.
PhosphoSitePlus; Q01098; -.
PaxDb; Q01098; -.
PRIDE; Q01098; -.
Ensembl; ENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734.
Ensembl; ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734.
GeneID; 14813; -.
KEGG; mmu:14813; -.
UCSC; uc007mgx.1; mouse.
CTD; 2905; -.
MGI; MGI:95822; Grin2c.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00910000143978; -.
HOGENOM; HOG000231061; -.
HOVERGEN; HBG052636; -.
InParanoid; Q01098; -.
KO; K05211; -.
OMA; REACQEG; -.
OrthoDB; EOG091G09KH; -.
PhylomeDB; Q01098; -.
TreeFam; TF314731; -.
Reactome; R-MMU-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-MMU-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-MMU-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
PRO; PR:Q01098; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020734; -.
ExpressionAtlas; Q01098; baseline and differential.
Genevisible; Q01098; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IPI:MGI.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005261; F:cation channel activity; IMP:MGI.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
GO; GO:0004972; F:NMDA glutamate receptor activity; IMP:MGI.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
GO; GO:0033058; P:directional locomotion; IGI:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IGI:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:1903539; P:protein localization to postsynaptic membrane; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0009611; P:response to wounding; IGI:MGI.
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 1239 Glutamate receptor ionotropic, NMDA 2C.
/FTId=PRO_0000011581.
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 1239 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 1237 1239 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:Q00959}.
SITE 612 612 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 912 912 Phosphoserine.
{ECO:0000250|UniProtKB:Q00961}.
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}.
SEQUENCE 1239 AA; 135420 MW; 793E8E731E20C3C9 CRC64;
MGGALGPALL LTSLLGAWAG LGAGQGEQAV TVAVVFGSSG PLQAQARTRL TPQNFLDLPL
EIQPLTIGVN 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 GYLVQPTMVV
IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS RHLTVATLEE RPFVIVESPD
PGTGGCVPNT VPCRRQSNHT FSSGDITPYT KLCCKGFCID ILKKLAKVVK FSYDLYLVTN
GKHGKRVRGV WNGMIGEVYY KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVARSNG
TVSPSAFLEP YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KSGGPSFTIG
KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF MIQEQYIDTV
SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH THMVKFNQRS VEDALTSLKM
GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IAMQKDSHWK RAIDLALLQF
LGDGETQKLE TVWLSGICHN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY
WKLRHSVPSS SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTAGSAQ ANVLKMLQAA
RDMVSTADVS GSLDRATRTI ENWGNNRRAP APTTSGPRSC TPGPPGQPSP SGWRPPGGGR
TPLARRAPQP PARPATCAGS PQPDVSRASC RHAWDARWPV RVGHQGSHLS ASERRALPER
SLLHAHCHYS SFPRAERSGR PFLPLFPEPP EPDDLPLLGP EQLARREALL RAAWARGPRP
RHASLPSSVA EAFTRSNPLP ARCTGHACAC PCPQSRPSCR HVAQTQSLRL PSYREACVEG
VPAGVAATWQ PRQHVCLHTH THLPFCWGTV CRHPPPCSSH SPWLIGTWEP PSHRGRTLGL
GTGYRDSGVL EEVSREACGT QGFPRSCTWR RISSLESEV


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