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Protein

Glutamate receptor ionotropic, NMDA 2C

Gene

Grin2c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei612 – 6121Functional determinant of NMDA receptorsBy similarity

GO - Molecular functioni

  • cation channel activity Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • ionotropic glutamate receptor activity Source: RGD
  • NMDA glutamate receptor activity Source: RGD
  • PDZ domain binding Source: RGD
  • protein N-terminus binding Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2C
Short name:
GluN2C
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-3
N-methyl D-aspartate receptor subtype 2C
Short name:
NMDAR2C
Short name:
NR2C
Gene namesi
Name:Grin2c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2739. Grin2c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 553534ExtracellularSequence analysisAdd
BLAST
Transmembranei554 – 57421HelicalSequence analysisAdd
BLAST
Topological domaini575 – 62652CytoplasmicSequence analysisAdd
BLAST
Transmembranei627 – 64721HelicalSequence analysisAdd
BLAST
Topological domaini648 – 814167ExtracellularSequence analysisAdd
BLAST
Transmembranei815 – 83521HelicalSequence analysisAdd
BLAST
Topological domaini836 – 1237402CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • NMDA selective glutamate receptor complex Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096669.
GuidetoPHARMACOLOGYi458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 12371218Glutamate receptor ionotropic, NMDA 2CPRO_0000011582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence analysis
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence analysis
Modified residuei875 – 8751PhosphoserineBy similarity
Modified residuei881 – 8811PhosphoserineBy similarity
Modified residuei912 – 9121PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ00961.
PRIDEiQ00961.

PTM databases

iPTMnetiQ00961.
PhosphoSiteiQ00961.

Interactioni

Subunit structurei

Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Interacts with PDZ domains of INADL and DLG4. 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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
InadlQ63ZW72EBI-631045,EBI-8366894From a different organism.

GO - Molecular functioni

  • PDZ domain binding Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi246576. 1 interaction.
IntActiQ00961. 5 interactions.
MINTiMINT-87425.
STRINGi10116.ENSRNOP00000004477.

Chemistry

BindingDBiQ00961.

Structurei

3D structure databases

ProteinModelPortaliQ00961.
SMRiQ00961. Positions 401-799.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1235 – 12373PDZ-binding

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOVERGENiHBG052636.
InParanoidiQ00961.
KOiK05211.
OrthoDBiEOG72ZCD1.
PhylomeDBiQ00961.
TreeFamiTF314731.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q00961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGALGPALL LTSLLGAWAR LGAGQGEQAV TVAVVFGSSG PLQTQARTRL
60 70 80 90 100
TSQNFLDLPL EIQPLTVGVN 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
GYLVRPTMVV IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS
410 420 430 440 450
RHLTVATLEE RPFVIVESPD PGTGGCVPNT VPCRRQSNHT FSSGDLTPYT
460 470 480 490 500
KLCCKGFCID ILKKLAKVVK FSYDLYLVTN GKHGKRVRGV WNGMIGEVYY
510 520 530 540 550
KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVSRSNG TVSPSAFLEP
560 570 580 590 600
YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KPGGPSFTIG
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 RAIDLALLQL LGDGETQKLE TVWLSGICQN
810 820 830 840 850
EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY WKLRHSVPNS
860 870 880 890 900
SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTADSAQ ANVLKMLQAA
910 920 930 940 950
RDMVNTADVS SSLDRATRTI ENWGNNRRVP APTASGPRSS TPGPPGQPSP
960 970 980 990 1000
SGWGPPGGGR TPLARRAPQP PARPATCGPP LPDVSRPSCR HASDARWPVR
1010 1020 1030 1040 1050
VGHQGPHVSA SERRALPERS LLPAHCHYSS FPRAERSGRP YLPLFPEPPE
1060 1070 1080 1090 1100
PDDLPLLGPE QLARREAMLR AAWARGPRPR HASLPSSVAE AFTRSNPLPA
1110 1120 1130 1140 1150
RCTGHACACP CPQSRPSCRH LAQAQSLRLP SYPEACVEGV PAGVATWQPR
1160 1170 1180 1190 1200
QHVCLHAHTR LPFCWGTVCR HPPPCTSHSP WLIGTWEPPA HRVRTLGLGT
1210 1220 1230
GYRDSGVLEE VSREACGTQG FPRSCTWRRV SSLESEV
Length:1,237
Mass (Da):135,271
Last modified:June 1, 1994 - v1
Checksum:iB175993804B337A4
GO

Sequence cautioni

The sequence BAA02499.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91563 mRNA. Translation: AAA41713.1.
D13212 mRNA. Translation: BAA02499.1. Different initiation.
RefSeqiNP_036707.3. NM_012575.3.
XP_006247768.1. XM_006247706.2.
XP_006247769.1. XM_006247707.1.
XP_006247770.1. XM_006247708.2.
XP_006247771.1. XM_006247709.2.
UniGeneiRn.9709.

Genome annotation databases

GeneIDi24411.
KEGGirno:24411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91563 mRNA. Translation: AAA41713.1.
D13212 mRNA. Translation: BAA02499.1. Different initiation.
RefSeqiNP_036707.3. NM_012575.3.
XP_006247768.1. XM_006247706.2.
XP_006247769.1. XM_006247707.1.
XP_006247770.1. XM_006247708.2.
XP_006247771.1. XM_006247709.2.
UniGeneiRn.9709.

3D structure databases

ProteinModelPortaliQ00961.
SMRiQ00961. Positions 401-799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246576. 1 interaction.
IntActiQ00961. 5 interactions.
MINTiMINT-87425.
STRINGi10116.ENSRNOP00000004477.

Chemistry

BindingDBiQ00961.
ChEMBLiCHEMBL2096669.
GuidetoPHARMACOLOGYi458.

PTM databases

iPTMnetiQ00961.
PhosphoSiteiQ00961.

Proteomic databases

PaxDbiQ00961.
PRIDEiQ00961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24411.
KEGGirno:24411.

Organism-specific databases

CTDi2905.
RGDi2739. Grin2c.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOVERGENiHBG052636.
InParanoidiQ00961.
KOiK05211.
OrthoDBiEOG72ZCD1.
PhylomeDBiQ00961.
TreeFamiTF314731.

Miscellaneous databases

PROiQ00961.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Heteromeric NMDA receptors: molecular and functional distinction of subtypes."
    Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.
    Science 256:1217-1221(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Molecular characterization of the family of the N-methyl-D-aspartate receptor subunits."
    Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.
    J. Biol. Chem. 268:2836-2843(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95."
    Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.
    Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG4.
  4. "CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins."
    Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.
    Mol. Cell. Neurosci. 11:161-172(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INADL.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNMDE3_RAT
AccessioniPrimary (citable) accession number: Q00961
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.