ID   NMD3A_MOUSE             Reviewed;        1135 AA.
AC   A2AIR5; A2AIR4; Q69Z52;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Glutamate receptor ionotropic, NMDA 3A;
DE            Short=GluN3A;
DE   AltName: Full=N-methyl-D-aspartate receptor;
DE   AltName: Full=N-methyl-D-aspartate receptor subtype 3A;
DE            Short=NMDAR3A;
DE            Short=NR3A;
DE   AltName: Full=NMDAR-L;
DE   Flags: Precursor;
GN   Name=Grin3a; Synonyms=Kiaa1973;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-1135 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH GIT1, AND TISSUE SPECIFICITY.
RX   PubMed=24297929; DOI=10.1073/pnas.1312211110;
RA   Fiuza M., Gonzalez-Gonzalez I., Perez-Otano I.;
RT   "GluN3A expression restricts spine maturation via inhibition of GIT1/Rac1
RT   signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20807-20812(2013).
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. During
CC       the development of neural circuits, plays a role in the synaptic
CC       refinement period, restricting spine maturation and growth (By
CC       similarity). By competing with GIT1 interaction with ARHGEF7/beta-PIX,
CC       may reduce GIT1/ARHGEF7-regulated local activation of RAC1, hence
CC       affecting signaling and limiting the maturation and growth of inactive
CC       synapses (PubMed:24297929). May also play a role in PPP2CB-NMDAR
CC       mediated signaling mechanism (By similarity).
CC       {ECO:0000250|UniProtKB:Q9R1M7, ECO:0000269|PubMed:24297929}.
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, GRIN2A or GRIN2B and PPP2CB. Probably interacts
CC       with PPP2CB. No complex with PPP2CB is detected when NMDARs are
CC       stimulated by NMDA (By similarity). Interacts (via C-terminus) with
CC       GIT1, but not with GRIA1/GluA1, nor with synaptophysin/SYP; this
CC       interaction competes with GIT1 interaction with ARHGEF7/beta-PIX
CC       (PubMed:24297929). {ECO:0000250|UniProtKB:Q9R1M7,
CC       ECO:0000269|PubMed:24297929}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1M7};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R1M7}.
CC       Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic
CC       density {ECO:0000250|UniProtKB:Q9R1M7}. Note=Enriched in postsynaptic
CC       plasma membrane and postsynaptic densities. Requires the presence of
CC       GRIN1 to be targeted at the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q9R1M7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AIR5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AIR5-2; Sequence=VSP_061048;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC       {ECO:0000269|PubMed:24297929}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. NR3A/GRIN3A subfamily. {ECO:0000305}.
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DR   EMBL; AL732521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173314; BAD32592.1; -; mRNA.
DR   CCDS; CCDS51175.1; -. [A2AIR5-2]
DR   CCDS; CCDS71385.1; -. [A2AIR5-1]
DR   RefSeq; NP_001028523.1; NM_001033351.2. [A2AIR5-2]
DR   RefSeq; NP_001263284.1; NM_001276355.1. [A2AIR5-1]
DR   AlphaFoldDB; A2AIR5; -.
DR   SMR; A2AIR5; -.
DR   STRING; 10090.ENSMUSP00000091381; -.
DR   ChEMBL; CHEMBL3832634; -.
DR   GlyConnect; 2354; 2 N-Linked glycans (1 site).
DR   GlyCosmos; A2AIR5; 12 sites, 2 glycans.
DR   GlyGen; A2AIR5; 12 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; A2AIR5; -.
DR   PhosphoSitePlus; A2AIR5; -.
DR   MaxQB; A2AIR5; -.
DR   PaxDb; 10090-ENSMUSP00000075970; -.
DR   ProteomicsDB; 311940; -.
DR   ProteomicsDB; 347316; -.
DR   ABCD; A2AIR5; 1 sequenced antibody.
DR   Antibodypedia; 54489; 42 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000076674.4; ENSMUSP00000075970.4; ENSMUSG00000039579.16. [A2AIR5-2]
DR   Ensembl; ENSMUST00000093859.11; ENSMUSP00000091381.5; ENSMUSG00000039579.16. [A2AIR5-1]
DR   GeneID; 242443; -.
DR   KEGG; mmu:242443; -.
DR   UCSC; uc033ica.1; mouse. [A2AIR5-1]
DR   AGR; MGI:1933206; -.
DR   CTD; 116443; -.
DR   MGI; MGI:1933206; Grin3a.
DR   VEuPathDB; HostDB:ENSMUSG00000039579; -.
DR   eggNOG; KOG1053; Eukaryota.
DR   GeneTree; ENSGT00940000158571; -.
DR   HOGENOM; CLU_002039_0_0_1; -.
DR   InParanoid; A2AIR5; -.
DR   OMA; TIVMFGC; -.
DR   OrthoDB; 1034721at2759; -.
DR   PhylomeDB; A2AIR5; -.
DR   TreeFam; TF314731; -.
DR   Reactome; R-MMU-9609736; Assembly and cell surface presentation of NMDA receptors.
DR   BioGRID-ORCS; 242443; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Grin3a; mouse.
DR   PRO; PR:A2AIR5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2AIR5; Protein.
DR   Bgee; ENSMUSG00000039579; Expressed in pedal digit 2 phalanx and 129 other cell types or tissues.
DR   ExpressionAtlas; A2AIR5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR   GO; GO:0004970; F:glutamate-gated receptor activity; ISO:MGI.
DR   GO; GO:0016594; F:glycine binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; IMP:MGI.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0048511; P:rhythmic process; ISO:MGI.
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:SF397; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 3A; 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   Alternative splicing; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1135
FT                   /note="Glutamate receptor ionotropic, NMDA 3A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5027148248"
FT   TOPO_DOM        27..674
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        696..748
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        749..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        770..930
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        952..1135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          59..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..987
FT                   /note="PPP2CB binding site"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1M7"
FT   REGION          1082..1115
FT                   /note="GIT1-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R1M7"
FT   COILED          1085..1119
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        549
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        886
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1003..1022
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061048"
SQ   SEQUENCE   1135 AA;  127542 MW;  71DBEF3EDFFA2A7E CRC64;
     MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
     APRAASRAQD GGRAGAQRDE PESGTWRPPA PSQGARWLGS ALHGRGPPGS RKLGEGAGTE
     TLWPRDALLF AVENLNRVEG LLPYNLSLEV VMAIEAGLGD LPLMPFSSPS SPWSSDPFSF
     LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSSVLHIPV LSIVRHEFPR ESQNPLHLQL
     SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTENNSKFH LESIINITAN
     LSSTKDLLSF LQVQLENIRN STPTMVMFGC DMGSIRQIFE MSTQFGLSPP DLHWVLGDSQ
     NVEELRTEGL PLGLIAHGKT TQSVFEYYVQ DAMELVARAV ATATMIQPEL ALLPSTMNCM
     DVKTTNLTSG QYLSRFLANT TFRGLSGSIK VKGSTIVSSE NNFFIWNLQY DPMGKPMWTR
     LGSWQGGRIV MDSGIWPEQA QRHKTHFHHP NKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
     QLCLDPMTND SSILDSLFSS LHSSNDTVPI KFKKCCYGYC IDLLEQLAED MNFDFDLYIV
     GDGKYGAWKN GHWTGLVGDL LSGTANMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
     DTAAPIGAFM WPLHWTMWLG IFVALHITAI FLTLYEWKSP FGMTPKGRNR NKVFSFSSAL
     NVCYALLFGR TAAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
     HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVQ YLKNDPEKLD
     AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTSNISEL ISQYKSHGFM
     DVLHDKWYKV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVYRLLL
     PRIKNKSKLQ YWLHTSQRFH RALNTSFVEE KQPCSKTKRV EKSRWRRWTC KTEGDSELSL
     FPRSNMGPQQ LMVWNTSNLS HDNQRKYIFN DEEGQNQLGT QTHQDIPLPP RRRELPASLT
     TNGKADSLNV ARNSVMQELS ELEKQIQVIR QELQLAVSRK TELEEYQRTN RTCES
//