Full text data of GRIN3A
GRIN3A
(KIAA1973)
[Confidence: low (only semi-automatic identification from reviews)]
Glutamate receptor ionotropic, NMDA 3A; GluN3A (N-methyl-D-aspartate receptor subtype 3A; NMDAR3A; NR3A; NMDAR-L; Flags: Precursor)
Glutamate receptor ionotropic, NMDA 3A; GluN3A (N-methyl-D-aspartate receptor subtype 3A; NMDAR3A; NR3A; NMDAR-L; Flags: Precursor)
UniProt
Q8TCU5
ID NMD3A_HUMAN Reviewed; 1115 AA.
AC Q8TCU5; B3DLF9; Q5VTR3; Q8TF29; Q8WXI6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3A;
DE Short=GluN3A;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-487.
RC 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
RT localization of genes encoding the human NMDA receptor subunits NR3A
RT and NR3B.";
RL Genomics 78:178-184(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-362; ARG-487 AND ASN-835, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11880201; DOI=10.1016/S0304-3940(01)02524-1;
RA Eriksson M., Nilsson A., Froelich-Fabre S., Aakesson E., Dunker J.,
RA Seiger A., Folkesson R., Benedikz E., Sundstroem E.;
RT "Cloning and expression of the human NMDA receptor subunit NR3A.";
RL Neurosci. Lett. 321:177-181(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII.
RT The complete sequences of 50 new cDNA clones which code for large
RT proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14684485; DOI=10.1196/annals.1300.049;
RA Mueller H.T., Meador-Woodruff J.H.;
RT "Expression of the NR3A subunit of the NMDA receptor in human fetal
RT brain.";
RL Ann. N. Y. Acad. Sci. 1003:448-451(2003).
RN [7]
RP INTERACTION WITH PPP2CB.
RX PubMed=11588171;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC with reduced single-channel conductance, low calcium permeability
CC and low voltage-dependent sensitivity to magnesium. Mediated by
CC glycine. May play a role in the development of dendritic spines.
CC May play a role in PPP2CB-NMDAR mediated signaling mechanism (By
CC similarity).
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
CC epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC subunit (GRIN3A or GRIN3B). Does not form functional homomeric
CC channels. Found in a complex with GRIN1, GRIN2A or GRIN2B and
CC PPP2CB. Probably interacts with PPP2CB. No complex with PPP2CB is
CC detected when NMDARs are stimulated by NMDA (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity). Cell junction, synapse, postsynaptic cell
CC membrane (By similarity). Cell junction, synapse, postsynaptic
CC cell membrane, postsynaptic density (By similarity). Note=Enriched
CC in postsynaptic plasma membrane and postsynaptic densities.
CC Requires the presence of GRIN1 to be targeted at the plasma
CC membrane (By similarity).
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC (TC 1.A.10.1) family. NR3A/GRIN3A subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85559.1; Type=Erroneous initiation;
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DR EMBL; AF416558; AAL40734.1; -; mRNA.
DR EMBL; AJ416950; CAC95229.2; -; mRNA.
DR EMBL; AB075853; BAB85559.1; ALT_INIT; mRNA.
DR EMBL; AL591377; CAH69962.1; -; Genomic_DNA.
DR EMBL; AL356516; CAH69962.1; JOINED; Genomic_DNA.
DR EMBL; AL356516; CAI16651.1; -; Genomic_DNA.
DR EMBL; AL591377; CAI16651.1; JOINED; Genomic_DNA.
DR EMBL; BC167432; AAI67432.1; -; mRNA.
DR RefSeq; NP_597702.2; NM_133445.2.
DR UniGene; Hs.654783; -.
DR ProteinModelPortal; Q8TCU5; -.
DR SMR; Q8TCU5; 143-497, 512-952.
DR MINT; MINT-6630950; -.
DR STRING; 9606.ENSP00000355155; -.
DR BindingDB; Q8TCU5; -.
DR ChEMBL; CHEMBL4787; -.
DR DrugBank; DB00659; Acamprosate.
DR DrugBank; DB01161; Chloroprocaine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB00392; Ethopropazine.
DR DrugBank; DB00949; Felbamate.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB01173; Orphenadrine.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00740; Riluzole.
DR PhosphoSite; Q8TCU5; -.
DR DMDM; 212276445; -.
DR PaxDb; Q8TCU5; -.
DR PRIDE; Q8TCU5; -.
DR Ensembl; ENST00000361820; ENSP00000355155; ENSG00000198785.
DR GeneID; 116443; -.
DR KEGG; hsa:116443; -.
DR UCSC; uc004bbp.2; human.
DR CTD; 116443; -.
DR GeneCards; GC09M104331; -.
DR H-InvDB; HIX0008248; -.
DR H-InvDB; HIX0125606; -.
DR HGNC; HGNC:16767; GRIN3A.
DR MIM; 606650; gene.
DR neXtProt; NX_Q8TCU5; -.
DR PharmGKB; PA28983; -.
DR eggNOG; NOG320645; -.
DR HOGENOM; HOG000231528; -.
DR HOVERGEN; HBG052634; -.
DR InParanoid; Q8TCU5; -.
DR KO; K05213; -.
DR OMA; MNCMEVE; -.
DR OrthoDB; EOG7QK0B4; -.
DR GeneWiki; GRIN3A; -.
DR GenomeRNAi; 116443; -.
DR NextBio; 79919; -.
DR PRO; PR:Q8TCU5; -.
DR Bgee; Q8TCU5; -.
DR CleanEx; HS_GRIN3A; -.
DR Genevestigator; Q8TCU5; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0042165; F:neurotransmitter binding; IEA:Ensembl.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:Ensembl.
DR InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR InterPro; IPR001320; Iontro_glu_rcpt.
DR InterPro; IPR001508; NMDA_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; SBP_bac_3.
DR Pfam; PF00060; Lig_chan; 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; SSF53822; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell junction; Cell membrane; Coiled coil; Complete proteome;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Polymorphism; Postsynaptic cell membrane;
KW Receptor; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 1115 Glutamate receptor ionotropic, NMDA 3A.
FT /FTId=PRO_0000011568.
FT TOPO_DOM 24 674 Extracellular (Potential).
FT TRANSMEM 675 695 Helical; (Potential).
FT TOPO_DOM 696 748 Cytoplasmic (Potential).
FT TRANSMEM 749 769 Helical; (Potential).
FT TOPO_DOM 770 930 Extracellular (Potential).
FT TRANSMEM 931 951 Helical; (Potential).
FT TOPO_DOM 952 1115 Cytoplasmic (Potential).
FT REGION 951 987 PPP2CB binding site (By similarity).
FT COILED 1058 1109 Potential.
FT CARBOHYD 145 145 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 275 275 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 426 426 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 439 439 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 549 549 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 565 565 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 886 886 N-linked (GlcNAc...) (Potential).
FT VARIANT 362 362 V -> M (in dbSNP:rs10989591).
FT /FTId=VAR_019672.
FT VARIANT 480 480 R -> H (in dbSNP:rs34755188).
FT /FTId=VAR_047150.
FT VARIANT 487 487 G -> R (in dbSNP:rs10989589).
FT /FTId=VAR_019673.
FT VARIANT 835 835 D -> N (in dbSNP:rs10989563).
FT /FTId=VAR_019674.
FT VARIANT 1041 1041 R -> Q (in dbSNP:rs3739722).
FT /FTId=VAR_019675.
FT CONFLICT 559 559 S -> N (in Ref. 1; AAL40734).
FT CONFLICT 977 977 Q -> R (in Ref. 1; AAL40734).
FT CONFLICT 1073 1073 N -> I (in Ref. 1; AAL40734).
SQ SEQUENCE 1115 AA; 125465 MW; 0FEEC995F6AAF940 CRC64;
MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
APRAASRAPD DSRAGAQRDE PEPGTRRSPA PSPGARWLGS TLHGRGPPGS RKPGEGARAE
ALWPRDALLF AVDNLNRVEG LLPYNLSLEV VMAIEAGLGD LPLLPFSSPS SPWSSDPFSF
LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSLVLHIPV ISIVRHEFPR ESQNPLHLQL
SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTQNNSKFH LGSIINITAN
LPSTQDLLSF LQIQLESIKN STPTVVMFGC DMESIRRIFE ITTQFGVMPP ELRWVLGDSQ
NVEELRTEGL PLGLIAHGKT TQSVFEHYVQ DAMELVARAV ATATMIQPEL ALIPSTMNCM
EVETTNLTSG QYLSRFLANT TFRGLSGSIR VKGSTIVSSE NNFFIWNLQH DPMGKPMWTR
LGSWQGGKIV MDYGIWPEQA QRHKTHFQHP SKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
QLCLDPMTND SSTLDSLFSS LHSSNDTVPI KFKKCCYGYC IDLLEKIAED MNFDFDLYIV
GDGKYGAWKN GHWTGLVGDL LRGTAHMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
DTAAPIGAFM WPLHWTMWLG IFVALHITAV FLTLYEWKSP FGLTPKGRNR SKVFSFSSAL
NICYALLFGR TVAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVE YLKNDPEKLD
AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTANISEL ISQYKSHGFM
DMLHDKWYRV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVYRLLL
PRIKNKSKLQ YWLHTSQRLH RAINTSFIEE KQQHFKTKRV EKRSNVGPRQ LTVWNTSNLS
HDNRRKYIFS DEEGQNQLGI RIHQDIPLPP RRRELPALRT TNGKADSLNV SRNSVMQELS
ELEKQIQVIR QELQLAVSRK TELEEYQRTS RTCES
//
ID NMD3A_HUMAN Reviewed; 1115 AA.
AC Q8TCU5; B3DLF9; Q5VTR3; Q8TF29; Q8WXI6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3A;
DE Short=GluN3A;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-487.
RC 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
RT localization of genes encoding the human NMDA receptor subunits NR3A
RT and NR3B.";
RL Genomics 78:178-184(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-362; ARG-487 AND ASN-835, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11880201; DOI=10.1016/S0304-3940(01)02524-1;
RA Eriksson M., Nilsson A., Froelich-Fabre S., Aakesson E., Dunker J.,
RA Seiger A., Folkesson R., Benedikz E., Sundstroem E.;
RT "Cloning and expression of the human NMDA receptor subunit NR3A.";
RL Neurosci. Lett. 321:177-181(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII.
RT The complete sequences of 50 new cDNA clones which code for large
RT proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1041.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14684485; DOI=10.1196/annals.1300.049;
RA Mueller H.T., Meador-Woodruff J.H.;
RT "Expression of the NR3A subunit of the NMDA receptor in human fetal
RT brain.";
RL Ann. N. Y. Acad. Sci. 1003:448-451(2003).
RN [7]
RP INTERACTION WITH PPP2CB.
RX PubMed=11588171;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC with reduced single-channel conductance, low calcium permeability
CC and low voltage-dependent sensitivity to magnesium. Mediated by
CC glycine. May play a role in the development of dendritic spines.
CC May play a role in PPP2CB-NMDAR mediated signaling mechanism (By
CC similarity).
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
CC epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC subunit (GRIN3A or GRIN3B). Does not form functional homomeric
CC channels. Found in a complex with GRIN1, GRIN2A or GRIN2B and
CC PPP2CB. Probably interacts with PPP2CB. No complex with PPP2CB is
CC detected when NMDARs are stimulated by NMDA (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity). Cell junction, synapse, postsynaptic cell
CC membrane (By similarity). Cell junction, synapse, postsynaptic
CC cell membrane, postsynaptic density (By similarity). Note=Enriched
CC in postsynaptic plasma membrane and postsynaptic densities.
CC Requires the presence of GRIN1 to be targeted at the plasma
CC membrane (By similarity).
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC -!- PTM: N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC (TC 1.A.10.1) family. NR3A/GRIN3A subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85559.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF416558; AAL40734.1; -; mRNA.
DR EMBL; AJ416950; CAC95229.2; -; mRNA.
DR EMBL; AB075853; BAB85559.1; ALT_INIT; mRNA.
DR EMBL; AL591377; CAH69962.1; -; Genomic_DNA.
DR EMBL; AL356516; CAH69962.1; JOINED; Genomic_DNA.
DR EMBL; AL356516; CAI16651.1; -; Genomic_DNA.
DR EMBL; AL591377; CAI16651.1; JOINED; Genomic_DNA.
DR EMBL; BC167432; AAI67432.1; -; mRNA.
DR RefSeq; NP_597702.2; NM_133445.2.
DR UniGene; Hs.654783; -.
DR ProteinModelPortal; Q8TCU5; -.
DR SMR; Q8TCU5; 143-497, 512-952.
DR MINT; MINT-6630950; -.
DR STRING; 9606.ENSP00000355155; -.
DR BindingDB; Q8TCU5; -.
DR ChEMBL; CHEMBL4787; -.
DR DrugBank; DB00659; Acamprosate.
DR DrugBank; DB01161; Chloroprocaine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB00392; Ethopropazine.
DR DrugBank; DB00949; Felbamate.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB01173; Orphenadrine.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB00740; Riluzole.
DR PhosphoSite; Q8TCU5; -.
DR DMDM; 212276445; -.
DR PaxDb; Q8TCU5; -.
DR PRIDE; Q8TCU5; -.
DR Ensembl; ENST00000361820; ENSP00000355155; ENSG00000198785.
DR GeneID; 116443; -.
DR KEGG; hsa:116443; -.
DR UCSC; uc004bbp.2; human.
DR CTD; 116443; -.
DR GeneCards; GC09M104331; -.
DR H-InvDB; HIX0008248; -.
DR H-InvDB; HIX0125606; -.
DR HGNC; HGNC:16767; GRIN3A.
DR MIM; 606650; gene.
DR neXtProt; NX_Q8TCU5; -.
DR PharmGKB; PA28983; -.
DR eggNOG; NOG320645; -.
DR HOGENOM; HOG000231528; -.
DR HOVERGEN; HBG052634; -.
DR InParanoid; Q8TCU5; -.
DR KO; K05213; -.
DR OMA; MNCMEVE; -.
DR OrthoDB; EOG7QK0B4; -.
DR GeneWiki; GRIN3A; -.
DR GenomeRNAi; 116443; -.
DR NextBio; 79919; -.
DR PRO; PR:Q8TCU5; -.
DR Bgee; Q8TCU5; -.
DR CleanEx; HS_GRIN3A; -.
DR Genevestigator; Q8TCU5; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
DR GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0042165; F:neurotransmitter binding; IEA:Ensembl.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:Ensembl.
DR InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR InterPro; IPR001320; Iontro_glu_rcpt.
DR InterPro; IPR001508; NMDA_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; SBP_bac_3.
DR Pfam; PF00060; Lig_chan; 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; SSF53822; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell junction; Cell membrane; Coiled coil; Complete proteome;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Polymorphism; Postsynaptic cell membrane;
KW Receptor; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 1115 Glutamate receptor ionotropic, NMDA 3A.
FT /FTId=PRO_0000011568.
FT TOPO_DOM 24 674 Extracellular (Potential).
FT TRANSMEM 675 695 Helical; (Potential).
FT TOPO_DOM 696 748 Cytoplasmic (Potential).
FT TRANSMEM 749 769 Helical; (Potential).
FT TOPO_DOM 770 930 Extracellular (Potential).
FT TRANSMEM 931 951 Helical; (Potential).
FT TOPO_DOM 952 1115 Cytoplasmic (Potential).
FT REGION 951 987 PPP2CB binding site (By similarity).
FT COILED 1058 1109 Potential.
FT CARBOHYD 145 145 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 275 275 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 426 426 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 439 439 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 549 549 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 565 565 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 886 886 N-linked (GlcNAc...) (Potential).
FT VARIANT 362 362 V -> M (in dbSNP:rs10989591).
FT /FTId=VAR_019672.
FT VARIANT 480 480 R -> H (in dbSNP:rs34755188).
FT /FTId=VAR_047150.
FT VARIANT 487 487 G -> R (in dbSNP:rs10989589).
FT /FTId=VAR_019673.
FT VARIANT 835 835 D -> N (in dbSNP:rs10989563).
FT /FTId=VAR_019674.
FT VARIANT 1041 1041 R -> Q (in dbSNP:rs3739722).
FT /FTId=VAR_019675.
FT CONFLICT 559 559 S -> N (in Ref. 1; AAL40734).
FT CONFLICT 977 977 Q -> R (in Ref. 1; AAL40734).
FT CONFLICT 1073 1073 N -> I (in Ref. 1; AAL40734).
SQ SEQUENCE 1115 AA; 125465 MW; 0FEEC995F6AAF940 CRC64;
MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
APRAASRAPD DSRAGAQRDE PEPGTRRSPA PSPGARWLGS TLHGRGPPGS RKPGEGARAE
ALWPRDALLF AVDNLNRVEG LLPYNLSLEV VMAIEAGLGD LPLLPFSSPS SPWSSDPFSF
LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSLVLHIPV ISIVRHEFPR ESQNPLHLQL
SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTQNNSKFH LGSIINITAN
LPSTQDLLSF LQIQLESIKN STPTVVMFGC DMESIRRIFE ITTQFGVMPP ELRWVLGDSQ
NVEELRTEGL PLGLIAHGKT TQSVFEHYVQ DAMELVARAV ATATMIQPEL ALIPSTMNCM
EVETTNLTSG QYLSRFLANT TFRGLSGSIR VKGSTIVSSE NNFFIWNLQH DPMGKPMWTR
LGSWQGGKIV MDYGIWPEQA QRHKTHFQHP SKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
QLCLDPMTND SSTLDSLFSS LHSSNDTVPI KFKKCCYGYC IDLLEKIAED MNFDFDLYIV
GDGKYGAWKN GHWTGLVGDL LRGTAHMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
DTAAPIGAFM WPLHWTMWLG IFVALHITAV FLTLYEWKSP FGLTPKGRNR SKVFSFSSAL
NICYALLFGR TVAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVE YLKNDPEKLD
AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTANISEL ISQYKSHGFM
DMLHDKWYRV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVYRLLL
PRIKNKSKLQ YWLHTSQRLH RAINTSFIEE KQQHFKTKRV EKRSNVGPRQ LTVWNTSNLS
HDNRRKYIFS DEEGQNQLGI RIHQDIPLPP RRRELPALRT TNGKADSLNV SRNSVMQELS
ELEKQIQVIR QELQLAVSRK TELEEYQRTS RTCES
//
MIM
606650
*RECORD*
*FIELD* NO
606650
*FIELD* TI
*606650 GLUTAMATE RECEPTOR, IONOTROPIC, N-METHYL-D-ASPARTATE 3A; GRIN3A
;;NR3A
*FIELD* TX
read moreN-methyl-D-aspartate (NMDA) receptors belong to the superfamily of
glutamate-regulated ion channels and are present in neurons throughout
the central nervous system (Andersson et al., 2001).
CLONING
By screening a human fetal brain cDNA library, Andersson et al. (2001)
isolated the GRIN3A cDNA. GRIN3A cDNA contains 3345 bp corresponding to
a protein, NR3A, of 1115 amino acids. The human gene showed 72.7%
identity to the rat NR3A gene.
GENE STRUCTURE
Analysis of exon/intron boundaries by Andersson et al. (2001) showed
that GRIN3A is encoded by 9 exons.
MAPPING
By sequence analysis, Andersson et al. (2001) mapped the GRIN3A gene to
9q34.
GENE FUNCTION
Chatterton et al. (2002) found that NR3B is expressed predominantly in
motor neurons, whereas NR3A is more widely distributed. When coexpressed
in Xenopus oocytes, NR3A or NR3B coassembles with NR1 (138249) to form
excitatory glycine receptors that are unaffected by glutamate or NMDA,
and inhibited by D-serine, a coactivator of conventional NMDA receptors.
Moreover, Chatterton et al. (2002) found that NR1/NR3A or NR1/NR3B
receptors form relatively calcium-impermeable cation channels that are
resistant to the open-channel blockers magnesium, MK-801, and memantine,
and to competitive antagonists. In cerebrocortical neurons containing
NR3 family members, glycine triggers a burst of firing, and membrane
patches manifest glycine-responsive single channels that are
suppressible by D-serine. By itself, glycine is normally thought of as
an inhibitory neurotransmitter. In contrast, these NR1/NR3A or NR1/NR3B
NMDA receptors constitute a type of excitatory glycine receptor.
Micu et al. (2006) showed that NMDA glutamate receptors mediate calcium
ion accumulation in central myelin in response to chemical ischemia in
vitro. Using 2-photon microscopy, they imaged fluorescence of the
calcium ion indicator X-rhod-1 loaded into oligodendrocytes and the
cytoplasmic compartment of the myelin sheath in adult rat optic nerves.
The AMPA/kainate receptor antagonist NBQX completely blocked the
ischemic calcium ion increase in oligodendroglial cell bodies, but only
modestly reduced the calcium ion increase in myelin. In contrast, the
calcium ion increase in myelin was abolished by broad-spectrum NMDA
receptor antagonists, but not by more selective blockers of NR2A and
NR2B subunit-containing receptors. In vitro ischemia causes
ultrastructural damage to both axon cylinders and myelin. NMDA receptor
antagonism greatly reduced the damage to myelin. NR1, NR2, and NR3
subunits were detected in myelin by immunohistochemistry and
immunoprecipitation, indicating that all necessary subunits were present
for the formation of functional NMDA receptors. Micu et al. (2006)
concluded that their data showed that the mature myelin sheath can
respond independently to injurious stimuli. Given that axons are known
to release glutamate, the finding that the calcium ion increase is
mediated in large part by activation of myelinic NMDA receptors
suggested a new mechanism of axomyelinic signaling.
ANIMAL MODEL
Das et al. (1998) generated mice deficient in NR3A by targeted
disruption. Mutant mice had enhanced NMDA responses and increased
dendritic spines in early postnatal cerebrocortical neurons, suggesting
that NR3A is involved in the development of synaptic elements by
modulating NMDAR activity.
*FIELD* RF
1. Andersson, O.; Stenqvist, A.; Attersand, A.; von Euler, G.: Nucleotide
sequence, genomic organization, and chromosomal localization of genes
encoding the human NMDA receptor subunits NR3A and NR3B. Genomics 78:
178-184, 2001.
2. Chatterton, J. E.; Awobuluyi, M.; Premkumar, L. S.; Takahashi,
H.; Talantova, M.; Shin, Y.; Cui, J.; Tu, S.; Sevarino, K. A.; Nakanishi,
N.; Tong, G.; Lipton, S. A.; Zhang, D.: Excitatory glycine receptors
containing the NR3 family of NMDA receptor subunits. Nature 415:
793-798, 2002.
3. Das, S.; Sasaki, Y. F.; Rothe, T.; Premkumar, L. S.; Takasu, M.;
Crandall, J. E.; Dikkes, P.; Conner, D. A.; Rayudu, P. V.; Cheung,
W.; Chen, H.-S. V.; Lipton, S. A.; Nakanishi, N.: Increased NMDA
current and spine density in mice lacking the NMDA receptor subunit
NR3A. Nature 393: 377-381, 1998.
4. Micu, I.; Jiang, Q.; Coderre, E.; Ridsdale, A.; Zhang, L.; Woulfe,
J.; Yin, X.; Trapp, B. D.; McRory, J. E.; Rehak, R.; Zamponi, G. W.;
Wang, W.; Stys, P. K.: NMDA receptors mediate calcium accumulation
in myelin during chemical ischaemia. Nature 439: 988-992, 2006.
*FIELD* CN
Ada Hamosh - updated: 12/6/2006
Ada Hamosh - updated: 2/7/2002
*FIELD* CD
Joanna S. Amberger: 1/29/2002
*FIELD* ED
joanna: 01/05/2009
alopez: 12/15/2006
terry: 12/6/2006
alopez: 2/25/2002
alopez: 2/7/2002
terry: 2/7/2002
joanna: 1/30/2002
joanna: 1/29/2002
*RECORD*
*FIELD* NO
606650
*FIELD* TI
*606650 GLUTAMATE RECEPTOR, IONOTROPIC, N-METHYL-D-ASPARTATE 3A; GRIN3A
;;NR3A
*FIELD* TX
read moreN-methyl-D-aspartate (NMDA) receptors belong to the superfamily of
glutamate-regulated ion channels and are present in neurons throughout
the central nervous system (Andersson et al., 2001).
CLONING
By screening a human fetal brain cDNA library, Andersson et al. (2001)
isolated the GRIN3A cDNA. GRIN3A cDNA contains 3345 bp corresponding to
a protein, NR3A, of 1115 amino acids. The human gene showed 72.7%
identity to the rat NR3A gene.
GENE STRUCTURE
Analysis of exon/intron boundaries by Andersson et al. (2001) showed
that GRIN3A is encoded by 9 exons.
MAPPING
By sequence analysis, Andersson et al. (2001) mapped the GRIN3A gene to
9q34.
GENE FUNCTION
Chatterton et al. (2002) found that NR3B is expressed predominantly in
motor neurons, whereas NR3A is more widely distributed. When coexpressed
in Xenopus oocytes, NR3A or NR3B coassembles with NR1 (138249) to form
excitatory glycine receptors that are unaffected by glutamate or NMDA,
and inhibited by D-serine, a coactivator of conventional NMDA receptors.
Moreover, Chatterton et al. (2002) found that NR1/NR3A or NR1/NR3B
receptors form relatively calcium-impermeable cation channels that are
resistant to the open-channel blockers magnesium, MK-801, and memantine,
and to competitive antagonists. In cerebrocortical neurons containing
NR3 family members, glycine triggers a burst of firing, and membrane
patches manifest glycine-responsive single channels that are
suppressible by D-serine. By itself, glycine is normally thought of as
an inhibitory neurotransmitter. In contrast, these NR1/NR3A or NR1/NR3B
NMDA receptors constitute a type of excitatory glycine receptor.
Micu et al. (2006) showed that NMDA glutamate receptors mediate calcium
ion accumulation in central myelin in response to chemical ischemia in
vitro. Using 2-photon microscopy, they imaged fluorescence of the
calcium ion indicator X-rhod-1 loaded into oligodendrocytes and the
cytoplasmic compartment of the myelin sheath in adult rat optic nerves.
The AMPA/kainate receptor antagonist NBQX completely blocked the
ischemic calcium ion increase in oligodendroglial cell bodies, but only
modestly reduced the calcium ion increase in myelin. In contrast, the
calcium ion increase in myelin was abolished by broad-spectrum NMDA
receptor antagonists, but not by more selective blockers of NR2A and
NR2B subunit-containing receptors. In vitro ischemia causes
ultrastructural damage to both axon cylinders and myelin. NMDA receptor
antagonism greatly reduced the damage to myelin. NR1, NR2, and NR3
subunits were detected in myelin by immunohistochemistry and
immunoprecipitation, indicating that all necessary subunits were present
for the formation of functional NMDA receptors. Micu et al. (2006)
concluded that their data showed that the mature myelin sheath can
respond independently to injurious stimuli. Given that axons are known
to release glutamate, the finding that the calcium ion increase is
mediated in large part by activation of myelinic NMDA receptors
suggested a new mechanism of axomyelinic signaling.
ANIMAL MODEL
Das et al. (1998) generated mice deficient in NR3A by targeted
disruption. Mutant mice had enhanced NMDA responses and increased
dendritic spines in early postnatal cerebrocortical neurons, suggesting
that NR3A is involved in the development of synaptic elements by
modulating NMDAR activity.
*FIELD* RF
1. Andersson, O.; Stenqvist, A.; Attersand, A.; von Euler, G.: Nucleotide
sequence, genomic organization, and chromosomal localization of genes
encoding the human NMDA receptor subunits NR3A and NR3B. Genomics 78:
178-184, 2001.
2. Chatterton, J. E.; Awobuluyi, M.; Premkumar, L. S.; Takahashi,
H.; Talantova, M.; Shin, Y.; Cui, J.; Tu, S.; Sevarino, K. A.; Nakanishi,
N.; Tong, G.; Lipton, S. A.; Zhang, D.: Excitatory glycine receptors
containing the NR3 family of NMDA receptor subunits. Nature 415:
793-798, 2002.
3. Das, S.; Sasaki, Y. F.; Rothe, T.; Premkumar, L. S.; Takasu, M.;
Crandall, J. E.; Dikkes, P.; Conner, D. A.; Rayudu, P. V.; Cheung,
W.; Chen, H.-S. V.; Lipton, S. A.; Nakanishi, N.: Increased NMDA
current and spine density in mice lacking the NMDA receptor subunit
NR3A. Nature 393: 377-381, 1998.
4. Micu, I.; Jiang, Q.; Coderre, E.; Ridsdale, A.; Zhang, L.; Woulfe,
J.; Yin, X.; Trapp, B. D.; McRory, J. E.; Rehak, R.; Zamponi, G. W.;
Wang, W.; Stys, P. K.: NMDA receptors mediate calcium accumulation
in myelin during chemical ischaemia. Nature 439: 988-992, 2006.
*FIELD* CN
Ada Hamosh - updated: 12/6/2006
Ada Hamosh - updated: 2/7/2002
*FIELD* CD
Joanna S. Amberger: 1/29/2002
*FIELD* ED
joanna: 01/05/2009
alopez: 12/15/2006
terry: 12/6/2006
alopez: 2/25/2002
alopez: 2/7/2002
terry: 2/7/2002
joanna: 1/30/2002
joanna: 1/29/2002