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Protein

Glutamate receptor ionotropic, NMDA 2C

Gene

Grin2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Mg2+ (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).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei511GlutamateBy similarity1
Binding sitei516GlutamateBy similarity1
Sitei612Functional determinant of NMDA receptorsBy similarity1
Binding sitei729GlutamateBy similarity1

GO - Molecular functioni

  • cation channel activity Source: MGI
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glutamate-gated calcium ion channel activity Source: UniProtKB
  • NMDA glutamate receptor activity Source: MGI

GO - Biological processi

  • calcium ion transmembrane import into cytosol Source: UniProtKB
  • directional locomotion Source: MGI
  • excitatory postsynaptic potential Source: MGI
  • negative regulation of protein catabolic process Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • protein localization Source: MGI
  • regulation of membrane potential Source: MGI
  • response to wounding Source: MGI

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium

Enzyme and pathway databases

ReactomeiR-MMU-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-8849932. Synaptic adhesion-like molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2C
Short name:
GluN2C
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-31 Publication
N-methyl D-aspartate receptor subtype 2C
Short name:
NMDAR2C
Short name:
NR2C1 Publication
Gene namesi
Name:Grin2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95822. Grin2c.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 554ExtracellularBy similarityAdd BLAST535
Transmembranei555 – 573HelicalBy similarityAdd BLAST19
Topological domaini574 – 600CytoplasmicBy similarityAdd BLAST27
Intramembranei601 – 620Discontinuously helicalBy similarityAdd BLAST20
Topological domaini621 – 627CytoplasmicBy similarity7
Transmembranei628 – 643HelicalBy similarityAdd BLAST16
Topological domaini644 – 814ExtracellularBy similarityAdd BLAST171
Transmembranei815 – 834HelicalBy similarityAdd BLAST20
Topological domaini835 – 1239CytoplasmicBy similarityAdd BLAST405

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

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).2 Publications

Chemistry databases

ChEMBLiCHEMBL3832634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001158120 – 1239Glutamate receptor ionotropic, NMDA 2CAdd BLAST1220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi70N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi82 ↔ 317By similarity
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi426 ↔ 453By similarity
Disulfide bondi433 ↔ 454By similarity
Glycosylationi438N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi539N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi743 ↔ 798By similarity
Modified residuei875PhosphoserineCombined sources1
Modified residuei881PhosphoserineCombined sources1
Modified residuei912PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ01098.
PRIDEiQ01098.

PTM databases

iPTMnetiQ01098.
PhosphoSitePlusiQ01098.

Expressioni

Tissue specificityi

Detected in cerebellum (at protein level) (PubMed:8987814). Detected in the granule cell layer of the cerebellum (PubMed:1377365).2 Publications

Gene expression databases

BgeeiENSMUSG00000020734.
ExpressionAtlasiQ01098. baseline and differential.
GenevisibleiQ01098. MM.

Interactioni

Subunit structurei

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).By similarityCurated1 Publication

Protein-protein interaction databases

BioGridi200070. 6 interactors.
IntActiQ01098. 1 interactor.
MINTiMINT-104161.
STRINGi10090.ENSMUSP00000003351.

Structurei

3D structure databases

ProteinModelPortaliQ01098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni509 – 511Glutamate bindingBy similarity3
Regioni601 – 620Pore-formingBy similarityAdd BLAST20
Regioni687 – 688Glutamate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1237 – 1239PDZ-binding3

Domaini

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.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000231061.
HOVERGENiHBG052636.
InParanoidiQ01098.
KOiK05211.
OMAiSAILYMM.
OrthoDBiEOG091G09KH.
PhylomeDBiQ01098.
TreeFamiTF314731.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGALGPALL LTSLLGAWAG LGAGQGEQAV TVAVVFGSSG PLQAQARTRL
60 70 80 90 100
TPQNFLDLPL EIQPLTIGVN NTNPSSILTQ ICGLLGAARV HGIVFEDNVD
110 120 130 140 150
TEAVAQLLDF VSSQTHVPIL SISGGSAVVL TPKEPGSAFL QLGVSLEQQL
160 170 180 190 200
QVLFKVLEEY DWSAFAVITS LHPGHALFLE GVRAVADASY LSWRLLDVLT
210 220 230 240 250
LELGPGGPRA RTQRLLRQVD APVLVAYCSR EEAEVLFAEA AQAGLVGPGH
260 270 280 290 300
VWLVPNLALG STDAPPAAFP VGLISVVTES WRLSLRQKVR DGVAILALGA
310 320 330 340 350
HSYRRQYGTL PAPAGDCRSH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG
360 370 380 390 400
GYLVQPTMVV IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS
410 420 430 440 450
RHLTVATLEE RPFVIVESPD PGTGGCVPNT VPCRRQSNHT FSSGDITPYT
460 470 480 490 500
KLCCKGFCID ILKKLAKVVK FSYDLYLVTN GKHGKRVRGV WNGMIGEVYY
510 520 530 540 550
KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVARSNG TVSPSAFLEP
560 570 580 590 600
YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KSGGPSFTIG
610 620 630 640 650
KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF
660 670 680 690 700
MIQEQYIDTV SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH
710 720 730 740 750
THMVKFNQRS VEDALTSLKM GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS
760 770 780 790 800
GKVFATTGYG IAMQKDSHWK RAIDLALLQF LGDGETQKLE TVWLSGICHN
810 820 830 840 850
EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY WKLRHSVPSS
860 870 880 890 900
SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTAGSAQ ANVLKMLQAA
910 920 930 940 950
RDMVSTADVS GSLDRATRTI ENWGNNRRAP APTTSGPRSC TPGPPGQPSP
960 970 980 990 1000
SGWRPPGGGR TPLARRAPQP PARPATCAGS PQPDVSRASC RHAWDARWPV
1010 1020 1030 1040 1050
RVGHQGSHLS ASERRALPER SLLHAHCHYS SFPRAERSGR PFLPLFPEPP
1060 1070 1080 1090 1100
EPDDLPLLGP EQLARREALL RAAWARGPRP RHASLPSSVA EAFTRSNPLP
1110 1120 1130 1140 1150
ARCTGHACAC PCPQSRPSCR HVAQTQSLRL PSYREACVEG VPAGVAATWQ
1160 1170 1180 1190 1200
PRQHVCLHTH THLPFCWGTV CRHPPPCSSH SPWLIGTWEP PSHRGRTLGL
1210 1220 1230
GTGYRDSGVL EEVSREACGT QGFPRSCTWR RISSLESEV
Length:1,239
Mass (Da):135,420
Last modified:February 1, 1996 - v2
Checksum:i793E8E731E20C3C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10694 mRNA. Translation: BAA01536.1.
CCDSiCCDS25624.1.
PIRiI49705.
RefSeqiNP_034480.2. NM_010350.2.
UniGeneiMm.39090.

Genome annotation databases

EnsembliENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734.
ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734.
GeneIDi14813.
KEGGimmu:14813.
UCSCiuc007mgx.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiNMDE3_MOUSE
AccessioniPrimary (citable) accession number: Q01098
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: November 22, 2017
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families