NMD3A_MOUSE
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 03-AUG-2022, entry version 124.
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}.
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; 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.ENSMUSP00000075970; -.
DR ChEMBL; CHEMBL3832634; -.
DR GlyConnect; 2354; 2 N-Linked glycans (1 site).
DR GlyGen; A2AIR5; 12 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q69Z52; -.
DR MaxQB; A2AIR5; -.
DR PRIDE; A2AIR5; -.
DR ProteomicsDB; 311940; -.
DR ProteomicsDB; 347316; -.
DR ABCD; A2AIR5; 1 sequenced antibody.
DR Antibodypedia; 54489; 29 antibodies from 10 providers.
DR Ensembl; ENSMUST00000076674; ENSMUSP00000075970; ENSMUSG00000039579. [A2AIR5-2]
DR Ensembl; ENSMUST00000093859; ENSMUSP00000091381; ENSMUSG00000039579. [A2AIR5-1]
DR GeneID; 242443; -.
DR KEGG; mmu:242443; -.
DR UCSC; uc033ica.1; mouse. [A2AIR5-1]
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; VGNSQHA; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; A2AIR5; -.
DR TreeFam; TF314731; -.
DR Reactome; R-MMU-9609736; Assembly and cell surface presentation of NMDA receptors.
DR BioGRID-ORCS; 242443; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Grin3a; mouse.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AIR5; protein.
DR Bgee; ENSMUSG00000039579; Expressed in pedal digit 2 phalanx and 128 other tissues.
DR ExpressionAtlas; A2AIR5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
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:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0016594; F:glycine binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
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:0004972; F:NMDA glutamate receptor activity; IMP:MGI.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated 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:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; ISO:MGI.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
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.
DR SUPFAM; SSF53822; SSF53822; 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
