NMD3B_MOUSE
ID NMD3B_MOUSE Reviewed; 1003 AA.
AC Q91ZU9; Q8VHV0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3B;
DE Short=GluN3B;
DE AltName: Full=N-methyl-D-aspartate receptor subunit NR3B;
DE Short=NMDAR3B;
DE Short=NR3B;
DE AltName: Full=NMDA receptor 4;
DE Short=Nr4;
DE Flags: Precursor;
GN Name=Grin3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Spinal cord;
RX PubMed=11717388; DOI=10.1523/jneurosci.21-23-j0003.2001;
RA Nishi M., Hinds H., Lu H.-P., Kawata M., Hayashi Y.;
RT "Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate
RT receptor subunit that works in a dominant-negative manner.";
RL J. Neurosci. 21:RC185.1-RC185.6(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN2A OR GRIN2B.
RC STRAIN=ICR; TISSUE=Cerebellum;
RX PubMed=12008020; DOI=10.1016/s0169-328x(02)00173-0;
RA Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
RT "Cloning and characterization of a novel NMDA receptor subunit NR3B: a
RT dominant subunit that reduces calcium permeability.";
RL Brain Res. Mol. Brain Res. 100:43-52(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 360-900.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11735224; DOI=10.1006/geno.2001.6666;
RA Andersson O., Stenqvist A., Attersand A., von Euler G.;
RT "Nucleotide sequence, genomic organization, and chromosomal localization of
RT genes encoding the human NMDA receptor subunits NR3A and NR3B.";
RL Genomics 78:178-184(2001).
RN [4]
RP PROTEIN SEQUENCE OF 513-538 AND 631-643, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN2A OR GRIN2B.
RX PubMed=14602821; DOI=10.1523/jneurosci.23-31-10064.2003;
RA Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT "Specific assembly with the NMDA receptor 3B subunit controls surface
RT expression and calcium permeability of NMDA receptors.";
RL J. Neurosci. 23:10064-10073(2003).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC reduced single-channel conductance, low calcium permeability and low
CC voltage-dependent sensitivity to magnesium. Mediated by glycine.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B). Does not form functional homomeric channels. Found in a
CC complex with GRIN1 and GRIN2A or GRIN2B. {ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:14602821}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14602821};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14602821}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:14602821}. Note=Requires the presence
CC of GRIN1 to be targeted at the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in the facial nucleus and the ambiguus
CC nucleus of the brainstem, pons, medulla, spinal cord and cerebellum.
CC {ECO:0000269|PubMed:11717388, ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:14602821}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR3B/GRIN3B subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF396649; AAL10018.1; -; mRNA.
DR EMBL; AY062435; AAL38983.1; -; mRNA.
DR EMBL; AF373861; AAL40418.1; -; mRNA.
DR CCDS; CCDS24001.1; -.
DR RefSeq; NP_569722.1; NM_130455.2.
DR AlphaFoldDB; Q91ZU9; -.
DR SMR; Q91ZU9; -.
DR CORUM; Q91ZU9; -.
DR STRING; 10090.ENSMUSP00000048576; -.
DR ChEMBL; CHEMBL3832634; -.
DR GlyGen; Q91ZU9; 6 sites.
DR iPTMnet; Q91ZU9; -.
DR PhosphoSitePlus; Q91ZU9; -.
DR jPOST; Q91ZU9; -.
DR PaxDb; Q91ZU9; -.
DR PRIDE; Q91ZU9; -.
DR ProteomicsDB; 293689; -.
DR Antibodypedia; 10301; 165 antibodies from 26 providers.
DR DNASU; 170483; -.
DR Ensembl; ENSMUST00000045085; ENSMUSP00000048576; ENSMUSG00000035745.
DR GeneID; 170483; -.
DR KEGG; mmu:170483; -.
DR UCSC; uc007gau.1; mouse.
DR CTD; 116444; -.
DR MGI; MGI:2150393; Grin3b.
DR VEuPathDB; HostDB:ENSMUSG00000035745; -.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000161021; -.
DR HOGENOM; CLU_002039_0_1_1; -.
DR InParanoid; Q91ZU9; -.
DR OMA; GSWRDGQ; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q91ZU9; -.
DR TreeFam; TF314731; -.
DR BioGRID-ORCS; 170483; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Grin3b; mouse.
DR PRO; PR:Q91ZU9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91ZU9; protein.
DR Bgee; ENSMUSG00000035745; Expressed in lumbar subsegment of spinal cord and 64 other tissues.
DR ExpressionAtlas; Q91ZU9; baseline and differential.
DR Genevisible; Q91ZU9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:0016594; F:glycine binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0051205; P:protein insertion into membrane; IMP:UniProtKB.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:UniProtKB.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Coiled coil; Direct protein sequencing;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1003
FT /note="Glutamate receptor ionotropic, NMDA 3B"
FT /id="PRO_0000011571"
FT TOPO_DOM 25..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..1003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 883..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..985
FT /note="Involved in the trafficking and surface expression
FT of NMDARs"
FT COILED 947..986
FT /evidence="ECO:0000255"
FT COMPBIAS 896..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 674
FT /note="F -> S (in Ref. 3; AAL40418)"
FT /evidence="ECO:0000305"
FT CONFLICT 700..701
FT /note="SS -> GN (in Ref. 3; AAL40418)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="G -> D (in Ref. 3; AAL40418)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="S -> R (in Ref. 3; AAL40418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 109158 MW; 911CBF784E8B7A16 CRC64;
MECVQTLWLS LALALARGSW VVRGHPQPCG VPTRAGASVR LAALLPRAPA ARARVLAALA
TPSPRLPHNL SLELVAVASP TRDPASLARG LCQVLAPPGV VASITFPEAR PELRLLQFLA
AATETPVLSV LRREVRAPLG APTPFHLQLD WASPLETILD VLVSLVRAHA WEDIALVLCR
VRDPSGLVTL WTSRASQAPK FVLDLSQLDS GNDSLRATLA LLGTLEGGGT PVSAAVLLGC
STAHAHEVLE AAPPGPQWLL GTPLPAEALP KTGLPPGVLV LGETGQPSLE AAVHDMVELV
ARALSSMALM HPERALLPAA VNCEDLKTGG SESTARTLAR FLSNTSFQGR TGAVWVAGSS
QVHVSRHFKV WSLRRDPLGA PAWATVGSWQ DGQLDFQPGA AALRVPSPSG TQARPKLRVV
TLVEHPFVFT RESDEDGQCP AGQLCLDPGT NDSARLDALF TALENGSVPR TLRRCCYGYC
IDLLERLAED LAFDFELYIV GDGKYGALRD GRWTGLVGDL LAGRAHMAVT SFSINSARSQ
VVDFTSPFFS TSLGIMVRTR DTASPIGAFM WPLHWSMWVG VFAALHLTAL FLTLYEWRSP
YGLTPRGRNR GTVFSYSSAL NLCYAILFGR TVSSKTPKCP TGRFLMNLWA IFCLLVLSSY
TANLAAVMVG DKTFEELSGI HDPKLHHPSQ GFRFGTVWES SAEAYIKASF PEMHAHMRRH
SAPTTPHGVA MLTSDPPKLN AFIMDKSLLD YEVSIDADCK LLTVGKPFAI EGYGIGLPQN
SPLTSNLSEF ISRYKSSGFI DLLHDKWYKM VPCGKRVFAV TETLQMGVYH LSGLFVLLCL
GLGSALLTSL GEHVFYRLVL PRIRRGNKLQ YWLHTSQKIH RALNTGPPEG QQERAEQECS
GPKEEQPAAD GAGRWRRVRR AVVERERRVR FLLEPGEAGG DHPWLCSNGP GVQAELRELE
LRIEAARERL RSALLRRGEL RAQLGDGTRL RPLRLLHAAP AES
