Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9R1M7 (NMD3A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, NMDA 3A

Short name=GluN3A
Alternative name(s):
Glutamate receptor chi-1
N-methyl-D-aspartate receptor
N-methyl-D-aspartate receptor subtype 3A
Short name=NMDAR3A
Short name=NR3A
NMDAR-L
NMDAR-L1
Gene names
Name:Grin3a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. May play a role in the development of dendritic spines. May also play a role in PPP2CB-NMDAR mediated signaling mechanism.

Subunit structure

Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A or GRIN3B). Does not form functional homomeric channels. Found in a complex with GRIN1, GRIN2A or GRIN2B and PPP2CB. Probably interacts with PPP2CB. No complex with PPP2CB is detected when NMDARs are stimulated by NMDA. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Note: Enriched in postsynaptic plasma membrane and postsynaptic densities. Requires the presence of GRIN1 to be targeted at the plasma membrane. Ref.5 Ref.6

Tissue specificity

Isoform 1 and isoform 2 are expressed in olfactory bulb, frontal occipital, entorhinal and pyriform cortices, hippocampus, striatum, thalamus, cerebellum and spinal cord. Ref.1 Ref.2 Ref.4

Developmental stage

Isoform 1 and isoform 2 are expressed in spinal cord, medulla, pons, tegmentum, thalamus and hypothalamus at 15 dpc onwards. Ref.1 Ref.2 Ref.4

Post-translational modification

N-glycosylated. Ref.6

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR3A/GRIN3A subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from direct assay PubMed 17182766. Source: UniProtKB

dendrite development

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor signaling pathway

Inferred from direct assay PubMed 16477151. Source: RGD

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

rhythmic process

Inferred from direct assay PubMed 16477151. Source: RGD

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 17182766. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from direct assay PubMed 15194871. Source: RGD

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay PubMed 16477151. Source: RGD

calcium channel activity

Inferred from electronic annotation. Source: Ensembl

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycine binding

Inferred from direct assay PubMed 17182766. Source: UniProtKB

ionotropic glutamate receptor activity

Inferred from direct assay PubMed 16477151. Source: RGD

neurotransmitter binding

Inferred from direct assay PubMed 16477151. Source: RGD

protein phosphatase 2A binding

Inferred from direct assay PubMed 15194871. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R1M7-1)

Also known as: NR3-long; NR3-l; NR3A-2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9R1M7-2)

Also known as: NR3-short; NR3-s;

The sequence of this isoform differs from the canonical sequence as follows:
     1003-1022: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 11351112Glutamate receptor ionotropic, NMDA 3A
PRO_0000011569

Regions

Topological domain24 – 674651Extracellular Potential
Transmembrane675 – 69521Helical; Potential
Topological domain696 – 74853Cytoplasmic Potential
Transmembrane749 – 76921Helical; Potential
Topological domain770 – 930161Extracellular Potential
Transmembrane931 – 95121Helical; Potential
Topological domain952 – 1135184Cytoplasmic Potential
Region951 – 98737PPP2CB binding site
Coiled coil1080 – 112950 Potential

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2751N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential
Glycosylation5651N-linked (GlcNAc...) Potential
Glycosylation8861N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1003 – 102220Missing in isoform 2.
VSP_011512

Secondary structure

..................................................... 1135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NR3-long) (NR3-l) (NR3A-2) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8EC1FEEAE50AB237

FASTA1,135127,607
        10         20         30         40         50         60 
MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT 

        70         80         90        100        110        120 
APRAASRAQE GGRAGAQRDD PESGTWRPPA PSQGARWLGS ALHGRGPPGS RKLGEGAGAE 

       130        140        150        160        170        180 
TLWPRDALLF AVENLNRVEG LLPYNLSLEV VMAIEAGLGD LPLMPFSSPS SPWSSDPFSF 

       190        200        210        220        230        240 
LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSSVLHIPV LSIVRHEFPR ESQNPLHLQL 

       250        260        270        280        290        300 
SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTENNSKFH LESVINITAN 

       310        320        330        340        350        360 
LSSTKDLLSF LQVQMDNIRN STPTMVMFGC DMDSIRQIFE MSTQFGLSPP ELHWVLGDSQ 

       370        380        390        400        410        420 
NVEELRTEGL PLGLIAHGKT TQSVFEYYVQ DAMELVARAV ATATMIQPEL ALLPSTMNCM 

       430        440        450        460        470        480 
DVKTTNLTSG QYLSRFLANT TFRGLSGSIK VKGSTIISSE NNFFIWNLQH DPMGKPMWTR 

       490        500        510        520        530        540 
LGSWQGGRIV MDSGIWPEQA QRHKTHFQHP NKLHLRVVTL IEHPFVFTRE VDDEGLCPAG 

       550        560        570        580        590        600 
QLCLDPMTND SSMLDRLFSS LHSSNDTVPI KFKKCCYGYC IDLLEQLAED MNFDFDLYIV 

       610        620        630        640        650        660 
GDGKYGAWKN GHWTGLVGDL LSGTANMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR 

       670        680        690        700        710        720 
DTAAPIGAFM WPLHWTMWLG IFVALHITAI FLTLYEWKSP FGMTPKGRNR NKVFSFSSAL 

       730        740        750        760        770        780 
NVCYALLFGR TAAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI 

       790        800        810        820        830        840 
HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVQ YLKNDPEKLD 

       850        860        870        880        890        900 
AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTSNISEL ISQYKSHGFM 

       910        920        930        940        950        960 
DVLHDKWYKV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVHRLLL 

       970        980        990       1000       1010       1020 
PRIKNKSKLQ YWLHTSQRFH RALNTSFVEE KQPRSKTKRV EKSRWRRWTC KTEGDSELSL 

      1030       1040       1050       1060       1070       1080 
FPRSNLGPQQ LMVWNTSNLS HDNQRKYIFN DEEGQNQLGT QAHQDIPLPQ RRRELPASLT 

      1090       1100       1110       1120       1130 
TNGKADSLNV TRSSVIQELS ELEKQIQVIR QELQLAVSRK TELEEYQKTN RTCES 

« Hide

Isoform 2 (NR3-short) (NR3-s) [UniParc].

Checksum: 975DAF3629B60CA1
Show »

FASTA1,115125,171

References

[1]"Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family."
Ciabarra A.M., Sullivan J.M., Gahn L.G., Pecht G., Heinemann S., Sevarino K.A.
J. Neurosci. 15:6498-6508(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Sprague-Dawley.
Tissue: Brain stem and Spinal cord.
[2]"Developmental and regional expression pattern of a novel NMDA receptor-like subunit (NMDAR-L) in the rodent brain."
Sucher N.J., Akbarian S., Chi C.L., Leclerc C.L., Awobuluyi M., Deitcher D.L., Wu M.K., Yuan J.P., Jones E.G., Lipton S.A.
J. Neurosci. 15:6509-6520(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Forebrain.
[3]"Altered single channel properties of NMDA receptors containing a novel NMDA receptor subunit splice variant, NR3A-2."
Perez-Otano I., Contractor A., Schulteis C.T., Gibb A., Heinemann S.F.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"Identification of a long variant of mRNA encoding the NR3 subunit of the NMDA receptor: its regional distribution and developmental expression in the rat brain."
Sun L., Margolis F.L., Shipley M.T., Lidow M.S.
FEBS Lett. 441:392-396(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 839-1122 (ISOFORMS 1/2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Brain.
[5]"An NMDA receptor signaling complex with protein phosphatase 2A."
Chan S.F., Sucher N.J.
J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B AND PPP2CB, INTERACTION WITH PPP2CB.
[6]"Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors."
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F.
J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, GLYCOSYLATION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
[7]"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits."
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.
Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
[8]"Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons."
Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V., Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J., Lipton S.A.
J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L34938 mRNA. Translation: AAA99501.1.
U29873 mRNA. Translation: AAB58957.1.
AF073379 mRNA. Translation: AAD41650.1.
AF061945 mRNA. Translation: AAD11811.1.
PIRT31068.
RefSeqNP_001185512.1. NM_001198583.1.
NP_612555.1. NM_138546.1.
UniGeneRn.180226.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RC7X-ray1.58A/B511-915[»]
2RC8X-ray1.45A/B511-915[»]
2RC9X-ray1.96A/B511-915[»]
4KCDX-ray1.68A/B512-660[»]
ProteinModelPortalQ9R1M7.
SMRQ9R1M7. Positions 512-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid251320. 1 interaction.
IntActQ9R1M7. 1 interaction.

Chemistry

BindingDBQ9R1M7.
ChEMBLCHEMBL1907608.

Proteomic databases

PaxDbQ9R1M7.
PRIDEQ9R1M7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID191573.
KEGGrno:191573.
UCSCRGD:621704. rat. [Q9R1M7-1]

Organism-specific databases

CTD116443.
RGD621704. Grin3a.

Phylogenomic databases

eggNOGNOG320645.
HOGENOMHOG000231528.
HOVERGENHBG052634.
InParanoidQ9R1M7.
KOK05213.
PhylomeDBQ9R1M7.
TreeFamTF314731.

Gene expression databases

GenevestigatorQ9R1M7.

Family and domain databases

InterProIPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF00060. Lig_chan. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9R1M7.
NextBio622654.
PROQ9R1M7.

Entry information

Entry nameNMD3A_RAT
AccessionPrimary (citable) accession number: Q9R1M7
Secondary accession number(s): O09098 expand/collapse secondary AC list , O09155, Q62800, Q63268, Q9Z2H0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references