NMDE2_RAT
ID NMDE2_RAT Reviewed; 1482 AA.
AC Q00960; Q62684;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
DE Short=GluN2B;
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2;
DE AltName: Full=N-methyl D-aspartate receptor subtype 2B;
DE Short=NMDAR2B;
DE Short=NR2B {ECO:0000303|PubMed:1350383};
DE Flags: Precursor;
GN Name=Grin2b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=1350383; DOI=10.1126/science.256.5060.1217;
RA Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
RA Burnashev N., Sakmann B., Seeburg P.H.;
RT "Heteromeric NMDA receptors: molecular and functional distinction of
RT subtypes.";
RL Science 256:1217-1221(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7524561; DOI=10.1016/0896-6273(94)90258-5;
RA Sullivan J.M., Traynelis S.F., Chen H.S., Escobar W., Heinemann S.F.,
RA Lipton S.A.;
RT "Identification of two cysteine residues that are required for redox
RT modulation of the NMDA subtype of glutamate receptor.";
RL Neuron 13:929-936(1994).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=7513428; DOI=10.1073/pnas.91.9.3954;
RA Moon I.S., Apperson M.L., Kennedy M.B.;
RT "The major tyrosine-phosphorylated protein in the postsynaptic density
RT fraction is N-methyl-D-aspartate receptor subunit 2B.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3954-3958(1994).
RN [4]
RP INTERACTION WITH DLG4.
RX PubMed=7569905; DOI=10.1126/science.7569905;
RA Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
RT "Domain interaction between NMDA receptor subunits and the postsynaptic
RT density protein PSD-95.";
RL Science 269:1737-1740(1995).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9509416;
RA Jin D.H., Jung Y.W., Ko B.H., Moon I.S.;
RT "Immunoblot analyses on the differential distribution of NR2A and NR2B
RT subunits in the adult rat brain.";
RL Mol. Cells 7:749-754(1997).
RN [6]
RP INTERACTION WITH PATJ.
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
RX PubMed=11588171; DOI=10.1523/jneurosci.21-20-07985.2001;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
RX PubMed=11160393; DOI=10.1523/jneurosci.21-04-01228.2001;
RA Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S.,
RA Sucher N.J., Heinemann S.F.;
RT "Assembly with the NR1 subunit is required for surface expression of NR3A-
RT containing NMDA receptors.";
RL J. Neurosci. 21:1228-1237(2001).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
RX PubMed=12391275; DOI=10.1124/mol.62.5.1119;
RA Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.;
RT "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2
RT subunits.";
RL Mol. Pharmacol. 62:1119-1127(2002).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
RX PubMed=11929923; DOI=10.1152/jn.00531.2001;
RA Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
RA Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
RA Lipton S.A.;
RT "Characterization and comparison of the NR3A subunit of the NMDA receptor
RT in recombinant systems and primary cortical neurons.";
RL J. Neurophysiol. 87:2052-2063(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886; SER-917;
RP SER-920; TYR-1039; SER-1255; SER-1259 AND SER-1303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22960932; DOI=10.1038/nn.3214;
RA Rodenas-Ruano A., Chavez A.E., Cossio M.J., Castillo P.E., Zukin R.S.;
RT "REST-dependent epigenetic remodeling promotes the developmental switch in
RT synaptic NMDA receptors.";
RL Nat. Neurosci. 15:1382-1390(2012).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND PRR7, AND INTERACTION WITH PRR7.
RX PubMed=27458189; DOI=10.15252/embj.201593070;
RA Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
RA Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
RT "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates
RT NMDA-mediated excitotoxicity.";
RL EMBO J. 35:1923-1934(2016).
RN [14]
RP INTERACTION WITH DLG3 AND DLG4, AND MUTAGENESIS OF SER-1413; LEU-1422 AND
RP SER-1450.
RX PubMed=28283559; DOI=10.1523/jneurosci.0827-16.2017;
RA Liu S., Zhou L., Yuan H., Vieira M., Sanz-Clemente A., Badger J.D. II,
RA Lu W., Traynelis S.F., Roche K.W.;
RT "A Rare Variant Identified Within the GluN2B C-Terminus in a Patient with
RT Autism Affects NMDA Receptor Surface Expression and Spine Density.";
RL J. Neurosci. 37:4093-4102(2017).
RN [15]
RP INTERACTION WITH ARC.
RX PubMed=31080121; DOI=10.1016/j.str.2019.04.001;
RA Nielsen L.D., Pedersen C.P., Erlendsson S., Teilum K.;
RT "The capsid domain of Arc changes its oligomerization propensity through
RT direct interaction with the NMDA receptor.";
RL Structure 0:0-0(2019).
RN [16] {ECO:0007744|PDB:3JPW, ECO:0007744|PDB:3JPY}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-394, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, ACTIVITY REGULATION, GLYCOSYLATION AT ASN-74 AND
RP ASN-341, MUTAGENESIS OF HIS-60; HIS-127; ASP-283; GLU-284; HIS-311 AND
RP HIS-359, AND DISULFIDE BOND.
RX PubMed=19910922; DOI=10.1038/emboj.2009.338;
RA Karakas E., Simorowski N., Furukawa H.;
RT "Structure of the zinc-bound amino-terminal domain of the NMDA receptor
RT NR2B subunit.";
RL EMBO J. 28:3910-3920(2009).
RN [17] {ECO:0007744|PDB:3QEL, ECO:0007744|PDB:3QEM}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-394, FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, ACTIVITY REGULATION, GLYCOSYLATION AT ASN-74 AND
RP ASN-341, AND DISULFIDE BONDS.
RX PubMed=21677647; DOI=10.1038/nature10180;
RA Karakas E., Simorowski N., Furukawa H.;
RT "Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA
RT receptors.";
RL Nature 475:249-253(2011).
RN [18] {ECO:0007744|PDB:4PE5}
RP X-RAY CRYSTALLOGRAPHY (3.96 ANGSTROMS) OF 27-852 IN COMPLEX WITH GRIN1 AND
RP GLUTAMATE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, GLYCOSYLATION
RP AT ASN-74; ASN-341 AND ASN-688, AND DISULFIDE BONDS.
RX PubMed=24876489; DOI=10.1126/science.1251915;
RA Karakas E., Furukawa H.;
RT "Crystal structure of a heterotetrameric NMDA receptor ion channel.";
RL Science 344:992-997(2014).
RN [19] {ECO:0007744|PDB:5B3J, ECO:0007744|PDB:5FXG, ECO:0007744|PDB:5FXH, ECO:0007744|PDB:5FXI, ECO:0007744|PDB:5FXJ, ECO:0007744|PDB:5FXK}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-394, STRUCTURE BY ELECTRON
RP MICROSCOPY (6.1 ANGSTROMS) OF 27-852 IN COMPLEX WITH GRIN1, FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND DISULFIDE BONDS.
RX PubMed=27135925; DOI=10.1038/nature17679;
RA Tajima N., Karakas E., Grant T., Simorowski N., Diaz-Avalos R.,
RA Grigorieff N., Furukawa H.;
RT "Activation of NMDA receptors and the mechanism of inhibition by
RT ifenprodil.";
RL Nature 534:63-68(2016).
RN [20] {ECO:0007744|PDB:5TPZ}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 32-393 IN COMPLEX WITH GRIN1,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-341, AND
RP DISULFIDE BONDS.
RX PubMed=27916457; DOI=10.1016/j.neuron.2016.11.006;
RA Romero-Hernandez A., Simorowski N., Karakas E., Furukawa H.;
RT "Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition
RT in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.";
RL Neuron 92:1324-1336(2016).
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:1350383, PubMed:19910922, PubMed:21677647, PubMed:24876489,
CC PubMed:27135925, PubMed:27916457). Sensitivity to glutamate and channel
CC kinetics depend on the subunit composition (Probable). In concert with
CC DAPK1 at extrasynaptic sites, acts as a central mediator for stroke
CC damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
CC receptor channel activity inducing injurious Ca2+ influx through them,
CC resulting in an irreversible neuronal death. Contributes to neural
CC pattern formation in the developing brain. Plays a role in long-term
CC depression (LTD) of hippocampus membrane currents and in synaptic
CC plasticity (By similarity). {ECO:0000250|UniProtKB:Q01097,
CC ECO:0000269|PubMed:1350383, ECO:0000269|PubMed:19910922,
CC ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:24876489,
CC ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27916457, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by micromolar levels
CC of zinc ions (PubMed:19910922). Channel activity is inhibited by
CC ifenprodil (PubMed:19910922, PubMed:21677647).
CC {ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647}.
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:1350383, PubMed:19910922,
CC PubMed:21677647, PubMed:24876489, PubMed:27135925, PubMed:27916457).
CC Can also form heterotetrameric channels that contain at least one zeta
CC subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B.
CC In vivo, the subunit composition may depend on the expression levels of
CC the different subunits. Found in a complex with GRIN1, GRIN3A and
CC PPP2CB. Found in a complex with GRIN1 and GRIN3B. Interacts with MAGI3.
CC Interacts with HIP1 and NETO1. Interacts with PDZ domains of PATJ, DLG3
CC and DLG4. Interacts with DAPK1 (By similarity). Found in a complex with
CC GRIN1 and PRR7 (PubMed:27458189). Interacts with PRR7
CC (PubMed:27458189). Interacts with CAMK2A (By similarity). Interacts
CC with ARC; preventing ARC oligomerization (PubMed:31080121). Interacts
CC with TMEM25 (By similarity). {ECO:0000250|UniProtKB:Q01097,
CC ECO:0000250|UniProtKB:Q13224, ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647,
CC ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:27916457,
CC ECO:0000269|PubMed:28283559, ECO:0000269|PubMed:31080121}.
CC -!- INTERACTION:
CC Q00960; P11275: Camk2a; NbExp=2; IntAct=EBI-396905, EBI-2640645;
CC Q00960; Q62936: Dlg3; NbExp=6; IntAct=EBI-396905, EBI-349596;
CC Q00960; P31016: Dlg4; NbExp=8; IntAct=EBI-396905, EBI-375655;
CC Q00960; P35439: Grin1; NbExp=12; IntAct=EBI-396905, EBI-877897;
CC Q00960; P35439-7: Grin1; NbExp=2; IntAct=EBI-396905, EBI-15932497;
CC Q00960; Q460M5: Lrfn2; NbExp=2; IntAct=EBI-396905, EBI-877185;
CC Q00960; P11798: Camk2a; Xeno; NbExp=4; IntAct=EBI-396905, EBI-400384;
CC Q00960; A0A1L8F5J9-8: grin1; Xeno; NbExp=6; IntAct=EBI-396905, EBI-16582829;
CC Q00960; Q8R4I7: Neto1; Xeno; NbExp=2; IntAct=EBI-396905, EBI-2314926;
CC Q00960; Q63ZW7: Patj; Xeno; NbExp=4; IntAct=EBI-396905, EBI-8366894;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647,
CC ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:27916457}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:7513428,
CC ECO:0000269|PubMed:9509416}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Late
CC endosome {ECO:0000250|UniProtKB:Q01097}. Lysosome
CC {ECO:0000250|UniProtKB:Q01097}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q01097}. Note=Co-localizes with the motor
CC protein KIF17 along microtubules. {ECO:0000250|UniProtKB:Q01097}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus including the dentate
CC gyrus (at protein level) (PubMed:22960932). Detected in adult olfactory
CC bulb, brain cortex, hippocampus, striatum, thalamus, superior
CC colliculus, with much lower levels in inferior colliculus, midbrain and
CC cerebellum. {ECO:0000269|PubMed:22960932, ECO:0000269|PubMed:9509416}.
CC -!- DEVELOPMENTAL STAGE: Expressed during postnatal days P3 to P60, with
CC decreased expression after postnatal day 14.
CC {ECO:0000269|PubMed:22960932}.
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:24876489}.
CC -!- PTM: Phosphorylated on tyrosine residues (PubMed:7513428).
CC Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor
CC channel activity (By similarity). {ECO:0000250|UniProtKB:Q01097,
CC ECO:0000269|PubMed:7513428}.
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; M91562; AAA41714.1; -; mRNA.
DR EMBL; U11419; AAA50554.1; -; mRNA.
DR PIR; B43274; B43274.
DR RefSeq; NP_036706.1; NM_012574.1.
DR PDB; 3JPW; X-ray; 2.80 A; A=32-394.
DR PDB; 3JPY; X-ray; 3.21 A; A=32-394.
DR PDB; 3QEL; X-ray; 2.60 A; B/D=31-394.
DR PDB; 3QEM; X-ray; 3.00 A; B/D=31-394.
DR PDB; 4PE5; X-ray; 3.96 A; B/D=27-852.
DR PDB; 5B3J; X-ray; 2.90 A; C/D=31-394.
DR PDB; 5FXG; EM; 6.80 A; B/D=27-852.
DR PDB; 5FXH; EM; 6.10 A; B/D=27-852.
DR PDB; 5FXI; EM; 6.40 A; B/D=27-852.
DR PDB; 5FXJ; EM; 6.50 A; B/D=27-852.
DR PDB; 5FXK; EM; 6.40 A; B/D=27-852.
DR PDB; 5TPZ; X-ray; 3.10 A; D=32-393.
DR PDB; 6CNA; EM; 4.60 A; B/D=34-843.
DR PDB; 6E7R; X-ray; 2.10 A; B/D=32-394.
DR PDB; 6E7S; X-ray; 2.72 A; B/D=32-394.
DR PDB; 6E7T; X-ray; 2.31 A; B/D=32-393.
DR PDB; 6E7U; X-ray; 2.27 A; B/D=32-394.
DR PDB; 6E7V; X-ray; 2.60 A; B/D=32-394.
DR PDB; 6E7W; X-ray; 2.67 A; B/D=32-394.
DR PDB; 6E7X; X-ray; 2.58 A; B/D=32-394.
DR PDB; 6WHR; EM; 3.99 A; B/D=27-852.
DR PDB; 6WHS; EM; 4.00 A; B/D=27-852.
DR PDB; 6WHT; EM; 4.39 A; B/D=27-852.
DR PDB; 6WHU; EM; 3.93 A; B/D=27-852.
DR PDB; 6WHV; EM; 4.05 A; B/D=27-852.
DR PDB; 6WHW; EM; 4.09 A; B/D=25-852.
DR PDB; 6WHX; EM; 4.09 A; B/D=25-852.
DR PDB; 6WHY; EM; 4.03 A; B/D=25-852.
DR PDB; 6WI0; EM; 4.27 A; B/D=27-852.
DR PDB; 6WI1; EM; 3.62 A; B/D=25-852.
DR PDB; 7TE6; X-ray; 4.55 A; B/F=31-394.
DR PDB; 7TE9; EM; 3.92 A; B/D=31-852.
DR PDB; 7TEB; EM; 4.23 A; B/D=27-852.
DR PDB; 7TEE; EM; 6.59 A; B/D=27-852.
DR PDB; 7TEQ; EM; 7.51 A; B/D=27-852.
DR PDB; 7TER; EM; 5.23 A; B/D=27-852.
DR PDB; 7TES; EM; 4.70 A; B/D=27-852.
DR PDB; 7TET; EM; 4.45 A; B/D=27-852.
DR PDBsum; 3JPW; -.
DR PDBsum; 3JPY; -.
DR PDBsum; 3QEL; -.
DR PDBsum; 3QEM; -.
DR PDBsum; 4PE5; -.
DR PDBsum; 5B3J; -.
DR PDBsum; 5FXG; -.
DR PDBsum; 5FXH; -.
DR PDBsum; 5FXI; -.
DR PDBsum; 5FXJ; -.
DR PDBsum; 5FXK; -.
DR PDBsum; 5TPZ; -.
DR PDBsum; 6CNA; -.
DR PDBsum; 6E7R; -.
DR PDBsum; 6E7S; -.
DR PDBsum; 6E7T; -.
DR PDBsum; 6E7U; -.
DR PDBsum; 6E7V; -.
DR PDBsum; 6E7W; -.
DR PDBsum; 6E7X; -.
DR PDBsum; 6WHR; -.
DR PDBsum; 6WHS; -.
DR PDBsum; 6WHT; -.
DR PDBsum; 6WHU; -.
DR PDBsum; 6WHV; -.
DR PDBsum; 6WHW; -.
DR PDBsum; 6WHX; -.
DR PDBsum; 6WHY; -.
DR PDBsum; 6WI0; -.
DR PDBsum; 6WI1; -.
DR PDBsum; 7TE6; -.
DR PDBsum; 7TE9; -.
DR PDBsum; 7TEB; -.
DR PDBsum; 7TEE; -.
DR PDBsum; 7TEQ; -.
DR PDBsum; 7TER; -.
DR PDBsum; 7TES; -.
DR PDBsum; 7TET; -.
DR AlphaFoldDB; Q00960; -.
DR SMR; Q00960; -.
DR BioGRID; 246575; 23.
DR ComplexPortal; CPX-284; NMDA receptor complex, GluN1-GluN2B.
DR ComplexPortal; CPX-295; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; Q00960; -.
DR DIP; DIP-33702N; -.
DR IntAct; Q00960; 20.
DR MINT; Q00960; -.
DR STRING; 10116.ENSRNOP00000011697; -.
DR BindingDB; Q00960; -.
DR ChEMBL; CHEMBL311; -.
DR DrugCentral; Q00960; -.
DR GuidetoPHARMACOLOGY; 457; -.
DR TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q00960; 7 sites, 11 N-linked glycans (1 site).
DR iPTMnet; Q00960; -.
DR PhosphoSitePlus; Q00960; -.
DR SwissPalm; Q00960; -.
DR PaxDb; Q00960; -.
DR PRIDE; Q00960; -.
DR ABCD; Q00960; 6 sequenced antibodies.
DR GeneID; 24410; -.
DR KEGG; rno:24410; -.
DR UCSC; RGD:2738; rat.
DR CTD; 2904; -.
DR RGD; 2738; Grin2b.
DR eggNOG; KOG1053; Eukaryota.
DR InParanoid; Q00960; -.
DR PhylomeDB; Q00960; -.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-RNO-9609736; Assembly and cell surface presentation of NMDA receptors.
DR EvolutionaryTrace; Q00960; -.
DR PRO; PR:Q00960; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0044307; C:dendritic branch; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0043083; C:synaptic cleft; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0008013; F:beta-catenin binding; IPI:RGD.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; ISO:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IPI:RGD.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0036094; F:small molecule binding; IPI:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0001508; P:action potential; IMP:RGD.
DR GO; GO:0008306; P:associative learning; IMP:RGD.
DR GO; GO:0001662; P:behavioral fear response; IMP:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IC:ComplexPortal.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
DR GO; GO:0071386; P:cellular response to corticosterone stimulus; IEP:RGD.
DR GO; GO:1904644; P:cellular response to curcumin; IEP:RGD.
DR GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
DR GO; GO:1904322; P:cellular response to forskolin; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
DR GO; GO:0010350; P:cellular response to magnesium starvation; IEP:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0042596; P:fear response; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
DR GO; GO:0007616; P:long-term memory; IEP:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0007613; P:memory; IDA:UniProtKB.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISO:RGD.
DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; IMP:SynGO.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IGI:ARUK-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:ComplexPortal.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IDA:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:ComplexPortal.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IDA:RGD.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; IC:ComplexPortal.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IC:ComplexPortal.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0051597; P:response to methylmercury; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IMP:RGD.
DR GO; GO:0051707; P:response to other organism; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IDA:RGD.
DR GO; GO:0046960; P:sensitization; IMP:RGD.
DR GO; GO:0007423; P:sensory organ development; ISO:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0001967; P:suckling behavior; ISO:RGD.
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; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Lysosome; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
KW Receptor; Reference proteome; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1482
FT /note="Glutamate receptor ionotropic, NMDA 2B"
FT /id="PRO_0000011579"
FT TOPO_DOM 27..557
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 558..576
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 577..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT INTRAMEM 604..623
FT /note="Discontinuously helical"
FT /evidence="ECO:0000305|PubMed:24876489"
FT TOPO_DOM 624..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 631..646
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 647..817
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 818..837
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 838..1482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT REGION 604..623
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0000305|PubMed:24876489"
FT REGION 1161..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1304
FT /note="Interaction with DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOTIF 1480..1482
FT /note="PDZ-binding"
FT COMPBIAS 1269..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19910922,
FT ECO:0007744|PDB:3JPY"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:19910922,
FT ECO:0007744|PDB:3JPY"
FT BINDING 514
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT BINDING 519
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT BINDING 690..691
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0007744|PDB:4PE5"
FT BINDING 732
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT SITE 615
FT /note="Functional determinant of NMDA receptors"
FT /evidence="ECO:0000250"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 962
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1039
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1109
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1472
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01097"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19910922,
FT ECO:0000269|PubMed:24876489, ECO:0007744|PDB:3JPW,
FT ECO:0007744|PDB:3JPY, ECO:0007744|PDB:3QEL,
FT ECO:0007744|PDB:3QEM, ECO:0007744|PDB:4PE5"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19910922,
FT ECO:0000269|PubMed:24876489, ECO:0007744|PDB:3JPW,
FT ECO:0007744|PDB:3JPY, ECO:0007744|PDB:3QEL,
FT ECO:0007744|PDB:3QEM, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PDB:5TPZ"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT DISULFID 86..321
FT /evidence="ECO:0000269|PubMed:19910922,
FT ECO:0007744|PDB:3JPW, ECO:0007744|PDB:3JPY,
FT ECO:0007744|PDB:3QEL, ECO:0007744|PDB:3QEM,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PDB:5B3J,
FT ECO:0007744|PDB:5TPZ"
FT DISULFID 429..456
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT DISULFID 436..457
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT DISULFID 746..801
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT MUTAGEN 60
FT /note="H->A: Normal zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 127
FT /note="H->A: Reduced zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 283
FT /note="D->A: Slightly reduced zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 284
FT /note="E->A: Reduced zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 311
FT /note="H->A: Normal zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 359
FT /note="H->A: Normal zinc binding."
FT /evidence="ECO:0000269|PubMed:19910922"
FT MUTAGEN 1413
FT /note="S->L: Decreased localization to the cell membrane.
FT Decreased interaction with DLG3 and DLG4. No effect on
FT glutamate-gated calcium ion channel activity."
FT /evidence="ECO:0000269|PubMed:28283559"
FT MUTAGEN 1422
FT /note="L->F: No effect on localizationto the cell membrane.
FT Decreased interaction with DLG3 and DLG4. No effect on
FT glutamate-gated calcium ion channel activity."
FT /evidence="ECO:0000269|PubMed:28283559"
FT MUTAGEN 1450
FT /note="S->F: No effect on localizationto the cell membrane.
FT Decreased interaction with DLG3 and DLG4. No effect on
FT glutamate-gated calcium ion channel activity."
FT /evidence="ECO:0000269|PubMed:28283559"
FT CONFLICT 1256
FT /note="E -> K (in Ref. 2; AAA50554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1430..1431
FT /note="VT -> SA (in Ref. 2; AAA50554)"
FT /evidence="ECO:0000305"
FT STRAND 34..44
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3QEL"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5B3J"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5TPZ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5TPZ"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 289..311
FT /evidence="ECO:0007829|PDB:6E7R"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5TPZ"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3JPY"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6E7R"
SQ SEQUENCE 1482 AA; 166071 MW; AEF8B9DF3C1B0D5D CRC64;
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI KDAHEKDDFH
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA DDTDQEAIAQ ILDFISAQTL
TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ
DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI
FEVANSVGLT GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP
KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE
SVDPLSGTCM RNTVPCQKRI ISENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL
VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI
LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH
LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS
DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI DGLYDCDNPP FTTQPRSISK
KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR
RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK
ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGEKHGVV GGVPAPWEKN
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
