GENTAUR Molecular Products.

 NMDE3_RAT               Reviewed;        1237 AA.
 Q00961;
 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
 01-JUN-1994, sequence version 1.
 12-SEP-2018, entry version 155.
 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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 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:0005622; C:intracellular; IEA:GOC.
 GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:RGD.
 GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 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.
 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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