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Protein

Glutamate receptor ionotropic, NMDA 2B

Gene

GRIN2B

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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+. Sensitivity to glutamate and channel kinetics depend on the subunit composition (By similarity). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death. Contributes to neural pattern formation in the developing brain. Plays a role in long-term depression (LTD) of hippocampus membrane currents and in synaptic plasticity (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi127ZincBy similarity1
Metal bindingi284ZincBy similarity1
Binding sitei514GlutamateBy similarity1
Binding sitei519GlutamateBy similarity1
Sitei615Functional determinant of NMDA receptorsBy similarity1
Binding sitei732GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-CFA-3928662. EPHB-mediated forward signaling.
R-CFA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-CFA-442729. CREB phosphorylation through the activation of CaMKII.
R-CFA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-CFA-5673001. RAF/MAP kinase cascade.
R-CFA-8849932. Synaptic adhesion-like molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2B
Short name:
GluN2B
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-2
N-methyl D-aspartate receptor subtype 2B
Short name:
NMDAR2B
Short name:
NR2B
Gene namesi
Name:GRIN2B
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 27

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 domaini27 – 557ExtracellularBy similarityAdd BLAST531
Transmembranei558 – 576HelicalBy similarityAdd BLAST19
Topological domaini577 – 603CytoplasmicBy similarityAdd BLAST27
Intramembranei604 – 623Discontinuously helicalBy similarityAdd BLAST20
Topological domaini624 – 630CytoplasmicBy similarity7
Transmembranei631 – 646HelicalBy similarityAdd BLAST16
Topological domaini647 – 817ExtracellularBy similarityAdd BLAST171
Transmembranei818 – 837HelicalBy similarityAdd BLAST20
Topological domaini838 – 1485CytoplasmicBy similarityAdd BLAST648

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000028957927 – 1485Glutamate receptor ionotropic, NMDA 2BAdd BLAST1459

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi86 ↔ 321By similarity
Glycosylationi341N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi429 ↔ 456By similarity
Disulfide bondi436 ↔ 457By similarity
Glycosylationi444N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi688N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi746 ↔ 801By similarity
Modified residuei882PhosphoserineBy similarity1
Modified residuei886PhosphoserineBy similarity1
Modified residuei917PhosphoserineBy similarity1
Modified residuei920PhosphoserineBy similarity1
Modified residuei962PhosphotyrosineBy similarity1
Modified residuei1039PhosphotyrosineBy similarity1
Modified residuei1058PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1064PhosphoserineBy similarity1
Modified residuei1109PhosphotyrosineBy similarity1
Modified residuei1133PhosphotyrosineBy similarity1
Modified residuei1143PhosphoserineBy similarity1
Modified residuei1155PhosphotyrosineBy similarity1
Modified residuei1255PhosphoserineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1303Phosphoserine; by DAPK1By similarity1
Modified residuei1475PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylated on tyrosine residues (By similarity). Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ5R1P3.
PRIDEiQ5R1P3.

Expressioni

Gene expression databases

BgeeiENSCAFG00000013148.

Interactioni

Subunit structurei

Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro). Can also form heterotetrameric channels that contain at least one zeta subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B. In vivo, the subunit composition may depend on the expression levels of the different subunits. Found in a complex with GRIN1, GRIN3A and PPP2CB. Found in a complex with GRIN1 and GRIN3B. Interacts with MAGI3. Interacts with HIP1 and Neto1. Interacts with PDZ domains of PATJ and DLG4. Interacts with DAPK1 (By similarity). Found in a complex with GRIN1 and PRR7. Interacts with PRR7 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000039796.

Structurei

3D structure databases

ProteinModelPortaliQ5R1P3.
SMRiQ5R1P3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni604 – 623Pore-formingBy similarityAdd BLAST20
Regioni690 – 691Glutamate bindingBy similarity2
Regioni1292 – 1304Interaction with DAPK1By similarityAdd BLAST13

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1483 – 1485PDZ-bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi984 – 989Poly-His6

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.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
GeneTreeiENSGT00760000119186.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ5R1P3.
KOiK05210.
TreeFamiTF314731.

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.

Q5R1P3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPRAECCSP KFWLVLAVLA VSGSRARSQK SPPSIGIAVI LVGTSDEVAI
60 70 80 90 100
KDAHEKDDFH HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA
110 120 130 140 150
DDTDQEAIAQ ILDFISAQTL TPILGIHGGS SMIMADKDES SMFFQFGPSI
160 170 180 190 200
EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ DFVNKIRSTI ENSFVGWELE
210 220 230 240 250
EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI FEVANSVGLT
260 270 280 290 300
GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
310 320 330 340 350
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS
360 370 380 390 400
FSEDGYQMHP KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE
410 420 430 440 450
QEDDHLSIVT LEEAPFVIVE SVDPLSGTCM RNTVPCQKRI VSENKTDEEP
460 470 480 490 500
GYIKKCCKGF CIDILKKISK SVKFTYDLYL VTNGKHGKKI NGTWNGMIGE
510 520 530 540 550
VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR SNGTVSPSAF
560 570 580 590 600
LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
610 620 630 640 650
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL
660 670 680 690 700
AAFMIQEEYV DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA
710 720 730 740 750
EMHAYMGKFN QRGVDDALLS LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT
760 770 780 790 800
IGSGKVFAST GYGIAIQKDS GWKRQVDLAI LQLFGDGEME ELEALWLTGI
810 820 830 840 850
CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH LFYWQFRHCF
860 870 880 890 900
MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
910 920 930 940 950
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN
960 970 980 990 1000
NPPCEENLFS DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSASSI
1010 1020 1030 1040 1050
DGLYDCDNPP FTTQPRSISK KPLDLGLPSS KHSQLSDLYG KFSFKSDRYS
1060 1070 1080 1090 1100
GHDDLIRSDV SDISTHTVTY GNIEGNAAKR RKQQYKDSLK KRPASAKSRR
1110 1120 1130 1140 1150
EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK ENSPHWEHVD
1160 1170 1180 1190 1200
LTDIYKEQSD DFKRDSVSGG GPCTNRSHLK HGAGDKHGVV SGVPAPWEKN
1210 1220 1230 1240 1250
LSNVDWEDRS GGNFCRSCPS KLHNYSTAVT GQNSGRQACI RCEACKKAGN
1260 1270 1280 1290 1300
LYDISEDNSL QELDQPAAPV AVPSNAPSTK YPQSPTNSKA QKKTRNKLRR
1310 1320 1330 1340 1350
QHSYDTFVDL QKEEAALAPR SVSLKDKGRF LDGSPYAHMF ETPAGESTFA
1360 1370 1380 1390 1400
NHESSVAAAG HRHHNNPGGG GYMLSKSLYP DRVTQNPFIP TFGDDQCLLH
1410 1420 1430 1440 1450
GSKSYFFRQP TVAGAPKARP DFRALVTNKP VVSALHGAVP GRFQKDICIG
1460 1470 1480
NQSNPCVPNN KNPRAFNGSS NGHVYEKLSS IESDV
Length:1,485
Mass (Da):166,244
Last modified:January 4, 2005 - v1
Checksum:i526E5868F98BDE1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195992 mRNA. Translation: BAD74215.1.
RefSeqiNP_001008719.1. NM_001008719.1.
XP_005636773.1. XM_005636716.2.
XP_013963742.1. XM_014108267.1.
XP_013963743.1. XM_014108268.1.
UniGeneiCfa.16222.

Genome annotation databases

EnsembliENSCAFT00000020886; ENSCAFP00000019393; ENSCAFG00000013148.
GeneIDi494009.
KEGGicfa:494009.

Similar proteinsi

Entry informationi

Entry nameiNMDE2_CANLF
AccessioniPrimary (citable) accession number: Q5R1P3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 4, 2005
Last modified: November 22, 2017
This is version 99 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families