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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

grin2b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Mg2+ (PubMed:18177891, PubMed:25008524, PubMed:28232581). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable).Curated3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei511Glutamate1 Publication1
Binding sitei516GlutamateBy similarity1
Binding sitei729GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • protein heterotetramerization Source: UniProtKB
  • response to magnesium ion Source: UniProtKB
  • response to zinc ion Source: UniProtKB

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2B
Short name:
GluN2B
Alternative name(s):
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B
Short name:
NR2B1 Publication
Gene namesi
Name:grin2b
OrganismiXenopus laevis (African clawed frog)Imported
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus
Proteomesi
  • UP000186698 Componentsi: Chromosome 4s, Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 554Extracellular1 PublicationAdd BLAST530
Transmembranei555 – 573Helical1 PublicationAdd BLAST19
Topological domaini574 – 600Cytoplasmic1 PublicationAdd BLAST27
Intramembranei601 – 620Discontinuously helical1 PublicationAdd BLAST20
Topological domaini621 – 627Cytoplasmic1 Publication7
Transmembranei628 – 643Helical1 PublicationAdd BLAST16
Topological domaini644 – 819Extracellular1 PublicationAdd BLAST176
Transmembranei820 – 839HelicalBy similarityAdd BLAST20
Topological domaini840 – 1448Cytoplasmic1 PublicationAdd BLAST609

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_501082110425 – 1448Glutamate receptor ionotropic, NMDA 2BSequence analysisAdd BLAST1424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi81 ↔ 316Combined sources2 Publications
Glycosylationi336N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi426 ↔ 453Combined sources2 Publications
Disulfide bondi433 ↔ 454Combined sources2 Publications
Glycosylationi685N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi743 ↔ 798Combined sources2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Detected in oocytes.1 Publication

Interactioni

Subunit structurei

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).Curated4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C0KD153EBI-16113306,EBI-16113290

Protein-protein interaction databases

DIPiDIP-61037N.
IntActiA7XY94. 1 interactor.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TLLX-ray3.59B/D20-839[»]
4TLMX-ray3.77B/D20-839[»]
5IOUelectron microscopy7.00B/D1-839[»]
5IOVelectron microscopy7.50B/D1-839[»]
5IPQelectron microscopy13.50B/D1-839[»]
5IPRelectron microscopy14.10B/D1-839[»]
5IPSelectron microscopy13.50B/D1-839[»]
5IPTelectron microscopy14.10B/D1-839[»]
5IPUelectron microscopy15.40B/D1-839[»]
5IPVelectron microscopy9.25B/D1-839[»]
5UOWelectron microscopy4.50D1-840[»]
5UP2electron microscopy6.00D1-840[»]
SMRiA7XY94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni601 – 620Pore-forming1 PublicationAdd BLAST20
Regioni687 – 688Glutamate bindingBy similarity2

Domaini

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.2 Publications

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052635.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7XY94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPTEACCYL KISLIILFYM GCYAQKHPNM DIAVILVGTT EEVAIKDVHE
60 70 80 90 100
KDDFHHLPVT PRVALVTMNE SDPKSIITRI CDLMSDKKVQ GVVFGDDTDQ
110 120 130 140 150
EAIAQILDFI SVQTLTPILG IHGGSSMIMA DKEEASMFFQ FGPSIEQQAS
160 170 180 190 200
VMLNIMEEYD WYIFSIVTTY FPGYQDFENK VRSTIENSFV GWELEEVIHL
210 220 230 240 250
DMSLDDIDSK IQNQLKKLQS PVILLYCTKE EATYIFEVAH SVGLTGYGFT
260 270 280 290 300
WIVPSLVAGD TDTVPDEFPT GLISVSYDEW DYDLPARVRD GIAIITTAAS
310 320 330 340 350
TMLSEHNSIP QSKSSCNNIQ ESRVYEAHML KRYLINVTFE GRNLSFSEDG
360 370 380 390 400
YQMHPKLVII LLNQERKWER VGKYKDRSLK MKYYVWPVFD LYPNSEEHKD
410 420 430 440 450
EHLSIVTLEE APFVIVEDVD PLSGTCMRNT VPCRKQIRPE NRTEEGGNYI
460 470 480 490 500
KRCCKGFCID ILKKIAKTVK FTYDLYLVTN GKHGKKINGT WNGMIGEVVT
510 520 530 540 550
KRAYMAVGSL TINEERSEVV DFSVPFIETG ISVMVSRSNG TVSPSAFLEP
560 570 580 590 600
FSADVWVMMF VMLLIVSAVA VFVFEYFSPV GYNRCLADGR EPGGPSFTIG
610 620 630 640 650
KAIWLLWGLV FNNSVPVQNP KGTTSKIMVS VWAFFAVIFL ASYTANLAAF
660 670 680 690 700
MIQEEYVDQV SGLSDKKFQR PNDFSPAFRF GTVPNGSTER NIRNNYLEMH
710 720 730 740 750
SYMVKFNQRS VQDALLSLKS GKLDAFIYDA AVLNYMAGRD EGCKLVTIGS
760 770 780 790 800
GKVFATTGYG IAIQKDSGWK RQVDLAILQL FGDGEMEELE ALWLTGICHN
810 820 830 840 850
EKNEVMSSQL DIDNMAGVFY MLAAAMALSL ITFIMEHLFF WQLRHCFMGV
860 870 880 890 900
CSGKPGMVFS ISRGIYSCIH GVAIEDRQSA LDSPSATMNN THSNILRLLR
910 920 930 940 950
TAKNMANLSG VNGSPQSALD FIRRESSVYD ISEHRRSFTH SDCKSFQPEE
960 970 980 990 1000
NLFSDYISEV ERTFGNLQLK DSNVYQDHFH HHRPHSIGSN SSIDGLYDCD
1010 1020 1030 1040 1050
NAPFTTQPRS LSKKPLDIGL PSKHPSPQIG DLYGKFSFKS DHYGAPDDLI
1060 1070 1080 1090 1100
RSDVSDISTH TVTYGNIEGN AKRRKQYKDS LKKRPASAKS RREFDEIELA
1110 1120 1130 1140 1150
YRRRQRSPDH KRYFRDKEGL RDFYLDQFRT KENNPHWEHV DLTHIYAERA
1160 1170 1180 1190 1200
DDFKHDTSCS NRQHQKHVGE FVQTDRKHGS GGNAWEKNMS NIEWEDRASS
1210 1220 1230 1240 1250
NFCRNCPSKM HNYTGQNTNR PACIRCEVCK KAGNLYDISE DNSLQDLEAR
1260 1270 1280 1290 1300
PIQAPNSKYP QSPNGKAQKR NRSKLHRQHS YDTFVDLQKE DVTLAPRSVS
1310 1320 1330 1340 1350
LKDKERFLDG SPYAHMFEMP NETSFTSKSH GPTHNPGGYM LSRSLYPDRV
1360 1370 1380 1390 1400
TQNPFIPTFG DDQCLLHGSK PYYFRQPAIG GLKGRADFRG AGKSLSAQHS
1410 1420 1430 1440
GPSGHFQKDI CIGNQPNACV SNNKNPRSFN NSTNGHVYEK LSSIESDV
Length:1,448
Mass (Da):163,913
Last modified:October 23, 2007 - v1
Checksum:iEBF9301FEE749D5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU104357 mRNA. Translation: ABU84989.1.
CM004473 Genomic DNA. Translation: OCT82994.1.
RefSeqiNP_001104191.1. NM_001110721.1.
XP_018114751.1. XM_018259262.1.
UniGeneiXl.83851.

Genome annotation databases

GeneIDi100126610.

Similar proteinsi

Entry informationi

Entry nameiNMDE2_XENLA
AccessioniPrimary (citable) accession number: A7XY94
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2017
Last sequence update: October 23, 2007
Last modified: November 22, 2017
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families