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P19491 (GRIA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor 2

Short name=GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name=GluA2
Gene names
Name:Gria2
Synonyms:Glur2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.19 Ref.20 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4 By similarity. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with NSF via its C-terminus. Interacts with CACNG2, PRKCABP and GRIP2. Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ domain) By similarity. Interacts with GRIA1 and SYNDIG1. 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 LRFN1. Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5. Ref.6 Ref.7 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.26 Ref.34 Ref.35

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Ref.6 Ref.12 Ref.14 Ref.19

Tissue specificity

Detected in forebrain. Detected in dendrites of neuronal cells. Ref.6 Ref.12 Ref.13

Developmental stage

Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 8 to 14 day old animals. Detected at intermediate levels at day 42 (at protein level). Ref.12

Domain

The M4 transmembrane segment mediates tetramerization and is required for cell surface expression By similarity.

Post-translational modification

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.

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.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA2 subfamily. [View classification]

RNA editing

Edited at position 607.
Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions By similarity. Ref.5

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
RNA editing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of protein localization

Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB

protein tetramerization

Inferred from direct assay Ref.34. Source: UniProtKB

receptor internalization

Inferred from direct assay PubMed 11100149. Source: UniProtKB

regulation of receptor recycling

Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB

regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 9697854. Source: UniProtKB

response to fungicide

Inferred from expression pattern PubMed 19591855. Source: RGD

response to lithium ion

Inferred from expression pattern PubMed 15269270. Source: UniProtKB

synaptic transmission

Inferred from direct assay PubMed 12554656. Source: RGD

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from direct assay Ref.19Ref.34. Source: UniProtKB

asymmetric synapse

Inferred from direct assay PubMed 12077196. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 19321442. Source: RGD

dendrite

Inferred from direct assay PubMed 15844209. Source: RGD

dendrite cytoplasm

Inferred from direct assay PubMed 17207780. Source: RGD

dendritic shaft

Inferred from direct assay Ref.11PubMed 11100149. Source: UniProtKB

dendritic spine

Inferred from direct assay PubMed 11348590. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from direct assay PubMed 12554656. Source: RGD

integral component of plasma membrane

Inferred from direct assay Ref.36. Source: UniProtKB

ionotropic glutamate receptor complex

Traceable author statement PubMed 11836517. Source: UniProtKB

neuronal cell body

Inferred from direct assay Ref.11PubMed 11100149. Source: UniProtKB

perikaryon

Inferred from direct assay PubMed 15844209. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 12077196. Source: RGD

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from direct assay PubMed 12554656. Source: RGD

protein complex

Inferred from physical interaction Ref.7. Source: UniProtKB

synapse

Inferred from direct assay Ref.7. Source: UniProtKB

synaptic vesicle membrane

Inferred from direct assay PubMed 12554656. Source: RGD

terminal bouton

Inferred from direct assay PubMed 15844209. Source: RGD

   Molecular_functionPDZ domain binding

Inferred from direct assay PubMed 10558890. Source: UniProtKB

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from direct assay Ref.19Ref.20. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 19461580Ref.35. Source: IntAct

ionotropic glutamate receptor activity

Inferred from direct assay Ref.34Ref.36. Source: UniProtKB

kainate selective glutamate receptor activity

Inferred from direct assay Ref.36. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18188153. Source: IntAct

protein kinase binding

Inferred from physical interaction PubMed 17329210. Source: RGD

receptor activity

Inferred from direct assay PubMed 11348590. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Flop (identifier: P19491-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Flip (identifier: P19491-2)

The sequence of this isoform differs from the canonical sequence as follows:
     765-766: NA → TP
     775-775: N → S
     779-779: L → V
     796-800: SGGGD → AKDSG
Isoform 3 (identifier: P19491-3)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     848-883: VAKNPQNINP...NVYGIESVKI → MTLSDVMRSK...GMNVSVTDLS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 883862Glutamate receptor 2
PRO_0000011535

Regions

Topological domain22 – 543522Extracellular Ref.34
Transmembrane544 – 56421Helical
Topological domain565 – 59127Cytoplasmic Ref.34
Intramembrane592 – 60716Helical; Pore-forming
Intramembrane608 – 6103
Topological domain611 – 6166Cytoplasmic Ref.34
Transmembrane617 – 63721Helical
Topological domain638 – 812175Extracellular Ref.34
Transmembrane813 – 83321Helical; Name=M4
Topological domain834 – 88350Cytoplasmic Ref.34
Region499 – 5013Glutamate binding
Region675 – 6762Glutamate binding

Sites

Binding site4711Glutamate
Binding site5061Glutamate
Binding site7261Glutamate

Amino acid modifications

Modified residue6831Phosphoserine; by PKC Ref.9
Modified residue7171Phosphoserine; by PKG Ref.9
Modified residue8761Phosphotyrosine Ref.13
Modified residue8801Phosphoserine By similarity
Lipidation6101S-palmitoyl cysteine By similarity
Lipidation8361S-palmitoyl cysteine By similarity
Glycosylation2561N-linked (GlcNAc...) Ref.35
Glycosylation3701N-linked (GlcNAc...) Ref.34 Ref.35
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 330 Ref.35 Ref.36
Disulfide bond739 ↔ 794 Ref.35 Ref.36

Natural variations

Alternative sequence765 – 7662NA → TP in isoform Flip.
VSP_000111
Alternative sequence7751N → S in isoform Flip.
VSP_000112
Alternative sequence7791L → V in isoform Flip.
VSP_000113
Alternative sequence796 – 8005SGGGD → AKDSG in isoform Flip.
VSP_000114
Alternative sequence848 – 88336VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3.
VSP_029310
Natural variant6071Q → R in RNA edited version.

Experimental info

Mutagenesis5041L → Y: Promotes dimerization. Strongly reduced desensitization. Ref.6 Ref.26
Mutagenesis7751N → D: Increases rate of desensitization. Ref.6 Ref.26
Mutagenesis851 – 8522NP → AA: Strongly reduces interaction with NSF. Ref.6

Secondary structure

.................................................................................................................................. 883
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Flop [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: DEFA817027C1CCD1

FASTA88398,688
        10         20         30         40         50         60 
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 

        70         80         90        100        110        120 
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 

       130        140        150        160        170        180 
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 

       190        200        210        220        230        240 
GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 

       250        260        270        280        290        300 
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 

       310        320        330        340        350        360 
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 

       370        380        390        400        410        420 
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 

       430        440        450        460        470        480 
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 

       490        500        510        520        530        540 
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 

       550        560        570        580        590        600 
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 

       610        620        630        640        650        660 
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 

       670        680        690        700        710        720 
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 

       730        740        750        760        770        780 
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 

       790        800        810        820        830        840 
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR 

       850        860        870        880 
AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI 

« Hide

Isoform Flip [UniParc].

Checksum: 3B70561B4F9E1C61
Show »

FASTA88398,745
Isoform 3 (Long) [UniParc].

Checksum: 13CE9B51B120A799
Show »

FASTA901100,409

References

[1]"A family of AMPA-selective glutamate receptors."
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H.
Science 249:556-560(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP).
Tissue: Brain.
[2]"Molecular cloning and functional expression of glutamate receptor subunit genes."
Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F.
Science 249:1033-1037(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
[3]"A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties."
Nakanishi N., Schneider N.A., Axel R.
Neuron 5:569-581(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
Tissue: Brain cortex and Hippocampus.
[4]"N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation."
Everts I., Villmann C., Hollmann M.
Mol. Pharmacol. 52:861-873(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), FUNCTION.
Strain: Sprague-Dawley.
[5]"RNA editing in brain controls a determinant of ion flow in glutamate-gated channels."
Sommer B., Koehler M., Sprengel R., Seeburg P.H.
Cell 67:11-19(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITION 607.
[6]"The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs."
Osten P., Srivastava S., Inman G.J., Vilim F.S., Khatri L., Lee L.M., States B.A., Einheber S., Milner T.A., Hanson P.I., Ziff E.B.
Neuron 21:99-110(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NSF, IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB, MUTAGENESIS OF 851-ASN-PRO-852.
[7]"Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
Xia J., Zhang X., Staudinger J., Huganir R.L.
Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCABP.
[8]"Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS."
Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.
Science 249:1580-1585(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
[9]"Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696."
Nakazawa K., Tadakuma T., Nokihara K., Ito M.
Neurosci. Res. 24:75-86(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-683 AND SER-717.
[10]"GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors."
Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.
Nature 386:279-284(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1.
Tissue: Hippocampus.
[11]"Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo."
Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., Standaert D.G., Weinberg R., Sheng M.
J. Neurosci. 19:6528-6537(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP2.
[12]"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors."
Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P.
Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[13]"Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases."
Hayashi T., Huganir R.L.
J. Neurosci. 24:6152-6160(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-876, TISSUE SPECIFICITY.
[14]"Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics."
Bedoukian M.A., Weeks A.M., Partin K.M.
J. Biol. Chem. 281:23908-23921(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
[15]"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN1.
[16]"AMPA receptor subunit-specific regulation by a distinct family of type II TARPs."
Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.
Neuron 59:986-996(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACNG5.
[17]"Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACNG5.
[18]Erratum
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
Nat. Neurosci. 12:808-808(2009)
[19]"Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors."
Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.
Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins."
Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.
Neuron 68:1082-1096(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior."
Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., Dawson V.L.
Cell 145:284-299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATAD1 AND GRIP1.
[22]"Structure of a glutamate-receptor ligand-binding core in complex with kainate."
Armstrong N., Sun Y., Chen G.Q., Gouaux E.
Nature 395:913-917(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE.
[23]"Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core."
Armstrong N., Gouaux E.
Neuron 28:165-181(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC.
[24]"Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate."
Jin R., Horning M., Mayer M.L., Gouaux E.
Biochemistry 41:15635-15643(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH QUISQUALATE, FUNCTION.
[25]"Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core."
Hogner A., Kastrup J.S., Jin R., Liljefors T., Mayer M.L., Egebjerg J., Larsen I.K., Gouaux E.
J. Mol. Biol. 322:93-109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA AND BR-HIBO.
[26]"Mechanism of glutamate receptor desensitization."
Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E.
Nature 417:245-253(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; DNQX AND KAINATE, FUNCTION, SUBUNIT, MUTAGENESIS OF LEU-504 AND ASN-775.
[27]"Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity."
Lunn M.-L., Hogner A., Stensboel T.B., Gouaux E., Egebjerg J., Kastrup J.S.
J. Med. Chem. 46:872-875(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA AND ZINC IONS.
[28]"Structural basis for partial agonist action at ionotropic glutamate receptors."
Jin R., Banke T.G., Mayer M.L., Traynelis S.F., Gouaux E.
Nat. Neurosci. 6:803-810(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH WILLARDIINES, FUNCTION.
[29]"Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes."
Armstrong N., Mayer M., Gouaux E.
Proc. Natl. Acad. Sci. U.S.A. 100:5736-5741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; KAINATE AND QUISQUALATE, FUNCTION.
[30]"Mechanism of positive allosteric modulators acting on AMPA receptors."
Jin R., Clark S., Weeks A.M., Dudman J.T., Gouaux E., Partin K.M.
J. Neurosci. 25:9027-9036(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ANIRACETAM AND CX614, FUNCTION.
[31]"Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2."
Frandsen A., Pickering D.S., Vestergaard B., Kasper C., Nielsen B.B., Greenwood J.R., Campiani G., Fattorusso C., Gajhede M., Schousboe A., Kastrup J.S.
Mol. Pharmacol. 67:703-713(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 AND KAINATE, FUNCTION.
[32]"Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor."
Armstrong N., Jasti J., Beich-Frandsen M., Gouaux E.
Cell 127:85-97(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[33]"The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209."
Kasper C., Pickering D.S., Mirza O., Olsen L., Kristensen A.S., Greenwood J.R., Liljefors T., Schousboe A., Waetjen F., Gajhede M., Sigurskjold B.W., Kastrup J.S.
J. Mol. Biol. 357:1184-1201(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND S1209, FUNCTION.
[34]"X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor."
Sobolevsky A.I., Rosconi M.P., Gouaux E.
Nature 462:745-756(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITH GLUTAMATE ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796, FUNCTION, SUBUNIT, MEMBRANE TOPOLOGY, GLYCOSYLATION AT ASN-370.
[35]"Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers."
Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M., Greger I.H.
EMBO J. 30:959-971(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-256 AND ASN-370.
[36]"Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations."
Ahmed A.H., Wang S., Chuang H.H., Oswald R.E.
J. Biol. Chem. 286:35257-35266(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 414-794 IN COMPLEXES WITH GLUTAMATE; IODOWILLARDIINE AND KAINATE, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36419 mRNA. Translation: AAA41244.1.
M38061 mRNA. Translation: AAC37652.1.
M85035 mRNA. Translation: AAA41240.1.
X54655 mRNA. Translation: CAA38465.1.
AF164344 mRNA. Translation: AAD51284.1.
PIRS13677.
RefSeqNP_001077280.1. NM_001083811.1.
NP_058957.1. NM_017261.2.
UniGeneRn.91361.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FTJX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1FTKX-ray1.60A404-528[»]
A653-796[»]
1FTLX-ray1.80A/B413-527[»]
A/B653-796[»]
1FTMX-ray1.70A/B/C413-527[»]
A/B/C653-796[»]
1FTOX-ray2.00A/B413-527[»]
A/B653-796[»]
1FW0X-ray1.90A413-527[»]
A653-796[»]
1GR2X-ray1.90A404-528[»]
A652-796[»]
1LB8X-ray2.30A/B413-527[»]
A/B653-796[»]
1LB9X-ray2.30A/B413-527[»]
A/B653-796[»]
1LBBX-ray2.10A413-527[»]
A653-796[»]
1LBCX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1M5BX-ray1.85A/B/C413-527[»]
A/B/C653-796[»]
1M5CX-ray1.65A413-527[»]
A653-796[»]
1M5DX-ray1.73A413-527[»]
A653-796[»]
1M5EX-ray1.46A/B/C413-527[»]
A/B/C653-796[»]
1M5FX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MM6X-ray2.15A/B413-527[»]
A/B653-796[»]
1MM7X-ray1.65A/B/C413-527[»]
A/B/C653-796[»]
1MQDX-ray1.46A/B/C/D413-527[»]
A/B/C/D653-794[»]
1MQGX-ray2.15A/B413-527[»]
A/B653-796[»]
1MQHX-ray1.80A413-527[»]
A653-796[»]
1MQIX-ray1.35A413-527[»]
A653-796[»]
1MQJX-ray1.65A413-527[»]
A653-796[»]
1MS7X-ray1.97A/B/C413-527[»]
A/B/C653-796[»]
1MXUX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1MXVX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MXWX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MXXX-ray2.00A/B/C413-527[»]
A/B/C653-796[»]
1MXYX-ray1.95A/B/C413-527[»]
A/B/C653-796[»]
1MXZX-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY0X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY1X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1MY2X-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
1MY3X-ray1.75A/B/C413-527[»]
A/B/C653-796[»]
1MY4X-ray1.90A/B/C413-527[»]
A/B/C653-796[»]
1N0TX-ray2.10A/B/C/D413-527[»]
A/B/C/D653-796[»]
1NNKX-ray1.85A413-527[»]
A653-796[»]
1NNPX-ray1.90A/B413-527[»]
A/B653-796[»]
1P1NX-ray1.60A413-527[»]
A653-796[»]
1P1OX-ray1.60A413-527[»]
A653-796[»]
1P1QX-ray2.00A/B/C413-527[»]
A/B/C653-796[»]
1P1UX-ray2.00A/B413-527[»]
A/B653-796[»]
1P1WX-ray1.80A/B413-527[»]
A/B653-796[»]
1SYHX-ray1.80A413-527[»]
A653-796[»]
1SYIX-ray2.10A/B413-527[»]
A/B653-796[»]
1WVJX-ray1.75A413-527[»]
A653-796[»]
1XHYX-ray1.85A413-527[»]
A653-796[»]
2AIXX-ray2.17A413-527[»]
A653-796[»]
2AL4X-ray1.70A/B/C/D/E/F413-527[»]
A/B/C/D/E/F653-796[»]
2AL5X-ray1.65A/B413-527[»]
A/B653-796[»]
2ANJX-ray2.10A413-527[»]
A653-796[»]
2CMOX-ray2.65A/B413-527[»]
A/B653-796[»]
2GFEX-ray1.54A/B/C413-527[»]
A/B/C653-795[»]
2I3VX-ray2.40A/B/C/D413-527[»]
A/B/C/D655-794[»]
2I3WX-ray2.30A/B413-527[»]
A/B653-794[»]
2P2AX-ray2.26A/B413-527[»]
A/B653-796[»]
2UXAX-ray2.38A/B/C412-795[»]
2XX7X-ray2.20A/B/C413-527[»]
A/B/C653-795[»]
2XX8X-ray1.55A/B/C413-527[»]
A/B/C653-796[»]
2XX9X-ray1.97A/B/C413-527[»]
A/B/C653-796[»]
2XXHX-ray1.50A/B/C413-527[»]
A/B/C653-796[»]
2XXIX-ray1.60A/B/C413-527[»]
A/B/C653-796[»]
3B6QX-ray2.00A413-527[»]
A653-796[»]
3B6TX-ray2.10A413-527[»]
A653-796[»]
3B6WX-ray1.70A/B/C/D413-527[»]
A/B/C/D653-796[»]
3B7DX-ray2.50A/B/C/D/E/F/G/H413-527[»]
A/B/C/D/E/F/G/H653-794[»]
3BBRX-ray2.25A/B413-527[»]
A/B653-796[»]
3BFTX-ray2.27A/B/C413-527[»]
A/B/C653-796[»]
3BFUX-ray1.95A/B/C/D413-527[»]
A/B/C/D653-796[»]
3BKIX-ray1.87B/C/D/P413-527[»]
B/C/D/P653-796[»]
3DP6X-ray1.55A/B/C413-527[»]
A/B/C653-794[»]
3H03X-ray1.90A/B/D/G414-527[»]
A/B/D/G653-794[»]
3H06X-ray2.80B/E/G/H/J/L/N/P414-527[»]
B/E/G/H/J/L/N/P653-794[»]
3H5VX-ray2.33A/B/C21-404[»]
3H5WX-ray2.69A/B21-404[»]
3H6TX-ray2.25A/B/C413-527[»]
A/B/C653-796[»]
3H6UX-ray1.85A413-527[»]
A653-796[»]
3H6VX-ray2.10A/B413-527[»]
A/B653-796[»]
3H6WX-ray1.49A/B413-527[»]
A/B653-796[»]
3HSYX-ray1.75A/B25-400[»]
3IJOX-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3IJXX-ray2.88B/D/H414-527[»]
B/D/H653-794[»]
3IK6X-ray2.10B/E/H414-527[»]
B/E/H653-794[»]
3IL1X-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3ILTX-ray2.11B/E/H414-527[»]
B/E/H653-794[»]
3ILUX-ray2.00B/E/H414-527[»]
B/E/H653-794[»]
3KG2X-ray3.60A/B/C/D25-412[»]
A/B/C/D414-847[»]
3KGCX-ray1.55A/B414-527[»]
A/B654-795[»]
3LSFX-ray1.85B/E/H414-527[»]
B/E/H653-794[»]
3LSLX-ray2.12A/D/G414-527[»]
A/D/G653-794[»]
3M3LX-ray1.85A/D/G414-794[»]
3N6VX-ray3.20A/B/C/D/E/F27-400[»]
3O28X-ray2.00A413-527[»]
A653-795[»]
3O29X-ray2.02A413-527[»]
A653-795[»]
3O2AX-ray1.90A413-527[»]
A653-795[»]
3O2JX-ray1.95A/B22-400[»]
3O6GX-ray1.80A413-527[»]
A653-795[»]
3O6HX-ray2.10A413-527[»]
A653-795[»]
3O6IX-ray1.80A413-527[»]
A653-795[»]
3PD8X-ray2.48A/B/C413-527[»]
A/B/C653-795[»]
3PD9X-ray2.10A/B413-527[»]
A/B653-795[»]
3PMVX-ray1.80A413-527[»]
A653-795[»]
3PMWX-ray2.20A413-527[»]
A653-795[»]
3PMXX-ray1.87A413-527[»]
A653-795[»]
3RTFX-ray1.70B/D/F414-527[»]
B/D/F653-794[»]
3RTWX-ray2.10B/D/F414-527[»]
B/D/F653-794[»]
3T93X-ray1.91B/D/F414-527[»]
B/D/F653-794[»]
3T96X-ray1.87B/D/F414-527[»]
B/D/F653-794[»]
3T9HX-ray2.02B/D/F414-527[»]
B/D/F653-794[»]
3T9UX-ray1.97A/B/C414-527[»]
A/B/C653-794[»]
3T9VX-ray1.98A/B414-527[»]
A/B653-794[»]
3T9XX-ray1.82B/D/F414-527[»]
B/D/F653-794[»]
3TDJX-ray1.95A/B413-527[»]
A/B653-796[»]
3TKDX-ray1.45A/B413-527[»]
A/B653-795[»]
3TZAX-ray1.90A/B413-527[»]
A/B653-796[»]
4FATX-ray1.40A413-527[»]
A653-796[»]
4G8MX-ray2.05A/B413-527[»]
A/B653-796[»]
4GXSX-ray1.96B/D414-527[»]
B/D653-794[»]
4H8JX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
4IGTX-ray1.24A413-527[»]
A653-796[»]
4ISUX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-796[»]
4IY5X-ray2.00A/B413-527[»]
A/B653-796[»]
4IY6X-ray1.72A413-527[»]
A653-796[»]
4L17X-ray2.80A/C/E/G413-527[»]
A/C/E/G653-796[»]
4LZ5X-ray1.50A/B/C404-527[»]
A/B/C653-796[»]
4LZ7X-ray2.10A/B/C404-527[»]
A/B/C653-796[»]
4LZ8X-ray1.85A/B/C404-527[»]
A/B/C653-796[»]
4N07X-ray1.87A/B/C413-527[»]
A/B/C653-796[»]
4O3AX-ray1.80A/B/C413-527[»]
A/B/C653-796[»]
4O3BX-ray1.91A/B413-527[»]
A/B653-796[»]
4O3CX-ray1.50A413-527[»]
A653-796[»]
ProteinModelPortalP19491.
SMRP19491. Positions 412-527, 655-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248250. 6 interactions.
DIPDIP-30952N.
IntActP19491. 20 interactions.
MINTMINT-86056.

Chemistry

BindingDBP19491.
ChEMBLCHEMBL3503.
DrugBankDB00606. Cyclothiazide.
GuidetoPHARMACOLOGY445.

PTM databases

PhosphoSiteP19491.

Proteomic databases

PaxDbP19491.
PRIDEP19491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29627.
KEGGrno:29627.
UCSCRGD:61862. rat. [P19491-1]

Organism-specific databases

CTD2891.
RGD61862. Gria2.

Phylogenomic databases

eggNOGNOG316680.
HOGENOMHOG000234372.
HOVERGENHBG051839.
KOK05198.
PhylomeDBP19491.

Gene expression databases

GenevestigatorP19491.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP19491.
NextBio609842.

Entry information

Entry nameGRIA2_RAT
AccessionPrimary (citable) accession number: P19491
Secondary accession number(s): Q9R174
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references