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Glutamate receptor 1 (GluR-1) (AMPA-selective glutamate receptor 1) (GluR-A) (GluR-K1) (Glutamate receptor ionotropic, AMPA 1) (GluA1)

 GRIA1_RAT               Reviewed;         907 AA.
P19490;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
22-NOV-2017, entry version 179.
RecName: Full=Glutamate receptor 1;
Short=GluR-1;
AltName: Full=AMPA-selective glutamate receptor 1;
AltName: Full=GluR-A;
AltName: Full=GluR-K1;
AltName: Full=Glutamate receptor ionotropic, AMPA 1;
Short=GluA1;
Flags: Precursor;
Name=Gria1; Synonyms=Glur1;
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 [MRNA] (ISOFORM FLOP).
TISSUE=Forebrain;
PubMed=2480522; DOI=10.1038/342643a0;
Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F.;
"Cloning by functional expression of a member of the glutamate
receptor family.";
Nature 342:643-648(1989).
[2]
SEQUENCE REVISION.
Hartley M.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
TISSUE=Brain;
PubMed=2166337; DOI=10.1126/science.2166337;
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
Sakmann B., Seeburg P.H.;
"A family of AMPA-selective glutamate receptors.";
Science 249:556-560(1990).
[4]
SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893.
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
Sakmann B., Seeburg P.H.;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
PubMed=2168579; DOI=10.1126/science.2168579;
Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M.,
Deneris E.S., Maron C., Heinemann S.F.;
"Molecular cloning and functional expression of glutamate receptor
subunit genes.";
Science 249:1033-1037(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND VARIANT THR-710.
TISSUE=Brain;
PubMed=1699275; DOI=10.1126/science.1699275;
Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N.,
Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.;
"Flip and flop: a cell-specific functional switch in glutamate-
operated channels of the CNS.";
Science 249:1580-1585(1990).
[7]
PHOSPHORYLATION AT SER-645.
PubMed=7877986; DOI=10.1073/pnas.92.5.1376;
Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A.,
Soderling T.R.;
"Identification of a Ca2+/calmodulin-dependent protein kinase II
regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995).
[8]
VARIANT THR-710, AND PHOSPHORYLATION AT SER-710.
PubMed=8848293; DOI=10.1016/0168-0102(95)00977-9;
Nakazawa K., Tadakuma T., Nokihara K., Ito M.;
"Antibody specific for phosphorylated AMPA-type glutamate receptors at
GluR2 Ser-696.";
Neurosci. Res. 24:75-86(1995).
[9]
PHOSPHORYLATION AT SER-849 AND SER-863, AND MUTAGENESIS OF SER-645 AND
SER-849.
PubMed=9405465; DOI=10.1074/jbc.272.51.32528;
Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.;
"Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-
propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent
kinase II.";
J. Biol. Chem. 272:32528-32533(1997).
[10]
INTERACTION WITH DLG1.
PubMed=9677374; DOI=10.1074/jbc.273.31.19518;
Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.;
"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-
4-propionic acid receptor GluR1 subunit.";
J. Biol. Chem. 273:19518-19524(1998).
[11]
INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF THR-905 AND LEU-907.
PubMed=12070168; DOI=10.1074/jbc.M204354200;
Cai C., Coleman S.K., Niemi K., Keinaenen K.;
"Selective binding of synapse-associated protein 97 to GluR-A alpha-
amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is
determined by a novel sequence motif.";
J. Biol. Chem. 277:31484-31490(2002).
[12]
INTERACTION WITH PDLIM4, AND SUBCELLULAR LOCATION.
PubMed=15456832; DOI=10.1523/JNEUROSCI.2100-04.2004;
Schulz T.W., Nakagawa T., Licznerski P., Pawlak V., Kolleker A.,
Rozov A., Kim J., Dittgen T., Koehr G., Sheng M., Seeburg P.H.,
Osten P.;
"Actin/alpha-actinin-dependent transport of AMPA receptors in
dendritic spines: role of the PDZ-LIM protein RIL.";
J. Neurosci. 24:8584-8594(2004).
[13]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2.
PubMed=16793768; DOI=10.1074/jbc.M600679200;
Bedoukian M.A., Weeks A.M., Partin K.M.;
"Different domains of the AMPA receptor direct stargazin-mediated
trafficking and stargazin-mediated modulation of kinetics.";
J. Biol. Chem. 281:23908-23921(2006).
[14]
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).
[15]
INTERACTION WITH PRKG2, PHOSPHORYLATION AT SER-863, AND MUTAGENESIS OF
ARG-855 AND SER-863.
PubMed=18031684; DOI=10.1016/j.neuron.2007.09.016;
Serulle Y., Zhang S., Ninan I., Puzzo D., McCarthy M., Khatri L.,
Arancio O., Ziff E.B.;
"A GluR1-cGKII interaction regulates AMPA receptor trafficking.";
Neuron 56:670-688(2007).
[16]
INTERACTION WITH CACNG5.
PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034;
Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.;
"AMPA receptor subunit-specific regulation by a distinct family of
type II TARPs.";
Neuron 59:986-996(2008).
[17]
INTERACTION WITH CACNG5.
PubMed=19234459; DOI=10.1038/nn.2266;
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M.,
Cull-Candy S.G.;
"Selective regulation of long-form calcium-permeable AMPA receptors by
an atypical TARP, gamma-5.";
Nat. Neurosci. 12:277-285(2009).
[18]
ERRATUM.
DOI=10.1038/nn0609-808c;
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M.,
Cull-Candy S.G.;
Nat. Neurosci. 12:808-808(2009).
[19]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19265014; DOI=10.1126/science.1167852;
Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
"Functional proteomics identify cornichon proteins as auxiliary
subunits of AMPA receptors.";
Science 323:1313-1319(2009).
[20]
INTERACTION WITH CNIH2 AND CACNG2.
PubMed=20805473; DOI=10.1073/pnas.1011706107;
Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W.,
Nicoll R.A.;
"Functional comparison of the effects of TARPs and cornichons on AMPA
receptor trafficking and gating.";
Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010).
[21]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH
DLG1, AND INTERACTION WITH DLG1.
PubMed=17069616; DOI=10.1111/j.1742-4658.2006.05521.x;
von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M.,
Goldman A., Keinanen K.;
"Crystal structure of the second PDZ domain of SAP97 in complex with a
GluR-A C-terminal peptide.";
FEBS J. 273:5219-5229(2006).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT,
GLYCOSYLATION AT ASN-249; ASN-257 AND ASN-363, AND DISULFIDE BOND.
PubMed=21639859; DOI=10.1042/BJ20110801;
Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.;
"Crystal structure of the glutamate receptor GluA1 N-terminal
domain.";
Biochem. J. 438:255-263(2011).
-!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
excitatory neurotransmitter at many synapses in the central
nervous system. Binding of the excitatory neurotransmitter L-
glutamate induces a conformation change, leading to the opening of
the cation channel, and thereby converts the chemical signal to an
electrical impulse. The receptor then desensitizes rapidly and
enters a transient inactive state, characterized by the presence
of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8,
shows resensitization which is characterized by a delayed
accumulation of current flux upon continued application of
glutamate. {ECO:0000269|PubMed:16793768,
ECO:0000269|PubMed:19265014}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits (PubMed:21639859). Tetramers may be formed by
the dimerization of dimers (By similarity). Interacts with HIP1
and RASGRF2. Interacts with SYNDIG1 and GRIA2 (By similarity).
Interacts with DLG1 (via C-terminus) (PubMed:12070168,
PubMed:17069616, PubMed:9677374). Interacts with LRFN1
(PubMed:16630835). Interacts with PRKG2 (PubMed:18031684).
Interacts with CNIH2 and CACNG2 (PubMed:20805473). Interacts with
CACNG5 (PubMed:18817736, PubMed:19234459). Interacts (via C-
terminus) with PDLIM4 (via LIM domain); this interaction as well
as the interaction of PDLIM4 with alpha-actinin is required for
their colocalization in early endosomes (PubMed:15456832). Found
in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2,
CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (PubMed:16793768,
PubMed:19265014). Interacts with SNX27 (via PDZ domain); the
interaction is required for recycling to the plasma membrane when
endocytosed and prevent degradation in lysosomes. Interacts (via
PDZ-binding motif) with SHANK3 (via PDZ domain) (By similarity).
Interacts with CACNG3; associates GRIA1 with the adaptor protein
complex 4 (AP-4) to target GRIA1 to the somatodendritic
compartment of neurons (By similarity).
{ECO:0000250|UniProtKB:P23818, ECO:0000250|UniProtKB:P42261,
ECO:0000269|PubMed:12070168, ECO:0000269|PubMed:15456832,
ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:16793768,
ECO:0000269|PubMed:17069616, ECO:0000269|PubMed:18031684,
ECO:0000269|PubMed:18817736, ECO:0000269|PubMed:19234459,
ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20805473,
ECO:0000269|PubMed:21639859, ECO:0000269|PubMed:9677374}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-371642, EBI-371642;
P10608:Adrb2; NbExp=3; IntAct=EBI-371642, EBI-7090342;
Q71RJ2:Cacng2; NbExp=2; IntAct=EBI-371642, EBI-8538384;
P19491:Gria2; NbExp=3; IntAct=EBI-371642, EBI-77718;
P70569:Myo5b; NbExp=2; IntAct=EBI-371642, EBI-975940;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23818}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15456832}; Multi-pass membrane protein
{ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23818}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine
{ECO:0000250|UniProtKB:P23818}. Early endosome membrane
{ECO:0000269|PubMed:15456832}; Multi-pass membrane protein
{ECO:0000305}. Recycling endosome membrane
{ECO:0000269|PubMed:15456832}; Multi-pass membrane protein
{ECO:0000305}. Note=Interaction with CACNG2, CNIH2 and CNIH3
promotes cell surface expression (PubMed:19265014). Colocalizes
with PDLIM4 in early endosomes (PubMed:15456832). Displays a
somatodendritic localization and is excluded from axons in neurons
(By similarity). {ECO:0000250|UniProtKB:P23818,
ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:19265014}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Flop;
IsoId=P19490-1; Sequence=Displayed;
Name=Flip;
IsoId=P19490-2; Sequence=VSP_000097, VSP_000098, VSP_000099,
VSP_000100, VSP_000101;
-!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level).
{ECO:0000269|PubMed:12070168}.
-!- DOMAIN: The M4 transmembrane segment mediates tetramerization and
is required for cell surface expression. {ECO:0000250}.
-!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
Cys-603 palmitoylation leads to Golgi retention and decreased cell
surface expression. In contrast, Cys-829 palmitoylation does not
affect cell surface expression but regulates stimulation-dependent
endocytosis (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-645 (PubMed:7877986). Phosphorylated at
Ser-710 by PKC (PubMed:8848293). Phosphorylated at Ser-849 by PKC,
PKA and CAMK2 (PubMed:9405465). Phosphorylated at Ser-863 by PKC,
PKA and PRKG2 (PubMed:9405465, PubMed:18031684).
{ECO:0000269|PubMed:18031684, ECO:0000269|PubMed:7877986,
ECO:0000269|PubMed:8848293, ECO:0000269|PubMed:9405465}.
-!- POLYMORPHISM: Both variants Ser-710 and Thr-710 are phosphorylated
at this position.
-!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
variety of receptors that are named according to their selective
agonists. This receptor binds AMPA (quisqualate) > glutamate >
kainate.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIA1 subfamily. {ECO:0000305}.
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EMBL; X17184; CAA35050.1; -; mRNA.
EMBL; M36418; AAA41243.2; -; mRNA.
EMBL; M38060; AAA63479.1; -; mRNA.
PIR; A40170; A40170.
PIR; S07059; ACRTK1.
RefSeq; NP_113796.1; NM_031608.1. [P19490-1]
UniGene; Rn.29971; -.
PDB; 2AWW; X-ray; 2.21 A; C=890-907.
PDB; 2G2L; X-ray; 2.35 A; C/D=890-907.
PDB; 3SAJ; X-ray; 2.50 A; A/B/C/D=22-392.
PDBsum; 2AWW; -.
PDBsum; 2G2L; -.
PDBsum; 3SAJ; -.
ProteinModelPortal; P19490; -.
SMR; P19490; -.
BioGrid; 248399; 10.
CORUM; P19490; -.
DIP; DIP-30929N; -.
ELM; P19490; -.
IntAct; P19490; 25.
MINT; MINT-726538; -.
BindingDB; P19490; -.
ChEMBL; CHEMBL3753; -.
TCDB; 1.A.10.1.1; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P19490; -.
PhosphoSitePlus; P19490; -.
SwissPalm; P19490; -.
PRIDE; P19490; -.
GeneID; 50592; -.
KEGG; rno:50592; -.
UCSC; RGD:621531; rat. [P19490-1]
CTD; 2890; -.
RGD; 621531; Gria1.
HOVERGEN; HBG051839; -.
InParanoid; P19490; -.
KO; K05197; -.
PhylomeDB; P19490; -.
EvolutionaryTrace; P19490; -.
PRO; PR:P19490; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
GO; GO:0044308; C:axonal spine; ISO:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
GO; GO:0032590; C:dendrite membrane; ISO:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
GO; GO:0032591; C:dendritic spine membrane; ISO:RGD.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0044309; C:neuron spine; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0098794; C:postsynapse; ISO:RGD.
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:0043234; C:protein complex; IDA:RGD.
GO; GO:0055037; C:recycling endosome; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:SynGO-UCL.
GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0031489; F:myosin V binding; IPI:RGD.
GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:ARUK-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0051018; F:protein kinase A binding; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
GO; GO:0031267; F:small GTPase binding; IPI:RGD.
GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
GO; GO:0071418; P:cellular response to amine stimulus; IEP:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
GO; GO:0060292; P:long term synaptic depression; ISO:RGD.
GO; GO:0007616; P:long-term memory; IMP:RGD.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
GO; GO:0045838; P:positive regulation of membrane potential; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IMP:RGD.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; NAS:UniProtKB.
InterPro; IPR001828; ANF_lig-bd_rcpt.
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; 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; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Receptor; Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 907 Glutamate receptor 1.
/FTId=PRO_0000011531.
TOPO_DOM 19 536 Extracellular. {ECO:0000250}.
TRANSMEM 537 557 Helical. {ECO:0000250}.
TOPO_DOM 558 584 Cytoplasmic. {ECO:0000250}.
INTRAMEM 585 600 Helical; Pore-forming. {ECO:0000250}.
INTRAMEM 601 603 {ECO:0000250}.
TOPO_DOM 604 609 Cytoplasmic. {ECO:0000250}.
TRANSMEM 610 630 Helical. {ECO:0000250}.
TOPO_DOM 631 805 Extracellular. {ECO:0000250}.
TRANSMEM 806 826 Helical; Name=M4. {ECO:0000250}.
TOPO_DOM 827 907 Cytoplasmic. {ECO:0000250}.
REGION 492 494 Glutamate binding. {ECO:0000250}.
REGION 668 669 Glutamate binding. {ECO:0000250}.
MOTIF 904 907 PDZ-binding.
BINDING 464 464 Glutamate. {ECO:0000250}.
BINDING 499 499 Glutamate. {ECO:0000250}.
BINDING 719 719 Glutamate. {ECO:0000250}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000269|PubMed:7877986}.
MOD_RES 710 710 Phosphoserine; by PKC.
{ECO:0000269|PubMed:8848293}.
MOD_RES 849 849 Phosphoserine; by PKC, PKA and CAMK2.
{ECO:0000269|PubMed:7877986,
ECO:0000269|PubMed:9405465}.
MOD_RES 863 863 Phosphoserine; by PKC, PKA and PKG/PRKG2.
{ECO:0000269|PubMed:18031684,
ECO:0000269|PubMed:9405465}.
LIPID 603 603 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 829 829 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21639859}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21639859}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21639859}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 323 {ECO:0000269|PubMed:21639859}.
DISULFID 732 787 {ECO:0000250}.
VAR_SEQ 758 758 N -> G (in isoform Flip).
{ECO:0000303|PubMed:1699275}.
/FTId=VSP_000097.
VAR_SEQ 768 768 N -> S (in isoform Flip).
{ECO:0000303|PubMed:1699275}.
/FTId=VSP_000098.
VAR_SEQ 772 772 L -> V (in isoform Flip).
{ECO:0000303|PubMed:1699275}.
/FTId=VSP_000099.
VAR_SEQ 778 778 N -> S (in isoform Flip).
{ECO:0000303|PubMed:1699275}.
/FTId=VSP_000100.
VAR_SEQ 790 793 GGGD -> KDSG (in isoform Flip).
{ECO:0000303|PubMed:1699275}.
/FTId=VSP_000101.
VARIANT 710 710 S -> T. {ECO:0000269|PubMed:1699275,
ECO:0000269|PubMed:8848293}.
MUTAGEN 645 645 S->A: No effect on phosphorylation by
CaMK2. {ECO:0000269|PubMed:9405465}.
MUTAGEN 849 849 S->A: Abolishes phosphorylation by CaMK2.
{ECO:0000269|PubMed:9405465}.
MUTAGEN 855 855 R->A: Decreases binding efficiency to
PRKG2.
MUTAGEN 855 855 R->E: Abolishes binding to PRKG2.
{ECO:0000269|PubMed:18031684}.
MUTAGEN 863 863 S->A: Decreases synaptic insertion during
chemical-induced long term potentiation.
{ECO:0000269|PubMed:18031684}.
MUTAGEN 905 905 T->A: Loss of interaction with DLG1.
{ECO:0000269|PubMed:12070168}.
MUTAGEN 907 907 L->A: Loss of interaction with DLG1.
{ECO:0000269|PubMed:12070168}.
CONFLICT 67 67 S -> T (in Ref. 6; AAA63479).
{ECO:0000305}.
CONFLICT 248 248 A -> R (in Ref. 6; AAA63479).
{ECO:0000305}.
CONFLICT 698 698 R -> L (in Ref. 6; AAA63479).
{ECO:0000305}.
STRAND 23 32 {ECO:0000244|PDB:3SAJ}.
STRAND 34 36 {ECO:0000244|PDB:3SAJ}.
HELIX 37 46 {ECO:0000244|PDB:3SAJ}.
STRAND 51 61 {ECO:0000244|PDB:3SAJ}.
HELIX 67 79 {ECO:0000244|PDB:3SAJ}.
STRAND 85 87 {ECO:0000244|PDB:3SAJ}.
HELIX 91 104 {ECO:0000244|PDB:3SAJ}.
STRAND 108 110 {ECO:0000244|PDB:3SAJ}.
STRAND 122 124 {ECO:0000244|PDB:3SAJ}.
HELIX 130 139 {ECO:0000244|PDB:3SAJ}.
STRAND 144 149 {ECO:0000244|PDB:3SAJ}.
HELIX 156 168 {ECO:0000244|PDB:3SAJ}.
STRAND 171 176 {ECO:0000244|PDB:3SAJ}.
HELIX 177 179 {ECO:0000244|PDB:3SAJ}.
HELIX 183 187 {ECO:0000244|PDB:3SAJ}.
TURN 188 191 {ECO:0000244|PDB:3SAJ}.
STRAND 196 203 {ECO:0000244|PDB:3SAJ}.
HELIX 206 208 {ECO:0000244|PDB:3SAJ}.
HELIX 209 218 {ECO:0000244|PDB:3SAJ}.
STRAND 225 233 {ECO:0000244|PDB:3SAJ}.
HELIX 235 237 {ECO:0000244|PDB:3SAJ}.
HELIX 240 245 {ECO:0000244|PDB:3SAJ}.
STRAND 250 254 {ECO:0000244|PDB:3SAJ}.
HELIX 261 276 {ECO:0000244|PDB:3SAJ}.
HELIX 288 309 {ECO:0000244|PDB:3SAJ}.
HELIX 334 342 {ECO:0000244|PDB:3SAJ}.
STRAND 346 348 {ECO:0000244|PDB:3SAJ}.
STRAND 351 353 {ECO:0000244|PDB:3SAJ}.
STRAND 359 361 {ECO:0000244|PDB:3SAJ}.
STRAND 366 372 {ECO:0000244|PDB:3SAJ}.
STRAND 375 383 {ECO:0000244|PDB:3SAJ}.
TURN 384 386 {ECO:0000244|PDB:3SAJ}.
STRAND 387 390 {ECO:0000244|PDB:3SAJ}.
STRAND 905 907 {ECO:0000244|PDB:2AWW}.
SEQUENCE 907 AA; 101579 MW; 2D4CFA7CCD532838 CRC64;
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ
FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL
NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW
WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK
GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM
PLGATGL


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