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Glutamate receptor ionotropic, NMDA 2B (GluN2B) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B)

 NMDE2_XENLA             Reviewed;        1448 AA.
A7XY94;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 1.
31-JAN-2018, entry version 66.
RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
Short=GluN2B;
AltName: Full=N-methyl D-aspartate receptor subtype 2B;
Short=NMDAR2B;
Short=NR2B {ECO:0000303|PubMed:18177891};
Flags: Precursor;
Name=grin2b;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355 {ECO:0000312|EMBL:ABU84989.1};
[1] {ECO:0000312|EMBL:ABU84989.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND TISSUE SPECIFICITY.
TISSUE=Oocyte {ECO:0000303|PubMed:18177891};
PubMed=18177891; DOI=10.1016/j.jmb.2007.11.105;
Schmidt C., Hollmann M.;
"Apparent homomeric NR1 currents observed in Xenopus oocytes are
caused by an endogenous NR2 subunit.";
J. Mol. Biol. 376:658-670(2008).
[2] {ECO:0000312|Proteomes:UP000186698}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J {ECO:0000312|Proteomes:UP000186698};
PubMed=27762356; DOI=10.1038/nature19840;
Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
"Genome evolution in the allotetraploid frog Xenopus laevis.";
Nature 538:336-343(2016).
[3] {ECO:0000244|PDB:4TLL, ECO:0000244|PDB:4TLM}
X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 20-839 IN COMPLEX WITH GRIN1
AND SYNTHETIC AGONIST, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
TOPOLOGY, DOMAIN, GLYCOSYLATION AT ASN-336 AND ASN-685, AND DISULFIDE
BONDS.
PubMed=25008524; DOI=10.1038/nature13548;
Lee C.H., Lu W., Michel J.C., Goehring A., Du J., Song X., Gouaux E.;
"NMDA receptor structures reveal subunit arrangement and pore
architecture.";
Nature 511:191-197(2014).
[4] {ECO:0000244|PDB:5IOU, ECO:0000244|PDB:5IOV, ECO:0000244|PDB:5IPQ}
STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS) OF 1-839 IN COMPLEX
WITH GRIN1 AND GLUTAMATE, AND SUBUNIT.
PubMed=27062927; DOI=10.1016/j.cell.2016.03.028;
Zhu S., Stein R.A., Yoshioka C., Lee C.H., Goehring A.,
Mchaourab H.S., Gouaux E.;
"Mechanism of NMDA Receptor Inhibition and Activation.";
Cell 165:704-714(2016).
[5] {ECO:0000244|PDB:5UOW, ECO:0000244|PDB:5UP2}
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-840 IN COMPLEX
WITH GRIN1 AND GRIN2A, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
FUNCTION, DOMAIN, GLYCOSYLATION AT ASN-336 AND ASN-685, AND DISULFIDE
BONDS.
PubMed=28232581; DOI=10.1126/science.aal3729;
Lu W., Du J., Goehring A., Gouaux E.;
"Cryo-EM structures of the triheteromeric NMDA receptor and its
allosteric modulation.";
Science 355:0-0(2017).
-!- FUNCTION: Component of NMDA receptor complexes that function as
heterotetrameric, ligand-gated ion channels with high calcium
permeability and voltage-dependent sensitivity to magnesium.
Channel activation requires binding of the neurotransmitter
glutamate to the epsilon subunit, glycine binding to the zeta
subunit, plus membrane depolarization to eliminate channel
inhibition by Mg(2+) (PubMed:18177891, PubMed:25008524,
PubMed:28232581). Sensitivity to glutamate and channel kinetics
depend on the subunit composition (Probable).
{ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581, ECO:0000305}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (grin1), and two epsilon subunits (grin2a,
grin2b, grin2c or grin2d) (in vitro) (PubMed:18177891,
PubMed:25008524, PubMed:27062927, PubMed:28232581). In vivo, the
subunit composition may depend on the expression levels of the
different subunits (Probable). {ECO:0000269|PubMed:18177891,
ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:27062927,
ECO:0000269|PubMed:28232581, ECO:0000305}.
-!- INTERACTION:
A0A1L8F5J9:grin1; NbExp=3; IntAct=EBI-16113306, EBI-15932423;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18177891,
ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}; Multi-
pass membrane protein {ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}. Cell junction, synapse, postsynaptic
cell membrane {ECO:0000255|SAAS:SAAS00582638}.
-!- TISSUE SPECIFICITY: Detected in oocytes.
{ECO:0000269|PubMed:18177891}.
-!- DOMAIN: A hydrophobic region that gives rise to the prediction of
a transmembrane span does not cross the membrane, but is part of a
discontinuously helical region that dips into the membrane and is
probably part of the pore and of the selectivity filter.
{ECO:0000305|PubMed:25008524, ECO:0000305|PubMed:28232581}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2B/GRIN2B subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; EU104357; ABU84989.1; -; mRNA.
EMBL; CM004473; OCT82994.1; -; Genomic_DNA.
RefSeq; NP_001104191.1; NM_001110721.1.
RefSeq; XP_018114751.1; XM_018259262.1.
UniGene; Xl.83851; -.
PDB; 4TLL; X-ray; 3.59 A; B/D=20-839.
PDB; 4TLM; X-ray; 3.77 A; B/D=20-839.
PDB; 5IOU; EM; 7.00 A; B/D=1-839.
PDB; 5IOV; EM; 7.50 A; B/D=1-839.
PDB; 5IPQ; EM; 13.50 A; B/D=1-839.
PDB; 5IPR; EM; 14.10 A; B/D=1-839.
PDB; 5IPS; EM; 13.50 A; B/D=1-839.
PDB; 5IPT; EM; 14.10 A; B/D=1-839.
PDB; 5IPU; EM; 15.40 A; B/D=1-839.
PDB; 5IPV; EM; 9.25 A; B/D=1-839.
PDB; 5UOW; EM; 4.50 A; D=1-840.
PDB; 5UP2; EM; 6.00 A; D=1-840.
PDBsum; 4TLL; -.
PDBsum; 4TLM; -.
PDBsum; 5IOU; -.
PDBsum; 5IOV; -.
PDBsum; 5IPQ; -.
PDBsum; 5IPR; -.
PDBsum; 5IPS; -.
PDBsum; 5IPT; -.
PDBsum; 5IPU; -.
PDBsum; 5IPV; -.
PDBsum; 5UOW; -.
PDBsum; 5UP2; -.
SMR; A7XY94; -.
DIP; DIP-61037N; -.
IntAct; A7XY94; 1.
GeneID; 100126610; -.
KEGG; xla:100126610; -.
CTD; 100126610; -.
HOVERGEN; HBG052635; -.
KO; K05210; -.
Proteomes; UP000186698; Chromosome 4s.
Proteomes; UP000186698; Unassembled WGS sequence.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0032026; P:response to magnesium ion; IDA:UniProtKB.
GO; GO:0010043; P:response to zinc ion; IDA:UniProtKB.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR018884; NMDAR2_C.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
Pfam; PF10565; NMDAR2_C; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
Metal-binding; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1448 Glutamate receptor ionotropic, NMDA 2B.
{ECO:0000255}.
/FTId=PRO_5010821104.
TOPO_DOM 25 554 Extracellular.
{ECO:0000269|PubMed:25008524}.
TRANSMEM 555 573 Helical. {ECO:0000269|PubMed:25008524}.
TOPO_DOM 574 600 Cytoplasmic.
{ECO:0000269|PubMed:25008524}.
INTRAMEM 601 620 Discontinuously helical.
{ECO:0000269|PubMed:25008524}.
TOPO_DOM 621 627 Cytoplasmic.
{ECO:0000269|PubMed:25008524}.
TRANSMEM 628 643 Helical. {ECO:0000269|PubMed:25008524}.
TOPO_DOM 644 819 Extracellular.
{ECO:0000269|PubMed:25008524}.
TRANSMEM 820 839 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 840 1448 Cytoplasmic.
{ECO:0000269|PubMed:25008524}.
REGION 601 620 Pore-forming.
{ECO:0000305|PubMed:25008524}.
REGION 687 688 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
BINDING 511 511 Glutamate. {ECO:0000305|PubMed:25008524}.
BINDING 516 516 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 729 729 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4TLL,
ECO:0000244|PDB:5UOW,
ECO:0000244|PDB:5UP2,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4TLM,
ECO:0000244|PDB:5UOW,
ECO:0000244|PDB:5UP2,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
DISULFID 81 316 {ECO:0000244|PDB:4TLL,
ECO:0000244|PDB:4TLM,
ECO:0000244|PDB:5UOW,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
DISULFID 426 453 {ECO:0000244|PDB:4TLL,
ECO:0000244|PDB:4TLM,
ECO:0000244|PDB:5UOW,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
DISULFID 433 454 {ECO:0000244|PDB:4TLL,
ECO:0000244|PDB:4TLM,
ECO:0000244|PDB:5UOW,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
DISULFID 743 798 {ECO:0000244|PDB:4TLL,
ECO:0000244|PDB:4TLM,
ECO:0000244|PDB:5UOW,
ECO:0000269|PubMed:25008524,
ECO:0000269|PubMed:28232581}.
SEQUENCE 1448 AA; 163913 MW; EBF9301FEE749D5D CRC64;
MRPTEACCYL KISLIILFYM GCYAQKHPNM DIAVILVGTT EEVAIKDVHE KDDFHHLPVT
PRVALVTMNE SDPKSIITRI CDLMSDKKVQ GVVFGDDTDQ EAIAQILDFI SVQTLTPILG
IHGGSSMIMA DKEEASMFFQ FGPSIEQQAS VMLNIMEEYD WYIFSIVTTY FPGYQDFENK
VRSTIENSFV GWELEEVIHL DMSLDDIDSK IQNQLKKLQS PVILLYCTKE EATYIFEVAH
SVGLTGYGFT WIVPSLVAGD TDTVPDEFPT GLISVSYDEW DYDLPARVRD GIAIITTAAS
TMLSEHNSIP QSKSSCNNIQ ESRVYEAHML KRYLINVTFE GRNLSFSEDG YQMHPKLVII
LLNQERKWER VGKYKDRSLK MKYYVWPVFD LYPNSEEHKD EHLSIVTLEE APFVIVEDVD
PLSGTCMRNT VPCRKQIRPE NRTEEGGNYI KRCCKGFCID ILKKIAKTVK FTYDLYLVTN
GKHGKKINGT WNGMIGEVVT KRAYMAVGSL TINEERSEVV DFSVPFIETG ISVMVSRSNG
TVSPSAFLEP FSADVWVMMF VMLLIVSAVA VFVFEYFSPV GYNRCLADGR EPGGPSFTIG
KAIWLLWGLV FNNSVPVQNP KGTTSKIMVS VWAFFAVIFL ASYTANLAAF MIQEEYVDQV
SGLSDKKFQR PNDFSPAFRF GTVPNGSTER NIRNNYLEMH SYMVKFNQRS VQDALLSLKS
GKLDAFIYDA AVLNYMAGRD EGCKLVTIGS GKVFATTGYG IAIQKDSGWK RQVDLAILQL
FGDGEMEELE ALWLTGICHN EKNEVMSSQL DIDNMAGVFY MLAAAMALSL ITFIMEHLFF
WQLRHCFMGV CSGKPGMVFS ISRGIYSCIH GVAIEDRQSA LDSPSATMNN THSNILRLLR
TAKNMANLSG VNGSPQSALD FIRRESSVYD ISEHRRSFTH SDCKSFQPEE NLFSDYISEV
ERTFGNLQLK DSNVYQDHFH HHRPHSIGSN SSIDGLYDCD NAPFTTQPRS LSKKPLDIGL
PSKHPSPQIG DLYGKFSFKS DHYGAPDDLI RSDVSDISTH TVTYGNIEGN AKRRKQYKDS
LKKRPASAKS RREFDEIELA YRRRQRSPDH KRYFRDKEGL RDFYLDQFRT KENNPHWEHV
DLTHIYAERA DDFKHDTSCS NRQHQKHVGE FVQTDRKHGS GGNAWEKNMS NIEWEDRASS
NFCRNCPSKM HNYTGQNTNR PACIRCEVCK KAGNLYDISE DNSLQDLEAR PIQAPNSKYP
QSPNGKAQKR NRSKLHRQHS YDTFVDLQKE DVTLAPRSVS LKDKERFLDG SPYAHMFEMP
NETSFTSKSH GPTHNPGGYM LSRSLYPDRV TQNPFIPTFG DDQCLLHGSK PYYFRQPAIG
GLKGRADFRG AGKSLSAQHS GPSGHFQKDI CIGNQPNACV SNNKNPRSFN NSTNGHVYEK
LSSIESDV


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