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Glutamate receptor ionotropic, NMDA 1 (GluN1) (Glutamate [NMDA] receptor subunit zeta-1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1)

 NMDZ1_RAT               Reviewed;         938 AA.
P35439; Q62646;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 199.
RecName: Full=Glutamate receptor ionotropic, NMDA 1;
Short=GluN1;
AltName: Full=Glutamate [NMDA] receptor subunit zeta-1;
AltName: Full=N-methyl-D-aspartate receptor subunit NR1 {ECO:0000303|PubMed:1350383};
Short=NMD-R1;
Flags: Precursor;
Name=Grin1; Synonyms=Nmdar1 {ECO:0000303|PubMed:1834949};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=1834949; DOI=10.1038/354031a0;
Moriyoshi K., Masu M., Ishii T., Shigemoto R., Mizuno N.,
Nakanishi S.;
"Molecular cloning and characterization of the rat NMDA receptor.";
Nature 354:31-37(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1386026; DOI=10.1016/0014-5793(92)80648-Z;
Anantharam V., Panchal R., Wilson A., Koltchin V.V., Treistman S.N.,
Bayley H.;
"Combinatorial RNA splicing alters the surface charge on the NMDA
receptor.";
FEBS Lett. 305:27-30(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), ALTERNATIVE SPLICING,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1388270; DOI=10.1073/pnas.89.18.8552;
Nakanishi N., Axel R., Shneider N.A.;
"Alternative splicing generates functionally distinct N-methyl-D-
aspartate receptors.";
Proc. Natl. Acad. Sci. U.S.A. 89:8552-8556(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Forebrain;
PubMed=7684237; DOI=10.1016/0896-6273(93)90209-A;
Hollmann M., Boulter J., Maron C., Beasley L., Sullivan J., Pecht G.,
Heinemann S.F.;
"Zinc potentiates agonist-induced currents at certain splice variants
of the NMDA receptor.";
Neuron 10:943-954(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8399301; DOI=10.1016/0005-2736(93)90249-Y;
Bai G., Kusiak J.W.;
"Cloning and analysis of the 5' flanking sequence of the rat N-methyl-
D-aspartate receptor 1 (NMDAR1) gene.";
Biochim. Biophys. Acta 1152:197-200(1993).
[6]
ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1352681; DOI=10.1016/0006-291X(92)91701-Q;
Sugihara H., Moriyoshi K., Ishii T., Masu M., Nakanishi S.;
"Structures and properties of seven isoforms of the NMDA receptor
generated by alternative splicing.";
Biochem. Biophys. Res. Commun. 185:826-832(1992).
[7]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=1350383; DOI=10.1126/science.256.5060.1217;
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
Burnashev N., Sakmann B., Seeburg P.H.;
"Heteromeric NMDA receptors: molecular and functional distinction of
subtypes.";
Science 256:1217-1221(1992).
[8]
SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8428958;
Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H.,
Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
"Molecular characterization of the family of the N-methyl-D-aspartate
receptor subunits.";
J. Biol. Chem. 268:2836-2843(1993).
[9]
PHOSPHORYLATION AT SER-897, DEPHOSPHORYLATION BY PPP2CB, AND
IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B; GRIN3A AND PPP2CB.
PubMed=11588171;
Chan S.F., Sucher N.J.;
"An NMDA receptor signaling complex with protein phosphatase 2A.";
J. Neurosci. 21:7985-7992(2001).
[10]
CHARACTERIZATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN2A OR
GRIN2B AND GRIN3A.
PubMed=11160393;
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A.,
Trimmer J.S., Sucher N.J., Heinemann S.F.;
"Assembly with the NR1 subunit is required for surface expression of
NR3A-containing NMDA receptors.";
J. Neurosci. 21:1228-1237(2001).
[11]
IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
PubMed=12391275; DOI=10.1124/mol.62.5.1119;
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B.,
Yasuda R.P.;
"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and
NR2 subunits.";
Mol. Pharmacol. 62:1119-1127(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
PubMed=11929923; DOI=10.1152/jn.00531.2001;
Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
Lipton S.A.;
"Characterization and comparison of the NR3A subunit of the NMDA
receptor in recombinant systems and primary cortical neurons.";
J. Neurophysiol. 87:2052-2063(2002).
[13]
INTERACTION WITH MPDZ AND DLG4.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
activity and NMDA receptor-dependent synaptic AMPA receptor
potentiation.";
Neuron 43:563-574(2004).
[14]
PHOSPHORYLATION AT SER-890.
PubMed=15936117; DOI=10.1016/j.neuint.2005.04.011;
Sanchez-Perez A.M., Felipo V.;
"Serines 890 and 896 of the NMDA receptor subunit NR1 are
differentially phosphorylated by protein kinase C isoforms.";
Neurochem. Int. 47:84-91(2005).
[15]
INTERACTION WITH LRFN2.
PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
Wenthold R.J.;
"A novel family of adhesion-like molecules that interacts with the
NMDA receptor.";
J. Neurosci. 26:2174-2183(2006).
[16]
INTERACTION WITH LRFN1.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
Kaang B.-K., Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the
differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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).
[18]
INTERACTION WITH MYZAP.
PubMed=18849881; DOI=10.1097/WNR.0b013e328317f05f;
Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
Yang J.;
"GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit
and reduces N-methyl D-aspartate toxicity.";
NeuroReport 19:1721-1726(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877 (ISOFORM E),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898 (ISOFORM G), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[20]
IDENTIFICATION IN COMPLEX WITH DLG4 AND PRR7, IDENTIFICATION IN A
COMPLEX WITH GRIN2B AND PRR7, AND INTERACTION WITH PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26912815; DOI=10.1124/mol.115.103036;
Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M.,
Sciabola S., Mony L., Paoletti P., Pandit J.;
"A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor
GluN2B-selective Antagonists.";
Mol. Pharmacol. 89:541-551(2016).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=28384476; DOI=10.1016/j.neuron.2017.03.018;
Sun W., Hansen K.B., Jahr C.E.;
"Allosteric Interactions between NMDA Receptor Subunits Shape the
Developmental Shift in Channel Properties.";
Neuron 94:58-64(2017).
[23] {ECO:0000244|PDB:1PB7, ECO:0000244|PDB:1PB8, ECO:0000244|PDB:1PB9, ECO:0000244|PDB:1PBQ}
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 394-800 IN COMPLEXES WITH
AGONIST SERINE AND ANTAGONIST, AND DISULFIDE BOND.
PubMed=12805203; DOI=10.1093/emboj/cdg303;
Furukawa H., Gouaux E.;
"Mechanisms of activation, inhibition and specificity: crystal
structures of the NMDA receptor NR1 ligand-binding core.";
EMBO J. 22:2873-2885(2003).
[24] {ECO:0000244|PDB:2A5T}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 394-800 IN COMPLEX WITH
GRIN2A; GLYCINE AND GLUTAMATE, SUBUNIT, AND DISULFIDE BOND.
PubMed=16281028; DOI=10.1038/nature04089;
Furukawa H., Singh S.K., Mancusso R., Gouaux E.;
"Subunit arrangement and function in NMDA receptors.";
Nature 438:185-192(2005).
[25] {ECO:0000244|PDB:1Y1M, ECO:0000244|PDB:1Y1Z, ECO:0000244|PDB:1Y20}
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 394-800 IN COMPLEXES WITH
AGONISTS, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BOND.
PubMed=15996549; DOI=10.1016/j.neuron.2005.05.022;
Inanobe A., Furukawa H., Gouaux E.;
"Mechanism of partial agonist action at the NR1 subunit of NMDA
receptors.";
Neuron 47:71-84(2005).
[26] {ECO:0000244|PDB:3Q41}
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 21-393, SUBUNIT, SUBCELLULAR
LOCATION, GLYCOSYLATION AT ASN-61; ASN-203; ASN-239; ASN-276 AND
ASN-368, AND DISULFIDE BONDS.
PubMed=21389213; DOI=10.1523/JNEUROSCI.6041-10.2011;
Farina A.N., Blain K.Y., Maruo T., Kwiatkowski W., Choe S.,
Nakagawa T.;
"Separation of domain contacts is required for heterotetrameric
assembly of functional NMDA receptors.";
J. Neurosci. 31:3565-3579(2011).
[27] {ECO:0000244|PDB:4PE5}
X-RAY CRYSTALLOGRAPHY (3.96 ANGSTROMS) OF 23-847 IN COMPLEX WITH
GRIN2B; GLYCINE AND ALLOSTERIC INHIBITOR, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-203; ASN-276;
ASN-300; ASN-368 AND ASN-440, AND DISULFIDE BONDS.
PubMed=24876489; DOI=10.1126/science.1251915;
Karakas E., Furukawa H.;
"Crystal structure of a heterotetrameric NMDA receptor ion channel.";
Science 344:992-997(2014).
[28] {ECO:0000244|PDB:5FXG, ECO:0000244|PDB:5FXH, ECO:0000244|PDB:5FXI, ECO:0000244|PDB:5FXJ, ECO:0000244|PDB:5FXK}
STRUCTURE BY ELECTRON MICROSCOPY (6.10 ANGSTROMS) OF 23-847 IN COMPLEX
WITH GRIN2A, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
PubMed=27135925; DOI=10.1038/nature17679;
Tajima N., Karakas E., Grant T., Simorowski N., Diaz-Avalos R.,
Grigorieff N., Furukawa H.;
"Activation of NMDA receptors and the mechanism of inhibition by
ifenprodil.";
Nature 534:63-68(2016).
[29] {ECO:0000244|PDB:5I56, ECO:0000244|PDB:5I57, ECO:0000244|PDB:5I58, ECO:0000244|PDB:5I59, ECO:0000244|PDB:5JTY}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 394-544 AND 663-800 IN
COMPLEXES WITH GLYCINE AND GRIN2A, FUNCTION, SUBCELLULAR LOCATION,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=27618671; DOI=10.1016/j.neuron.2016.08.014;
Yi F., Mou T.C., Dorsett K.N., Volkmann R.A., Menniti F.S.,
Sprang S.R., Hansen K.B.;
"Structural Basis for Negative Allosteric Modulation of GluN2A-
Containing NMDA Receptors.";
Neuron 91:1316-1329(2016).
[30] {ECO:0000244|PDB:5U8C}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 394-544 AND 663-800 IN
COMPLEX WITH GRIN2A AND SYNTHETIC ANTAGONIST, FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND DISULFIDE BONDS.
PubMed=28468946; DOI=10.1124/mol.116.107912;
Romero-Hernandez A., Furukawa H.;
"Novel Mode of Antagonist Binding in NMDA Receptors Revealed by the
Crystal Structure of the GluN1-GluN2A Ligand-Binding Domain Complexed
to NVP-AAM077.";
Mol. Pharmacol. 92:22-29(2017).
[31] {ECO:0000244|PDB:5DEX, ECO:0000244|PDB:5VIH, ECO:0000244|PDB:5VII, ECO:0000244|PDB:5VIJ}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 394-544 AND 663-800 IN
COMPLEX WITH GRIN2A AND GLYCINE, AND DISULFIDE BONDS.
Mou T.C., Sprang S.R., Hansen K.B.;
"Crystal structure of GluN1/GluN2A NMDA receptor agonist binding
domains with glycine and antagonist, phenyl-ACEPC.";
Submitted (APR-2017) to the PDB data bank.
-!- 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:1350383, PubMed:1834949,
PubMed:1388270, PubMed:8428958, PubMed:18177891, PubMed:28384476,
PubMed:15996549, PubMed:24876489, PubMed:27135925,
PubMed:27618671, PubMed:28468946). Sensitivity to glutamate and
channel kinetics depend on the subunit composition
(PubMed:28384476). {ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549,
ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949,
ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:28384476,
ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:8428958}.
-!- 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:28384476, PubMed:16281028, PubMed:15996549,
PubMed:21389213, PubMed:24876489, PubMed:27135925,
PubMed:28468946, Ref.31). Can also form heterotetrameric channels
that contain at least one zeta subunit (GRIN1), an epsilon
subunit, plus GRIN3A or GRIN3B (in vitro) (PubMed:11160393,
PubMed:11929923, PubMed:12391275). In vivo, the subunit
composition may vary in function of the expression levels of the
different subunits (Probable). Found in a complex with GRIN2A or
GRIN2B, GRIN3A and PPP2CB (PubMed:11588171). Found in a complex
with GRIN2A or GRIN2B and GRIN3B (By similarity). Interacts with
SNX27 (via PDZ domain); the interaction is required for recycling
to the plasma membrane when endocytosed and prevent degradation in
lysosomes (By similarity). Interacts with DLG4 and MPDZ
(PubMed:15312654). Interacts with LRFN1 and LRFN2
(PubMed:16495444, PubMed:16630835). Interacts with MYZAP
(PubMed:18849881). Found in a complex with DLG4 and PRR7
(PubMed:27458189). Found in a complex with GRIN2B and PRR7
(PubMed:27458189). Interacts with PRR7; the interaction is reduced
following NMDA receptor activity (PubMed:27458189).
{ECO:0000250|UniProtKB:P35438, ECO:0000269|PubMed:11160393,
ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:11929923,
ECO:0000269|PubMed:12391275, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15996549,
ECO:0000269|PubMed:16281028, ECO:0000269|PubMed:16495444,
ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:18177891,
ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:21389213,
ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
ECO:0000269|PubMed:8428958, ECO:0000269|Ref.31, ECO:0000305}.
-!- INTERACTION:
P31016:Dlg4; NbExp=4; IntAct=EBI-877897, EBI-375655;
Q00960:Grin2b; NbExp=12; IntAct=EBI-877897, EBI-396905;
Q460M5:Lrfn2; NbExp=2; IntAct=EBI-877897, EBI-877185;
Q80TG9:Lrfn2 (xeno); NbExp=2; IntAct=EBI-877897, EBI-877092;
Q9JJ40:Pdzk1; NbExp=3; IntAct=EBI-877897, EBI-7713572;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549,
ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949,
ECO:0000269|PubMed:21389213, ECO:0000269|PubMed:24876489,
ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27618671,
ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
ECO:0000269|PubMed:8428958}; Multi-pass membrane protein
{ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Cell
junction, synapse, postsynaptic cell membrane {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Note=Enriched in postsynaptic plasma
membrane and postsynaptic densities. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=A;
IsoId=P35439-1; Sequence=Displayed;
Name=B;
IsoId=P35439-2; Sequence=VSP_000140;
Name=C; Synonyms=NMDAR1-2a subunit;
IsoId=P35439-3; Sequence=VSP_000141;
Name=D;
IsoId=P35439-4; Sequence=VSP_000144;
Name=E;
IsoId=P35439-5; Sequence=VSP_000142, VSP_000143;
Note=Contains a phosphoserine at position 877.
{ECO:0000244|PubMed:22673903};
Name=F; Synonyms=NMDAR1-2b subunit;
IsoId=P35439-6; Sequence=VSP_000140, VSP_000141;
Name=G; Synonyms=NMDAR1-4b subunit;
IsoId=P35439-7; Sequence=VSP_000140, VSP_000142, VSP_000143;
Note=Contains a phosphoserine at position 898.
{ECO:0000244|PubMed:22673903};
-!- TISSUE SPECIFICITY: Detected throughout the brain, in brain
cortex, cerebellum, thalamus and olfactory bulb.
{ECO:0000269|PubMed:1350383}.
-!- 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:0000250|UniProtKB:A0A1L8F5J9}.
-!- PTM: NMDA is probably regulated by C-terminal phosphorylation of
an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by
protein phosphatase 2A (PPP2CB). Its phosphorylated state is
influenced by the formation of the NMDAR-PPP2CB complex and the
NMDAR channel activity. {ECO:0000269|PubMed:11588171,
ECO:0000269|PubMed:15936117}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR1/GRIN1 subfamily. {ECO:0000305}.
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EMBL; X63255; CAA44914.1; -; mRNA.
EMBL; AY157515; AAA16366.1; -; Genomic_DNA.
EMBL; X65227; CAA46335.1; -; mRNA.
EMBL; U08261; AAB50926.1; -; mRNA.
EMBL; U08262; AAB50927.1; -; mRNA.
EMBL; U08263; AAB50928.1; -; mRNA.
EMBL; U08264; AAB50929.1; -; mRNA.
EMBL; U08265; AAB50930.1; -; mRNA.
EMBL; U08267; AAB50932.1; -; mRNA.
EMBL; U08268; AAB50933.1; -; mRNA.
EMBL; S39217; AAB22431.1; -; mRNA.
EMBL; S39218; AAB22432.1; -; mRNA.
EMBL; S39219; AAB22433.1; -; mRNA.
EMBL; S39220; AAB22434.1; -; mRNA.
EMBL; S39221; AAB22435.1; -; mRNA.
PIR; JN0336; JN0336.
PIR; JN0337; JN0337.
PIR; JN0338; JN0338.
PIR; JN0339; JN0339.
PIR; JN0340; JN0340.
PIR; JN0341; JN0341.
PIR; JN0342; JN0342.
PIR; S19710; S19710.
RefSeq; NP_001257531.1; NM_001270602.1. [P35439-2]
RefSeq; NP_001257532.1; NM_001270603.1. [P35439-6]
RefSeq; NP_001257534.1; NM_001270605.1. [P35439-3]
RefSeq; NP_001257537.1; NM_001270608.1. [P35439-7]
RefSeq; NP_001257539.1; NM_001270610.1. [P35439-5]
RefSeq; NP_001274352.1; NM_001287423.1. [P35439-4]
RefSeq; NP_058706.1; NM_017010.2. [P35439-1]
UniGene; Rn.9840; -.
PDB; 1PB7; X-ray; 1.35 A; A=394-544, A=663-800.
PDB; 1PB8; X-ray; 1.45 A; A=394-544, A=663-800.
PDB; 1PB9; X-ray; 1.60 A; A=394-544, A=663-800.
PDB; 1PBQ; X-ray; 1.90 A; A/B=394-544, A/B=663-800.
PDB; 1Y1M; X-ray; 1.80 A; A/B=394-544, A/B=663-800.
PDB; 1Y1Z; X-ray; 1.50 A; A=394-544, A=663-800.
PDB; 1Y20; X-ray; 1.40 A; A=394-544, A=663-800.
PDB; 2A5T; X-ray; 2.00 A; A=394-544.
PDB; 3Q41; X-ray; 3.40 A; A/B/C=21-393.
PDB; 4KCC; X-ray; 1.89 A; A=394-544, A=663-800.
PDB; 4KFQ; X-ray; 2.20 A; A/B=394-544, A/B=663-800.
PDB; 4NF4; X-ray; 2.00 A; A=394-544, A=663-800.
PDB; 4NF5; X-ray; 1.90 A; A=394-544, A=663-800.
PDB; 4NF6; X-ray; 2.10 A; A=394-544, A=663-800.
PDB; 4NF8; X-ray; 1.86 A; A=394-544, A=663-800.
PDB; 4PE5; X-ray; 3.96 A; A/C=23-847.
PDB; 5DEX; X-ray; 2.40 A; A=394-544, A=663-800.
PDB; 5FXG; EM; 6.80 A; A/C=23-863.
PDB; 5FXH; EM; 6.10 A; A/C=23-863.
PDB; 5FXI; EM; 6.40 A; A/C=23-863.
PDB; 5FXJ; EM; 6.50 A; A/C=23-863.
PDB; 5FXK; EM; 6.40 A; A/C=23-863.
PDB; 5I56; X-ray; 2.28 A; A=394-544, A=663-800.
PDB; 5I57; X-ray; 1.70 A; A=394-544, A=684-821.
PDB; 5I58; X-ray; 2.52 A; A=394-544, A=663-800.
PDB; 5I59; X-ray; 2.25 A; A=394-544, A=663-800.
PDB; 5JTY; X-ray; 2.72 A; A=394-544, A=684-821.
PDB; 5U8C; X-ray; 1.60 A; A=394-544, A=663-800.
PDB; 5VIH; X-ray; 2.40 A; A=394-544, A=663-800.
PDB; 5VII; X-ray; 1.95 A; A=394-544, A=663-800.
PDB; 5VIJ; X-ray; 2.10 A; A=394-544, A=663-800.
PDBsum; 1PB7; -.
PDBsum; 1PB8; -.
PDBsum; 1PB9; -.
PDBsum; 1PBQ; -.
PDBsum; 1Y1M; -.
PDBsum; 1Y1Z; -.
PDBsum; 1Y20; -.
PDBsum; 2A5T; -.
PDBsum; 3Q41; -.
PDBsum; 4KCC; -.
PDBsum; 4KFQ; -.
PDBsum; 4NF4; -.
PDBsum; 4NF5; -.
PDBsum; 4NF6; -.
PDBsum; 4NF8; -.
PDBsum; 4PE5; -.
PDBsum; 5DEX; -.
PDBsum; 5FXG; -.
PDBsum; 5FXH; -.
PDBsum; 5FXI; -.
PDBsum; 5FXJ; -.
PDBsum; 5FXK; -.
PDBsum; 5I56; -.
PDBsum; 5I57; -.
PDBsum; 5I58; -.
PDBsum; 5I59; -.
PDBsum; 5JTY; -.
PDBsum; 5U8C; -.
PDBsum; 5VIH; -.
PDBsum; 5VII; -.
PDBsum; 5VIJ; -.
ProteinModelPortal; P35439; -.
SMR; P35439; -.
BioGrid; 246573; 7.
CORUM; P35439; -.
DIP; DIP-674N; -.
IntAct; P35439; 17.
MINT; MINT-101336; -.
STRING; 10116.ENSRNOP00000029227; -.
BindingDB; P35439; -.
ChEMBL; CHEMBL330; -.
GuidetoPHARMACOLOGY; 455; -.
TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P35439; -.
PhosphoSitePlus; P35439; -.
UniCarbKB; P35439; -.
PaxDb; P35439; -.
PRIDE; P35439; -.
Ensembl; ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
Ensembl; ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
GeneID; 24408; -.
KEGG; rno:24408; -.
UCSC; RGD:2736; rat. [P35439-1]
CTD; 2902; -.
RGD; 2736; Grin1.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000231491; -.
HOVERGEN; HBG052638; -.
InParanoid; P35439; -.
KO; K05208; -.
OrthoDB; EOG091G0M5H; -.
PhylomeDB; P35439; -.
TreeFam; TF351405; -.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-RNO-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-RNO-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
EvolutionaryTrace; P35439; -.
PRO; PR:P35439; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000011726; -.
ExpressionAtlas; P35439; baseline and differential.
Genevisible; P35439; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:BHF-UCL.
GO; GO:0044307; C:dendritic branch; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0043083; C:synaptic cleft; IDA:RGD.
GO; GO:0097060; C:synaptic membrane; IPI:ARUK-UCL.
GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0005262; F:calcium channel activity; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; ISO:RGD.
GO; GO:0005516; F:calmodulin binding; ISO:RGD.
GO; GO:0005261; F:cation channel activity; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
GO; GO:0035254; F:glutamate receptor binding; IPI:RGD.
GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IDA:RGD.
GO; GO:0032403; F:protein complex binding; IPI:ARUK-UCL.
GO; GO:0046983; F:protein dimerization activity; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
GO; GO:0008306; P:associative learning; ISO:RGD.
GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
GO; GO:0001661; P:conditioned taste aversion; ISO:RGD.
GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
GO; GO:0007612; P:learning; ISO:RGD.
GO; GO:0007611; P:learning or memory; ISO:RGD.
GO; GO:0007616; P:long-term memory; ISO:RGD.
GO; GO:0060179; P:male mating behavior; ISO:RGD.
GO; GO:0007613; P:memory; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0050905; P:neuromuscular process; ISO:RGD.
GO; GO:0008355; P:olfactory learning; ISO:RGD.
GO; GO:0021586; P:pons maturation; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IGI:ARUK-UCL.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IGI:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
GO; GO:0018964; P:propylene metabolic process; ISO:RGD.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:RGD.
GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
GO; GO:0010646; P:regulation of cell communication; ISO:RGD.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
GO; GO:0043576; P:regulation of respiratory gaseous exchange; ISO:RGD.
GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
GO; GO:0007585; P:respiratory gaseous exchange; ISO:RGD.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0001975; P:response to amphetamine; ISO:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0045471; P:response to ethanol; ISO:RGD.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0043278; P:response to morphine; ISO:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IDA:RGD.
GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
GO; GO:0035176; P:social behavior; ISO:RGD.
GO; GO:0001964; P:startle response; ISO:RGD.
GO; GO:0001967; P:suckling behavior; ISO:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
GO; GO:0008542; P:visual learning; ISO:RGD.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF10562; CaM_bdg_C0; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 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; Alternative splicing; Calcium; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Ligand-gated ion channel; Magnesium;
Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 938 Glutamate receptor ionotropic, NMDA 1.
/FTId=PRO_0000011589.
TOPO_DOM 19 559 Extracellular.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 560 580 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 581 602 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
INTRAMEM 603 624 Discontinuously helical.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
TOPO_DOM 625 630 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 631 647 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 648 812 Extracellular.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 813 833 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 834 938 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
REGION 516 518 Glycine binding. {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:24876489}.
REGION 603 624 Pore-forming.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
BINDING 523 523 Glycine. {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24876489}.
BINDING 688 688 Glycine. {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24876489}.
BINDING 732 732 Glycine. {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ,
ECO:0000269|PubMed:16281028,
ECO:0000269|PubMed:24876489}.
MOD_RES 889 889 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 890 890 Phosphoserine; by PKC.
{ECO:0000269|PubMed:15936117}.
MOD_RES 896 896 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 897 897 Phosphoserine; by PKC.
{ECO:0000269|PubMed:11588171}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3Q41}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3Q41,
ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3Q41}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3Q41,
ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3Q41,
ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 79 308 {ECO:0000244|PDB:3Q41,
ECO:0000244|PDB:4PE5}.
DISULFID 420 454 {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:1PB8,
ECO:0000244|PDB:1PB9,
ECO:0000244|PDB:1PBQ,
ECO:0000244|PDB:1Y1M,
ECO:0000244|PDB:1Y1Z,
ECO:0000244|PDB:1Y20,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4KCC,
ECO:0000244|PDB:4KFQ,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ}.
DISULFID 436 455 {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:1PB8,
ECO:0000244|PDB:1PB9,
ECO:0000244|PDB:1PBQ,
ECO:0000244|PDB:1Y1M,
ECO:0000244|PDB:1Y1Z,
ECO:0000244|PDB:1Y20,
ECO:0000244|PDB:2A5T,
ECO:0000244|PDB:4KCC,
ECO:0000244|PDB:4KFQ,
ECO:0000244|PDB:4NF4,
ECO:0000244|PDB:4NF5,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4NF8,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5DEX,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5I57,
ECO:0000244|PDB:5I58,
ECO:0000244|PDB:5I59,
ECO:0000244|PDB:5JTY,
ECO:0000244|PDB:5U8C,
ECO:0000244|PDB:5VIH,
ECO:0000244|PDB:5VII,
ECO:0000244|PDB:5VIJ}.
DISULFID 744 798 {ECO:0000244|PDB:1PB7,
ECO:0000244|PDB:1PB8,
ECO:0000244|PDB:1PB9,
ECO:0000244|PDB:1PBQ,
ECO:0000244|PDB:1Y1Z,
ECO:0000244|PDB:1Y20,
ECO:0000244|PDB:4KCC,
ECO:0000244|PDB:4KFQ,
ECO:0000244|PDB:4NF6,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5I56,
ECO:0000244|PDB:5U8C}.
VAR_SEQ 190 190 K -> KSKKRNYENLDQLSYDNKRGPK (in isoform
B, isoform F and isoform G).
{ECO:0000305}.
/FTId=VSP_000140.
VAR_SEQ 864 900 Missing (in isoform F and isoform C).
{ECO:0000305}.
/FTId=VSP_000141.
VAR_SEQ 864 885 DRKSGRAEPDPKKKATFRAITS -> QYHPTDITGPLNLSD
PSVSTVV (in isoform E and isoform G).
{ECO:0000305}.
/FTId=VSP_000142.
VAR_SEQ 886 938 Missing (in isoform E and isoform G).
{ECO:0000305}.
/FTId=VSP_000143.
VAR_SEQ 901 938 STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES ->
QYHPTDITGPLNLSDPSVSTVV (in isoform D).
{ECO:0000305}.
/FTId=VSP_000144.
STRAND 26 35 {ECO:0000244|PDB:3Q41}.
HELIX 36 50 {ECO:0000244|PDB:3Q41}.
STRAND 59 66 {ECO:0000244|PDB:3Q41}.
HELIX 71 80 {ECO:0000244|PDB:3Q41}.
HELIX 83 85 {ECO:0000244|PDB:3Q41}.
STRAND 87 92 {ECO:0000244|PDB:3Q41}.
TURN 98 103 {ECO:0000244|PDB:3Q41}.
HELIX 104 112 {ECO:0000244|PDB:3Q41}.
TURN 113 115 {ECO:0000244|PDB:3Q41}.
STRAND 118 122 {ECO:0000244|PDB:3Q41}.
HELIX 126 129 {ECO:0000244|PDB:3Q41}.
TURN 131 133 {ECO:0000244|PDB:3Q41}.
STRAND 137 141 {ECO:0000244|PDB:3Q41}.
HELIX 144 146 {ECO:0000244|PDB:3Q41}.
HELIX 147 156 {ECO:0000244|PDB:3Q41}.
HELIX 157 159 {ECO:0000244|PDB:3Q41}.
STRAND 163 170 {ECO:0000244|PDB:3Q41}.
HELIX 171 185 {ECO:0000244|PDB:3Q41}.
TURN 186 188 {ECO:0000244|PDB:3Q41}.
STRAND 192 197 {ECO:0000244|PDB:3Q41}.
HELIX 205 212 {ECO:0000244|PDB:3Q41}.
STRAND 218 222 {ECO:0000244|PDB:3Q41}.
HELIX 225 237 {ECO:0000244|PDB:3Q41}.
STRAND 246 248 {ECO:0000244|PDB:3Q41}.
TURN 251 254 {ECO:0000244|PDB:3Q41}.
TURN 256 260 {ECO:0000244|PDB:3Q41}.
STRAND 267 271 {ECO:0000244|PDB:3Q41}.
HELIX 277 296 {ECO:0000244|PDB:3Q41}.
STRAND 298 300 {ECO:0000244|PDB:3Q41}.
HELIX 317 326 {ECO:0000244|PDB:3Q41}.
STRAND 334 336 {ECO:0000244|PDB:3Q41}.
STRAND 338 340 {ECO:0000244|PDB:3Q41}.
STRAND 342 344 {ECO:0000244|PDB:3Q41}.
STRAND 351 357 {ECO:0000244|PDB:3Q41}.
STRAND 360 363 {ECO:0000244|PDB:3Q41}.
STRAND 365 367 {ECO:0000244|PDB:3Q41}.
STRAND 372 374 {ECO:0000244|PDB:3Q41}.
STRAND 398 402 {ECO:0000244|PDB:1PB7}.
TURN 406 408 {ECO:0000244|PDB:1PB7}.
STRAND 409 413 {ECO:0000244|PDB:1PB7}.
TURN 416 418 {ECO:0000244|PDB:5I59}.
STRAND 426 428 {ECO:0000244|PDB:4NF4}.
STRAND 434 439 {ECO:0000244|PDB:1PB7}.
STRAND 450 457 {ECO:0000244|PDB:1PB7}.
HELIX 458 470 {ECO:0000244|PDB:1PB7}.
STRAND 474 478 {ECO:0000244|PDB:1PB7}.
STRAND 487 489 {ECO:0000244|PDB:1PB7}.
STRAND 491 494 {ECO:0000244|PDB:1Y1M}.
STRAND 496 498 {ECO:0000244|PDB:1PB7}.
HELIX 500 506 {ECO:0000244|PDB:1PB7}.
STRAND 511 513 {ECO:0000244|PDB:1PB7}.
HELIX 521 524 {ECO:0000244|PDB:1PB7}.
STRAND 527 529 {ECO:0000244|PDB:1PB7}.
STRAND 533 543 {ECO:0000244|PDB:1PB7}.
STRAND 666 668 {ECO:0000244|PDB:5VII}.
HELIX 670 673 {ECO:0000244|PDB:1PB7}.
STRAND 677 679 {ECO:0000244|PDB:5VIJ}.
STRAND 684 687 {ECO:0000244|PDB:1Y1Z}.
HELIX 688 694 {ECO:0000244|PDB:1PB7}.
HELIX 697 699 {ECO:0000244|PDB:1PB7}.
HELIX 700 706 {ECO:0000244|PDB:1PB7}.
TURN 707 709 {ECO:0000244|PDB:1PB7}.
STRAND 711 713 {ECO:0000244|PDB:1PB7}.
HELIX 714 722 {ECO:0000244|PDB:1PB7}.
STRAND 727 732 {ECO:0000244|PDB:1PB7}.
HELIX 733 742 {ECO:0000244|PDB:1PB7}.
STRAND 746 748 {ECO:0000244|PDB:1PB7}.
STRAND 753 758 {ECO:0000244|PDB:1PB7}.
STRAND 761 763 {ECO:0000244|PDB:1PB7}.
HELIX 769 781 {ECO:0000244|PDB:1PB7}.
HELIX 784 792 {ECO:0000244|PDB:1PB7}.
STRAND 794 796 {ECO:0000244|PDB:1PB7}.
HELIX 805 813 {ECO:0000244|PDB:5I57}.
SEQUENCE 938 AA; 105509 MW; 613D36E38F05BC73 CRC64;
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM
TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES


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