NMDE2_XENLA
ID NMDE2_XENLA Reviewed; 1448 AA.
AC A7XY94;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
DE Short=GluN2B;
DE AltName: Full=N-methyl D-aspartate receptor subtype 2B;
DE Short=NMDAR2B;
DE Short=NR2B {ECO:0000303|PubMed:18177891};
DE Flags: Precursor;
GN Name=grin2b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:ABU84989.1};
RN [1] {ECO:0000312|EMBL:ABU84989.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Oocyte {ECO:0000303|PubMed:18177891};
RX PubMed=18177891; DOI=10.1016/j.jmb.2007.11.105;
RA Schmidt C., Hollmann M.;
RT "Apparent homomeric NR1 currents observed in Xenopus oocytes are caused by
RT an endogenous NR2 subunit.";
RL J. Mol. Biol. 376:658-670(2008).
RN [2] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [3] {ECO:0007744|PDB:4TLL, ECO:0007744|PDB:4TLM}
RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 20-839 IN COMPLEX WITH GRIN1 AND
RP SYNTHETIC AGONIST, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
RP DOMAIN, GLYCOSYLATION AT ASN-336 AND ASN-685, AND DISULFIDE BONDS.
RX PubMed=25008524; DOI=10.1038/nature13548;
RA Lee C.H., Lu W., Michel J.C., Goehring A., Du J., Song X., Gouaux E.;
RT "NMDA receptor structures reveal subunit arrangement and pore
RT architecture.";
RL Nature 511:191-197(2014).
RN [4] {ECO:0007744|PDB:5IOU, ECO:0007744|PDB:5IOV, ECO:0007744|PDB:5IPQ}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS) OF 1-839 IN COMPLEX WITH
RP GRIN1 AND GLUTAMATE, AND SUBUNIT.
RX PubMed=27062927; DOI=10.1016/j.cell.2016.03.028;
RA Zhu S., Stein R.A., Yoshioka C., Lee C.H., Goehring A., Mchaourab H.S.,
RA Gouaux E.;
RT "Mechanism of NMDA Receptor Inhibition and Activation.";
RL Cell 165:704-714(2016).
RN [5] {ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-840 IN COMPLEX WITH
RP GRIN1 AND GRIN2A, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, FUNCTION,
RP DOMAIN, GLYCOSYLATION AT ASN-336 AND ASN-685, AND DISULFIDE BONDS.
RX PubMed=28232581; DOI=10.1126/science.aal3729;
RA Lu W., Du J., Goehring A., Gouaux E.;
RT "Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric
RT modulation.";
RL Science 355:0-0(2017).
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+)
CC (PubMed:18177891, PubMed:25008524, PubMed:28232581). Sensitivity to
CC glutamate and channel kinetics depend on the subunit composition
CC (Probable). {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524,
CC ECO:0000269|PubMed:28232581, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of
CC two zeta subunits (grin1), and two epsilon subunits (grin2a, grin2b,
CC grin2c or grin2d) (in vitro) (PubMed:18177891, PubMed:25008524,
CC PubMed:27062927, PubMed:28232581). In vivo, the subunit composition may
CC depend on the expression levels of the different subunits (Probable).
CC {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524,
CC ECO:0000269|PubMed:27062927, ECO:0000269|PubMed:28232581, ECO:0000305}.
CC -!- INTERACTION:
CC A7XY94; A0A1L8F5J9: grin1; NbExp=3; IntAct=EBI-16113306, EBI-15932423;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18177891,
CC ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:25008524,
CC ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in oocytes. {ECO:0000269|PubMed:18177891}.
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000305|PubMed:25008524, ECO:0000305|PubMed:28232581}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2B/GRIN2B subfamily. {ECO:0000305}.
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DR EMBL; EU104357; ABU84989.1; -; mRNA.
DR EMBL; CM004473; OCT82994.1; -; Genomic_DNA.
DR RefSeq; NP_001104191.1; NM_001110721.1.
DR RefSeq; XP_018114751.1; XM_018259262.1.
DR PDB; 4TLL; X-ray; 3.59 A; B/D=20-839.
DR PDB; 4TLM; X-ray; 3.77 A; B/D=20-839.
DR PDB; 5IOU; EM; 7.00 A; B/D=1-839.
DR PDB; 5IOV; EM; 7.50 A; B/D=1-839.
DR PDB; 5IPQ; EM; 13.50 A; B/D=1-839.
DR PDB; 5IPR; EM; 14.10 A; B/D=1-839.
DR PDB; 5IPS; EM; 13.50 A; B/D=1-839.
DR PDB; 5IPT; EM; 14.10 A; B/D=1-839.
DR PDB; 5IPU; EM; 15.40 A; B/D=1-839.
DR PDB; 5IPV; EM; 9.25 A; B/D=1-839.
DR PDB; 5UN1; X-ray; 3.60 A; B/D/F/H=400-839.
DR PDB; 5UOW; EM; 4.50 A; D=1-840.
DR PDB; 5UP2; EM; 6.00 A; D=1-840.
DR PDBsum; 4TLL; -.
DR PDBsum; 4TLM; -.
DR PDBsum; 5IOU; -.
DR PDBsum; 5IOV; -.
DR PDBsum; 5IPQ; -.
DR PDBsum; 5IPR; -.
DR PDBsum; 5IPS; -.
DR PDBsum; 5IPT; -.
DR PDBsum; 5IPU; -.
DR PDBsum; 5IPV; -.
DR PDBsum; 5UN1; -.
DR PDBsum; 5UOW; -.
DR PDBsum; 5UP2; -.
DR AlphaFoldDB; A7XY94; -.
DR SMR; A7XY94; -.
DR DIP; DIP-61037N; -.
DR IntAct; A7XY94; 1.
DR STRING; 8355.A7XY94; -.
DR iPTMnet; A7XY94; -.
DR GeneID; 100126610; -.
DR KEGG; xla:100126610; -.
DR CTD; 100126610; -.
DR OMA; SREVYSC; -.
DR OrthoDB; 188544at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 100126610; Expressed in blastula and 5 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0032026; P:response to magnesium ion; IDA:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IDA:UniProtKB.
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; IPR018884; NMDAR2_C.
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 Pfam; PF10565; NMDAR2_C; 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 3D-structure; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Metal-binding; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1448
FT /note="Glutamate receptor ionotropic, NMDA 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_5010821104"
FT TOPO_DOM 25..554
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TRANSMEM 555..573
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 574..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25008524"
FT INTRAMEM 601..620
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 621..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TRANSMEM 628..643
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 644..819
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TRANSMEM 820..839
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 840..1448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25008524"
FT REGION 601..620
FT /note="Pore-forming"
FT /evidence="ECO:0000305|PubMed:25008524"
FT REGION 1254..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 511
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:25008524"
FT BINDING 516
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 687..688
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 729
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLM,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT DISULFID 81..316
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:4TLM, ECO:0007744|PDB:5UOW"
FT DISULFID 426..453
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:4TLM, ECO:0007744|PDB:5UOW"
FT DISULFID 433..454
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:4TLM, ECO:0007744|PDB:5UOW"
FT DISULFID 743..798
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:4TLM, ECO:0007744|PDB:5UOW"
SQ 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
