ID   NMD3B_RAT               Reviewed;        1002 AA.
AC   Q8VHN2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Glutamate receptor ionotropic, NMDA 3B;
DE            Short=GluN3B;
DE   AltName: Full=N-methyl-D-aspartate receptor subtype 3B;
DE            Short=NMDAR3B;
DE            Short=NR3B;
DE   Flags: Precursor;
GN   Name=Grin3b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11823786; DOI=10.1038/nature715;
RA   Chatterton J.E., Awobuluyi M., Premkumar L.S., Takahashi H., Talantova M.,
RA   Shin Y., Cui J., Tu S., Sevarino K.K.A., Nakanishi N., Tong G.,
RA   Lipton S.A., Zhang D.;
RT   "Excitatory glycine receptors containing the NR3 family of NMDA receptor
RT   subunits.";
RL   Nature 415:793-798(2002).
RN   [2]
RP   SEQUENCE REVISION.
RA   Chatterton J.E., Awobuluyi M., Cui J., Sevarino K.K.A., Lipton S.A.,
RA   Zhang D.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
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).
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 containing GRIN1 and GRIN2A (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}.
CC       Note=Requires the presence of GRIN1 to be targeted at the plasma
CC       membrane. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the hippocampus, the corpus callosum,
CC       in the facial and trigeminal nuclei of the brainstem and the ventral
CC       horn of the spinal cord. {ECO:0000269|PubMed:11735224,
CC       ECO:0000269|PubMed:11823786}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. NR3B/GRIN3B subfamily. {ECO:0000305}.
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DR   EMBL; AF440691; AAL69893.2; -; mRNA.
DR   RefSeq; NP_579842.2; NM_133308.2.
DR   PDB; 2RCA; X-ray; 1.58 A; A/B=413-560, A/B=676-815.
DR   PDB; 2RCB; X-ray; 1.62 A; A/B=413-560, A/B=676-815.
DR   PDBsum; 2RCA; -.
DR   PDBsum; 2RCB; -.
DR   AlphaFoldDB; Q8VHN2; -.
DR   SMR; Q8VHN2; -.
DR   STRING; 10116.ENSRNOP00000017064; -.
DR   BindingDB; Q8VHN2; -.
DR   ChEMBL; CHEMBL1907608; -.
DR   ChEMBL; CHEMBL2096669; -.
DR   ChEMBL; CHEMBL4524129; -.
DR   DrugCentral; Q8VHN2; -.
DR   GlyCosmos; Q8VHN2; 6 sites, No reported glycans.
DR   GlyGen; Q8VHN2; 6 sites.
DR   PhosphoSitePlus; Q8VHN2; -.
DR   PaxDb; 10116-ENSRNOP00000017064; -.
DR   GeneID; 170796; -.
DR   KEGG; rno:170796; -.
DR   UCSC; RGD:621705; rat.
DR   AGR; RGD:621705; -.
DR   CTD; 116444; -.
DR   RGD; 621705; Grin3b.
DR   eggNOG; KOG1053; Eukaryota.
DR   InParanoid; Q8VHN2; -.
DR   OrthoDB; 1034721at2759; -.
DR   PhylomeDB; Q8VHN2; -.
DR   EvolutionaryTrace; Q8VHN2; -.
DR   PRO; PR:Q8VHN2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IDA:RGD.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR   GO; GO:0005261; F:monoatomic cation channel activity; IDA:RGD.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IDA:RGD.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IEA:GOC.
DR   GO; GO:1905430; P:cellular response to glycine; IDA:RGD.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0051205; P:protein insertion into membrane; ISO:RGD.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd06377; PBP1_iGluR_NMDA_NR3; 1.
DR   CDD; cd13720; PBP2_iGluR_NMDA_Nr3; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF364; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3B; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Coiled coil; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1002
FT                   /note="Glutamate receptor ionotropic, NMDA 3B"
FT                   /id="PRO_0000011572"
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..1002
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          882..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..984
FT                   /note="Involved in the trafficking and surface expression
FT                   of NMDARs"
FT                   /evidence="ECO:0000250"
FT   COILED          944..985
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        892..910
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   STRAND          416..421
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   TURN            425..427
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          428..432
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          440..446
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           453..465
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           470..472
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          473..478
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           479..491
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          494..499
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           515..521
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          526..528
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           536..539
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          548..558
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           683..686
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           701..709
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           711..717
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          722..724
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           725..733
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          734..736
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          740..745
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           746..755
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          761..773
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   STRAND          776..778
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           784..796
FT                   /evidence="ECO:0007829|PDB:2RCA"
FT   HELIX           799..807
FT                   /evidence="ECO:0007829|PDB:2RCA"
SQ   SEQUENCE   1002 AA;  109158 MW;  4AC840EF97E0AB83 CRC64;
     MESVRTLWLS VALALAVGSR VVRGHPQPCR VPTRAGASVR LAALLPRAPA ARARVLAALA
     TPAPRLPHNL SLELVAVASP TRDPASLARG LCQVLAPPGV VASIAFPEAR PELRLLQFLA
     AATETPVVSV LRREVRTALG APTPFHLQLD WASPLETILD VLVSLVRAHA WEDIALVLCR
     VRDPGSLVTL WTNHASQAPK FVLDLSRLDS RNDSLRAGLA LLGALEGGGT PVPAAVLLGC
     STARAHEVLE AAPPGPQWLL GTPLPAEALP TTGLPPGVLA LGETEQHSLE AVVHDMVELV
     AQALSSMALV HPERALLPAV VNCDDLKTGG SEATGRTLAR FLGNTSFQGR TGAVWVTGSS
     QVHVSRHFKV WSLRRDPLGA PAWATVGSWQ DGQLDFQPGA AALRVPSPSG TQARPKLRVV
     TLVEHPFVFT RESDEDGQCP AGQLCLDPGT NDSARLDALF AALVNGSVPR 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 FSGLFVLLCL
     GLGSALLTSL GEHVFYRLVL PRIRRGNKLQ YWLHTSQKIH RALNTGPPEG QQERAEQERS
     GPKDELPATD GAGRWRRVRR AVERERRVRF LLEPGEAGGD RPWLCSNGPG LQAELRELEL
     RIEAARERLR SALLRRGELR ALLGDGTRLR PLRLLHAAPA ES
//