Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glutamate receptor 4 (GluR-4) (GluR4) (AMPA-selective glutamate receptor 4) (GluR-D) (Glutamate receptor ionotropic, AMPA 4) (GluA4)

 GRIA4_RAT               Reviewed;         902 AA.
P19493; Q64241;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
07-NOV-2018, entry version 174.
RecName: Full=Glutamate receptor 4;
Short=GluR-4;
Short=GluR4;
AltName: Full=AMPA-selective glutamate receptor 4;
AltName: Full=GluR-D;
AltName: Full=Glutamate receptor ionotropic, AMPA 4;
Short=GluA4;
Flags: Precursor;
Name=Gria4; Synonyms=Glur4;
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 1).
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1977421; DOI=10.1016/0896-6273(90)90213-Y;
Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A.,
Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.;
"Cloning of a novel glutamate receptor subunit, GluR5: expression in
the nervous system during development.";
Neuron 5:583-595(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1372042;
Gallo V., Upson L.M., Hayes W.P., Vyklicky L. Jr., Winters C.A.,
Buonanno A.;
"Molecular cloning and development analysis of a new glutamate
receptor subunit isoform in cerebellum.";
J. Neurosci. 12:1010-1023(1992).
[5]
PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-407 AND ASN-414,
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF ASN-407 AND
ASN-414.
PubMed=12603841; DOI=10.1046/j.1471-4159.2003.01611.x;
Pasternack A., Coleman S.K., Fethiere J., Madden D.R., LeCaer J.P.,
Rossier J., Pasternack M., Keinaenen K.;
"Characterization of the functional role of the N-glycans in the AMPA
receptor ligand-binding domain.";
J. Neurochem. 84:1184-1192(2003).
[6]
INTERACTION WITH PRKCABP (ISOFORM 3).
PubMed=10027300; DOI=10.1016/S0896-6273(00)80689-3;
Xia J., Zhang X., Staudinger J., Huganir R.L.;
"Clustering of AMPA receptors by the synaptic PDZ domain-containing
protein PICK1.";
Neuron 22:179-187(1999).
[7]
PHOSPHORYLATION AT SER-862, INTERACTION WITH PRKCG, AND SUBCELLULAR
LOCATION.
PubMed=12471040; DOI=10.1074/jbc.M205587200;
Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.;
"Protein kinase C gamma associates directly with the GluR4 alpha-
amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit.
Effect on receptor phosphorylation.";
J. Biol. Chem. 278:6307-6313(2003).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH EPB41L1.
PubMed=12574408;
Coleman S.K., Cai C., Mottershead D.G., Haapalahti J.-P.,
Keinaenen K.;
"Surface expression of GluR-D AMPA receptor is dependent on an
interaction between its C-terminal domain and a 4.1 protein.";
J. Neurosci. 23:798-806(2003).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-
glycoproteome heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 416-795 IN COMPLEX WITH
GLUTAMATE AND DIHYDROKAINIC ACID, FUNCTION, AND SUBUNIT.
PubMed=19102704; DOI=10.1021/bi8013196;
Gill A., Birdsey-Benson A., Jones B.L., Henderson L.P., Madden D.R.;
"Correlating AMPA receptor activation and cleft closure across
subunits: crystal structures of the GluR4 ligand-binding domain in
complex with full and partial agonists.";
Biochemistry 47:13831-13841(2008).
[15]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 415-796 IN COMPLEX WITH
GLUTAMATE, AMPA BINDING, AND DISULFIDE BOND.
PubMed=19022251; DOI=10.1016/j.febslet.2008.11.005;
Kasper C., Frydenvang K., Naur P., Gajhede M., Pickering D.S.,
Kastrup J.S.;
"Molecular mechanism of agonist recognition by the ligand-binding core
of the ionotropic glutamate receptor 4.";
FEBS Lett. 582:4089-4094(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 416-795 IN COMPLEX WITH
GLUTAMATE AND DIHYDROKAINIC ACID, AND FUNCTION.
PubMed=20107073; DOI=10.1523/JNEUROSCI.4558-09.2010;
Birdsey-Benson A., Gill A., Henderson L.P., Madden D.R.;
"Enhanced efficacy without further cleft closure: reevaluating twist
as a source of agonist efficacy in AMPA receptors.";
J. Neurosci. 30:1463-1470(2010).
-!- FUNCTION: Receptor for glutamate that functions as ligand-gated
ion channel in the central nervous system and plays an important
role in excitatory synaptic transmission. 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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12603841, ECO:0000269|PubMed:19102704,
ECO:0000269|PubMed:20107073}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers. Interacts with EPB41L1 via its C-terminus. Isoform 3
interacts with PRKCABP. Found in a complex with GRIA1, GRIA2,
GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and
CACNG8. Interacts with CACNG5 and PRKCG.
{ECO:0000269|PubMed:12471040, ECO:0000269|PubMed:12574408,
ECO:0000269|PubMed:18817736, ECO:0000269|PubMed:19022251,
ECO:0000269|PubMed:19102704, ECO:0000269|PubMed:19234459,
ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:20107073}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7761834, EBI-7761834;
P19491-2:Gria2; NbExp=2; IntAct=EBI-15852899, EBI-15817825;
P97879:Grip1; NbExp=3; IntAct=EBI-7761834, EBI-936113;
P49185:Mapk8; NbExp=2; IntAct=EBI-7761834, EBI-7456505;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell junction, synapse, postsynaptic cell membrane; Multi-pass
membrane protein. Cell projection, dendrite. Note=Interaction with
CNIH2, CNIH3 and PRKCG promotes cell surface expression.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Flop;
IsoId=P19493-1; Sequence=Displayed;
Name=2; Synonyms=Flip;
IsoId=P19493-2; Sequence=VSP_000123, VSP_000124, VSP_000125;
Name=3; Synonyms=4C flop;
IsoId=P19493-3; Sequence=VSP_000126;
-!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level).
-!- DOMAIN: The M4 transmembrane segment mediates tetramerization and
is required for cell surface expression. {ECO:0000250}.
-!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
Cys-611 palmitoylation leads to Golgi retention and decreased cell
surface expression. In contrast, Cys-837 palmitoylation does not
affect cell surface expression but regulates stimulation-dependent
endocytosis (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-862 by PRKCG; phosphorylation increases
plasma membrane-associated GRI4 expression.
{ECO:0000269|PubMed:12471040}.
-!- 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. GRIA4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M36421; AAA41246.1; -; mRNA.
EMBL; M85037; AAA41242.1; -; mRNA.
EMBL; M38063; AAA63481.1; -; mRNA.
EMBL; S94371; AAB21763.1; -; mRNA.
PIR; A44839; A44839.
PIR; D40170; D40170.
RefSeq; NP_001106655.1; NM_001113184.1.
RefSeq; NP_058959.2; NM_017263.2.
UniGene; Rn.10938; -.
PDB; 3EN3; X-ray; 2.43 A; A=416-528, A=654-795.
PDB; 3EPE; X-ray; 1.85 A; A/B=416-528, A/B=654-795.
PDB; 3FAS; X-ray; 1.40 A; A/B=415-528, A/B=654-796.
PDB; 3FAT; X-ray; 1.90 A; A/B/C=415-528, A/B/C=654-796.
PDB; 3KEI; X-ray; 1.90 A; A/B=416-528, A/B=654-795.
PDB; 3KFM; X-ray; 2.20 A; A=416-528, A=654-795.
PDB; 4GPA; X-ray; 2.25 A; A=22-401.
PDB; 5FWX; X-ray; 2.50 A; B/D=22-401.
PDBsum; 3EN3; -.
PDBsum; 3EPE; -.
PDBsum; 3FAS; -.
PDBsum; 3FAT; -.
PDBsum; 3KEI; -.
PDBsum; 3KFM; -.
PDBsum; 4GPA; -.
PDBsum; 5FWX; -.
ProteinModelPortal; P19493; -.
SMR; P19493; -.
BioGrid; 248252; 1.
CORUM; P19493; -.
DIP; DIP-41142N; -.
IntAct; P19493; 5.
MINT; P19493; -.
STRING; 10116.ENSRNOP00000009542; -.
BindingDB; P19493; -.
ChEMBL; CHEMBL3505; -.
TCDB; 1.A.10.1.2; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; P19493; -.
PhosphoSitePlus; P19493; -.
SwissPalm; P19493; -.
UniCarbKB; P19493; -.
PaxDb; P19493; -.
PRIDE; P19493; -.
GeneID; 29629; -.
KEGG; rno:29629; -.
UCSC; RGD:61863; rat. [P19493-1]
CTD; 2893; -.
RGD; 61863; Gria4.
HOGENOM; HOG000234372; -.
HOVERGEN; HBG051839; -.
InParanoid; P19493; -.
KO; K05200; -.
PhylomeDB; P19493; -.
EvolutionaryTrace; P19493; -.
PRO; PR:P19493; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:UniProtKB.
GO; GO:0032983; C:kainate selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IMP:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0004971; F:AMPA glutamate receptor activity; IMP:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:UniProtKB.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
GO; GO:0050803; P:regulation of synapse structure or activity; TAS:UniProtKB.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
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; Direct protein sequencing;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 902 Glutamate receptor 4.
/FTId=PRO_0000011540.
TOPO_DOM 22 544 Extracellular. {ECO:0000250}.
TRANSMEM 545 565 Helical. {ECO:0000250}.
TOPO_DOM 566 592 Cytoplasmic. {ECO:0000250}.
INTRAMEM 593 608 Helical; Pore-forming. {ECO:0000250}.
INTRAMEM 609 611 {ECO:0000250}.
TOPO_DOM 612 617 Cytoplasmic. {ECO:0000250}.
TRANSMEM 618 638 Helical. {ECO:0000250}.
TOPO_DOM 639 813 Extracellular. {ECO:0000250}.
TRANSMEM 814 834 Helical; Name=M4. {ECO:0000250}.
TOPO_DOM 835 902 Cytoplasmic. {ECO:0000250}.
REGION 500 502 Glutamate binding.
REGION 676 677 Glutamate binding.
BINDING 472 472 Glutamate. {ECO:0000269|PubMed:19022251,
ECO:0000269|PubMed:19102704,
ECO:0000269|PubMed:20107073}.
BINDING 507 507 Glutamate. {ECO:0000269|PubMed:19022251,
ECO:0000269|PubMed:19102704,
ECO:0000269|PubMed:20107073}.
BINDING 727 727 Glutamate. {ECO:0000250}.
MOD_RES 862 862 Phosphoserine; by PKC/PRKCG.
{ECO:0000269|PubMed:12471040}.
LIPID 611 611 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 837 837 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12603841}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12603841}.
DISULFID 84 331 {ECO:0000250}.
DISULFID 740 795 {ECO:0000269|PubMed:19022251}.
VAR_SEQ 765 767 GNA -> RTP (in isoform 2).
{ECO:0000303|PubMed:1699275,
ECO:0000303|PubMed:1977421}.
/FTId=VSP_000123.
VAR_SEQ 776 780 NEQGL -> SEAGV (in isoform 2).
{ECO:0000303|PubMed:1699275,
ECO:0000303|PubMed:1977421}.
/FTId=VSP_000124.
VAR_SEQ 797 801 SGGGD -> PKDSG (in isoform 2).
{ECO:0000303|PubMed:1699275,
ECO:0000303|PubMed:1977421}.
/FTId=VSP_000125.
VAR_SEQ 849 902 LTFSEATRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIR
QSSGLAVIASDLP -> VAKSAQTFNPTSSQNTHNLATYRE
GYNVYGTESIKI (in isoform 3).
{ECO:0000303|PubMed:1372042}.
/FTId=VSP_000126.
MUTAGEN 407 407 N->Q: No effect on surface expression and
channel activity; when associated with Q-
414. {ECO:0000269|PubMed:12603841}.
MUTAGEN 414 414 N->Q: No effect on surface expression and
channel activity; when associated with Q-
407. {ECO:0000269|PubMed:12603841}.
CONFLICT 111 112 SA -> RR (in Ref. 2; AAA41242).
{ECO:0000305}.
CONFLICT 454 454 I -> S (in Ref. 2; AAA41242).
{ECO:0000305}.
CONFLICT 734 734 T -> I (in Ref. 2; AAA41242).
{ECO:0000305}.
CONFLICT 855 855 T -> I (in Ref. 2; AAA41242).
{ECO:0000305}.
STRAND 25 33 {ECO:0000244|PDB:4GPA}.
HELIX 38 52 {ECO:0000244|PDB:4GPA}.
TURN 57 59 {ECO:0000244|PDB:4GPA}.
STRAND 61 70 {ECO:0000244|PDB:4GPA}.
HELIX 76 88 {ECO:0000244|PDB:4GPA}.
STRAND 92 96 {ECO:0000244|PDB:4GPA}.
TURN 100 102 {ECO:0000244|PDB:4GPA}.
HELIX 103 112 {ECO:0000244|PDB:4GPA}.
STRAND 116 119 {ECO:0000244|PDB:4GPA}.
STRAND 129 133 {ECO:0000244|PDB:4GPA}.
HELIX 139 148 {ECO:0000244|PDB:4GPA}.
STRAND 153 158 {ECO:0000244|PDB:4GPA}.
HELIX 165 175 {ECO:0000244|PDB:4GPA}.
TURN 176 178 {ECO:0000244|PDB:4GPA}.
STRAND 180 185 {ECO:0000244|PDB:4GPA}.
HELIX 191 204 {ECO:0000244|PDB:4GPA}.
STRAND 208 212 {ECO:0000244|PDB:4GPA}.
HELIX 215 228 {ECO:0000244|PDB:4GPA}.
STRAND 236 239 {ECO:0000244|PDB:4GPA}.
STRAND 241 243 {ECO:0000244|PDB:4GPA}.
HELIX 244 246 {ECO:0000244|PDB:4GPA}.
HELIX 250 255 {ECO:0000244|PDB:4GPA}.
STRAND 258 263 {ECO:0000244|PDB:4GPA}.
HELIX 270 279 {ECO:0000244|PDB:4GPA}.
TURN 284 286 {ECO:0000244|PDB:4GPA}.
TURN 288 291 {ECO:0000244|PDB:4GPA}.
HELIX 296 317 {ECO:0000244|PDB:4GPA}.
HELIX 342 350 {ECO:0000244|PDB:4GPA}.
STRAND 353 356 {ECO:0000244|PDB:4GPA}.
STRAND 359 363 {ECO:0000244|PDB:4GPA}.
STRAND 367 369 {ECO:0000244|PDB:5FWX}.
STRAND 373 380 {ECO:0000244|PDB:4GPA}.
STRAND 383 391 {ECO:0000244|PDB:4GPA}.
TURN 392 394 {ECO:0000244|PDB:4GPA}.
STRAND 395 398 {ECO:0000244|PDB:4GPA}.
STRAND 416 421 {ECO:0000244|PDB:3FAS}.
TURN 425 427 {ECO:0000244|PDB:3FAS}.
STRAND 428 430 {ECO:0000244|PDB:3FAS}.
HELIX 434 436 {ECO:0000244|PDB:3FAS}.
HELIX 439 442 {ECO:0000244|PDB:3FAS}.
STRAND 443 445 {ECO:0000244|PDB:3FAS}.
HELIX 446 458 {ECO:0000244|PDB:3FAS}.
STRAND 461 466 {ECO:0000244|PDB:3FAS}.
TURN 477 479 {ECO:0000244|PDB:3FAS}.
HELIX 484 490 {ECO:0000244|PDB:3FAS}.
STRAND 495 497 {ECO:0000244|PDB:3FAS}.
HELIX 505 508 {ECO:0000244|PDB:3FAS}.
STRAND 511 513 {ECO:0000244|PDB:3FAS}.
STRAND 517 520 {ECO:0000244|PDB:3FAS}.
STRAND 522 527 {ECO:0000244|PDB:3FAS}.
HELIX 658 662 {ECO:0000244|PDB:3FAS}.
STRAND 665 670 {ECO:0000244|PDB:3FAS}.
STRAND 672 675 {ECO:0000244|PDB:3KEI}.
HELIX 676 683 {ECO:0000244|PDB:3FAS}.
HELIX 687 698 {ECO:0000244|PDB:3FAS}.
STRAND 705 707 {ECO:0000244|PDB:3FAS}.
HELIX 708 717 {ECO:0000244|PDB:3FAS}.
TURN 718 720 {ECO:0000244|PDB:3FAS}.
STRAND 721 727 {ECO:0000244|PDB:3FAS}.
HELIX 728 735 {ECO:0000244|PDB:3FAS}.
STRAND 742 746 {ECO:0000244|PDB:3FAS}.
STRAND 752 754 {ECO:0000244|PDB:3FAS}.
STRAND 757 759 {ECO:0000244|PDB:3FAS}.
HELIX 765 777 {ECO:0000244|PDB:3FAS}.
HELIX 780 789 {ECO:0000244|PDB:3FAS}.
TURN 790 792 {ECO:0000244|PDB:3FAS}.
SEQUENCE 902 AA; 100758 MW; 873D1B4C710C4459 CRC64;
MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA
PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP
SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH
VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA
NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL
TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN
VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DMPTLGNDTA AIENRTVVVT
TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK
IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL
DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW
FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER MVSPIESAED
LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG
KFAFLLESTM NEYTEQRKPC DTMKVGGNLD SKGYGVATPK GSSLGNAVNL AVLKLNEQGL
LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS
RAEAKRMKLT FSEATRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD
LP


Related products :

Catalog number Product name Quantity
18-783-77674 SHEEP ANTI GLUTAMATE RECEPTOR 2 - GLUTAMATE RECEPTOR 2; GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.02 mg
10-783-79552 SYNTHETIC HUMAN GLUTAMATE RECEPTOR 2 (aa831-842) - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 0.05 mg
18-662-20066 Glutamate receptor 1 - GluR-1; GluR-A; GluR-K1; Glutamate receptor ionotropic. AMPA 1; AMPA-selective glutamate receptor 1 Polyclonal 0.1 ml
18-003-42968 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 mg Protein A
18-662-20065 Glutamate receptor 1 - GluR-1; GluR-A; GluR-K1; Glutamate receptor ionotropic. AMPA 1; AMPA-selective glutamate receptor 1 Polyclonal 0.1 ml
18-662-20050 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 ml
18-662-20051 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 ml
18-003-43297 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 mg Protein A
18-003-42645 Glutamate receptor. ionotropic kainate 2 - Glutamate receptor 6; GluR-6; GluR6; Excitatory amino acid receptor 4; EAA4 Polyclonal 0.1 mg Protein A
18-003-42646 Glutamate receptor. ionotropic kainate 2 - Glutamate receptor 6; GluR-6; GluR6; Excitatory amino acid receptor 4; EAA4 Polyclonal 0.05 mg Aff Pur
201-20-2385 GRIA2{glutamate receptor, ionotropic, AMPA 2}rabbit.pAb 0.2ml
E94801Ra ELISA Kit for Glutamate Receptor, Ionotropic, AMPA 1 (GRIA1) 96T/Kit
E11296h Human Glutamate Receptor, Ionotropic, AMPA 4 ELISA 96T
E11295h Human Glutamate Receptor, Ionotropic, AMPA 3 ELISA 96T
UB-E10079 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
E11294h Human Glutamate Receptor, Ionotropic, AMPA 2 ELISA 96T
E11293h Human Glutamate Receptor, Ionotropic, AMPA 1 ELISA 96T
201-11-1567 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
GRIA3 GRIA1 Gene glutamate receptor, ionotropic, AMPA 1
GRIA4 GRIA2 Gene glutamate receptor, ionotropic, AMPA 2
QY-E10079 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
UB-E20662 Mouse Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
201-12-3869 Human Glutamate Receptor, Ionotropic, AMPA 3(GRIA3)ELISA Kit 96T
GWB-245BF1 Anti- GRIA2 (glutamate receptor. ionotropic. AMPA 2) Antibody
UB-E05158 Human Glutamate Receptor, Ionotropic, AMPA 3(GRIA3)ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur