Reviewed, UniProtKB/Swiss-Prot P19491 (GRIA2_RAT)

Names and origin

Protein names

Recommended name:
    Glutamate receptor 2
      Short name=GluR-2
Alternative name(s):
    GluR-B
    GluR-K2
    Glutamate receptor ionotropic, AMPA 2
    AMPA-selective glutamate receptor 2

Gene names

Name:	Gria2
Synonyms:	Glur2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	883 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.4 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26
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 CACNG2, PRKCABP, GRIP1 and GRIP2. Interacts with NSF via its C-terminus. Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ domain) By similarity. Ref.19 Ref.6 Ref.7 Ref.10 Ref.11 Ref.14
Subcellular location	Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Note: Interaction with CACNG2 promotes cell surface expression. Ref.6 Ref.14 Ref.12
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
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) family. [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 process	Ion transport Transport
Cellular component	Cell junction Cell membrane Endoplasmic reticulum Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing RNA editing
Domain	Signal Transmembrane
Molecular function	Ionic channel Receptor
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	establishment of protein localization Inferred from mutant phenotype. Source: UniProtKB ion transport Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of synaptic transmission Inferred from mutant phenotype. Source: UniProtKB receptor internalization Inferred from direct assay. Source: UniProtKB regulation of receptor recycling Inferred from mutant phenotype. Source: UniProtKB regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype. Source: UniProtKB response to lithium ion Inferred from expression pattern. Source: UniProtKB synaptic transmission Inferred from physical interaction. Source: RGD
Cellular component	asymmetric synapse Inferred from direct assay. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW dendrite cytoplasm Inferred from direct assay. Source: RGD dendritic shaft Ref.11 Inferred from direct assay. Source: UniProtKB dendritic spine Inferred from direct assay. Source: UniProtKB endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW growth cone Inferred from direct assay. Source: RGD ionotropic glutamate receptor complex Traceable author statement. Source: UniProtKB perikaryon Inferred from direct assay. Source: RGD postsynaptic density Inferred from direct assay. Source: RGD postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW presynaptic membrane Inferred from direct assay. Source: RGD synaptic vesicle membrane Inferred from direct assay. Source: RGD terminal button Inferred from direct assay. Source: RGD
Molecular function	PDZ domain binding Ref.7 Inferred from direct assay. Source: UniProtKB alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Traceable author statement. Source: RGD extracellular-glutamate-gated ion channel activity Inferred from electronic annotation. Source: InterPro protein kinase binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Grip2	Q9WTW1-3	4	EBI-77718,EBI-936068
Mpp4	Q9QYH1	1	EBI-77718,EBI-937554
NSF	P18708	1	EBI-77718,EBI-925742	From a different organism.
Nsf	Q9QUL6	4	EBI-77718,EBI-925794
Pick1	Q9EP80	6	EBI-77718,EBI-77728

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 883

862

Glutamate receptor 2

PRO_0000011535

Regions

Topological domain

22 – 543

522

Extracellular Potential

Transmembrane

544 – 564

21

Potential

Topological domain

565 – 624

60

Cytoplasmic Potential

Transmembrane

625 – 645

21

Potential

Topological domain

646 – 812

167

Extracellular Potential

Transmembrane

813 – 833

21

Potential

Topological domain

834 – 883

50

Cytoplasmic Potential

Region

499 – 501

3

Glutamate binding

Region

675 – 676

2

Glutamate binding

Sites

Binding site

506

1

Glutamate

Binding site

726

1

Glutamate

Amino acid modifications

Modified residue

683

1

Phosphoserine; by PKC Ref.9

Modified residue

717

1

Phosphoserine; by PKG Ref.9

Modified residue

869

1

Phosphotyrosine By similarity

Modified residue

876

1

Phosphotyrosine Ref.13

Modified residue

880

1

Phosphoserine By similarity

Lipidation

610

1

S-palmitoyl cysteine By similarity

Lipidation

836

1

S-palmitoyl cysteine By similarity

Glycosylation

256

1

N-linked (GlcNAc...) Potential

Glycosylation

370

1

N-linked (GlcNAc...) Potential

Glycosylation

406

1

N-linked (GlcNAc...) Potential

Glycosylation

413

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

765 – 766

2

NA → TP in isoform Flip.

VSP_000111

Alternative sequence

775

1

N → S in isoform Flip.

VSP_000112

Alternative sequence

779

1

L → V in isoform Flip.

VSP_000113

Alternative sequence

796 – 800

5

SGGGD → AKDSG in isoform Flip.

VSP_000114

Alternative sequence

848 – 883

36

VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3.

VSP_029310

Natural variant

607

1

Q → R in RNA edited version.

Experimental info

Mutagenesis

504

1

L → Y: Promotes dimerization. Strongly reduced desensitization. Ref.19 Ref.6

Mutagenesis

775

1

N → D: Increases rate of desensitization. Ref.19 Ref.6

Mutagenesis

851 – 852

2

NP → AA: Strongly reduces interaction with NSF. Ref.6

Secondary structure

1

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883

Helix Strand Turn

Details...

Beta strand

416 – 420

5

Turn

424 – 426

3

Beta strand

427 – 429

3

Helix

433 – 435

3

Helix

438 – 441

4

Beta strand

442 – 444

3

Helix

445 – 457

13

Beta strand

461 – 465

5

Turn

476 – 478

3

Helix

483 – 489

7

Beta strand

494 – 496

3

Helix

504 – 507

4

Beta strand

510 – 512

3

Beta strand

516 – 519

4

Beta strand

521 – 526

6

Helix

657 – 662

6

Beta strand

664 – 671

8

Helix

675 – 682

8

Helix

686 – 697

12

Beta strand

704 – 706

3

Helix

707 – 716

10

Turn

717 – 719

3

Beta strand

720 – 726

7

Helix

727 – 733

7

Beta strand

741 – 745

5

Beta strand

751 – 753

3

Beta strand

756 – 758

3

Helix

764 – 776

13

Helix

779 – 788

10

Turn

789 – 791

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Flop [UniParc]. Last modified July 15, 1998. Version 2. Checksum: DEFA817027C1CCD1	FASTA	883	98,688
	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
	Isoform Flip. Checksum: 3B70561B4F9E1C61	FASTA	883	98,745
	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 SSLGTPVNLA VLKLSEQGVL 790 800 810 820 830 840 DKLKNKWWYD KGECGAKDSG SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR 850 860 870 880 AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI
	Isoform 3 (Long). Checksum: 13CE9B51B120A799	FASTA	901	100,409
	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 850 860 870 880 890 900 AEAKRMKMTL SDVMRSKARL SITGSTGENG RVMTPEFPKA VHAVPYVSPG MGMNVSVTDL S

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: 2166337] [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: 2168579] [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: 1699567] [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: 9351977] [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: 1717158] [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: 9697855] [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: 10027300] [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: 1699275] [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: 8848293] [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: 9069286] [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: 10414981] [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: 14687553] [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: 15240807] [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: 16793768] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
[15]	"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: 9804426] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE.
[16]	"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: 11086992] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC.
[17]	"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: 12501192] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH QUISQUALATE, FUNCTION.
[18]	"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: 12215417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA AND BR-HIBO.
[19]	"Mechanism of glutamate receptor desensitization." Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E. Nature 417:245-253(2002) [PubMed: 12015593] [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.
[20]	"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: 12593667] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA AND ZINC IONS.
[21]	"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: 12872125] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH WILLARDIINES, FUNCTION.
[22]	"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: 12730367] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; KAINATE AND QUISQUALATE, FUNCTION.
[23]	"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: 16192394] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ANIRACETAM AND CX614, FUNCTION.
[24]	"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: 15591246] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 AND KAINATE, FUNCTION.
[25]	"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: 17018279] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, MASS SPECTROMETRY.
[26]	"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: 16483599] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND S1209, FUNCTION.
+	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.

IPI

IPI00231061.
IPI00324625.
IPI00876626.

PIR

S13677.

RefSeq

NP_001077280.1.
NP_058957.1.

UniGene

Rn.91361

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FTJ	X-ray	1.90	A/B/C	413-796	[»]
1FTK	X-ray	1.60	A	404-796	[»]
1FTL	X-ray	1.80	A/B	413-796	[»]
1FTM	X-ray	1.70	A/B/C	413-796	[»]
1FTO	X-ray	2.00	A/B	413-796	[»]
1FW0	X-ray	1.90	A	413-796	[»]
1GR2	X-ray	1.90	A	404-796	[»]
1LB8	X-ray	2.30	A/B	413-796	[»]
1LB9	X-ray	2.30	A/B	413-796	[»]
1LBB	X-ray	2.10	A	413-796	[»]
1LBC	X-ray	1.80	A/B/C	413-796	[»]
1M5B	X-ray	1.85	A/B/C	413-796	[»]
1M5C	X-ray	1.65	A	413-796	[»]
1M5D	X-ray	1.73	A	413-796	[»]
1M5E	X-ray	1.46	A/B/C	413-796	[»]
1M5F	X-ray	1.95	A/B/C	413-796	[»]
1MM6	X-ray	2.15	A/B	413-796	[»]
1MM7	X-ray	1.65	A/B/C	413-796	[»]
1MQD	X-ray	1.46	A/B/C/D	413-794	[»]
1MQG	X-ray	2.15	A/B	413-796	[»]
1MQH	X-ray	1.80	A	413-796	[»]
1MQI	X-ray	1.35	A	413-796	[»]
1MQJ	X-ray	1.65	A	413-796	[»]
1MS7	X-ray	1.97	A/B/C	413-796	[»]
1MXU	X-ray	1.80	A/B/C	413-796	[»]
1MXV	X-ray	1.95	A/B/C	413-796	[»]
1MXW	X-ray	1.90	A/B/C	413-796	[»]
1MXX	X-ray	2.00	A/B/C	413-796	[»]
1MXY	X-ray	1.95	A/B/C	413-796	[»]
1MXZ	X-ray	1.90	A/B/C	413-796	[»]
1MY0	X-ray	1.90	A/B/C	413-796	[»]
1MY1	X-ray	1.90	A/B/C	413-796	[»]
1MY2	X-ray	1.80	A/B/C	413-796	[»]
1MY3	X-ray	1.75	A/B/C	413-796	[»]
1MY4	X-ray	1.90	A/B/C	413-796	[»]
1N0T	X-ray	2.10	A/B/C/D	413-796	[»]
1NNK	X-ray	1.85	A	413-796	[»]
1NNP	X-ray	1.90	A/B	413-796	[»]
1P1N	X-ray	1.60	A	413-796	[»]
1P1O	X-ray	1.60	A	413-796	[»]
1P1Q	X-ray	2.00	A/B/C	413-796	[»]
1P1U	X-ray	2.00	A/B	413-796	[»]
1P1W	X-ray	1.80	A/B	413-796	[»]
1SYH	X-ray	1.80	A	413-796	[»]
1SYI	X-ray	2.10	A/B	413-796	[»]
1WVJ	X-ray	1.75	A	413-796	[»]
1XHY	X-ray	1.85	A	413-796	[»]
2AIX	X-ray	2.17	A	413-796	[»]
2AL4	X-ray	1.70	A/B/C/D/E/F	413-796	[»]
2AL5	X-ray	1.65	A/B	413-796	[»]
2ANJ	X-ray	2.10	A	413-796	[»]
2CMO	X-ray	2.65	A/B	413-796	[»]
2GFE	X-ray	1.54	A/B/C	413-795	[»]
2I3V	X-ray	2.40	A/B/C/D	413-794	[»]
2I3W	X-ray	2.30	A/B	413-794	[»]
2P2A	X-ray	2.26	A/B	413-796	[»]
2UXA	X-ray	2.38	A/B/C	412-795	[»]
3B6Q	X-ray	2.00	A	413-796	[»]
3B6T	X-ray	2.10	A	413-796	[»]
3B6W	X-ray	1.70	A/B/C/D	413-796	[»]
3B7D	X-ray	2.50	A/B/C/D/E/F/G/H	413-794	[»]
3BBR	X-ray	2.25	A/B	413-796	[»]
3BFT	X-ray	2.27	A/B/C	413-796	[»]
3BFU	X-ray	1.95	A/B/C/D	413-796	[»]
3BKI	X-ray	1.87	B/C/D/P	413-796	[»]
3DP6	X-ray	1.55	A/B/C	404-796	[»]
3H03	X-ray	1.90	A/B/D/G	414-794	[»]
3H06	X-ray	2.80	B/E/G/H/J/L/N/P	414-794	[»]
3H5V	X-ray	2.33	A/B/C	21-404	[»]
3H5W	X-ray	2.69	A/B	21-404	[»]
3H6T	X-ray	2.25	A/B/C	413-796	[»]
3H6U	X-ray	1.85	A	413-796	[»]
3H6V	X-ray	2.10	A/B	413-796	[»]
3H6W	X-ray	1.49	A/B	413-796	[»]
3IJO	X-ray	2.00	B/E/H	414-794	[»]
3IJX	X-ray	2.88	B/D/H	414-794	[»]
3IK6	X-ray	2.10	B/E/H	414-794	[»]
3IL1	X-ray	2.00	B/E/H	414-794	[»]
3ILT	X-ray	2.11	B/E/H	414-794	[»]
3ILU	X-ray	2.00	B/E/H	414-794	[»]
3KG2	X-ray	3.60	A/B/C/D	25-847	[»]
3KGC	X-ray	1.55	A/B	413-796	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P19491. 8 interactions.

STRING

P19491.

PTM databases

PhosphoSite

P19491.

Genome annotation databases

Ensembl

ENSRNOT00000039610; ENSRNOP00000035005; ENSRNOG00000028589; Rattus norvegicus. [Genome view]

GeneID

29627.

KEGG

rno:29627.

Organism-specific databases

CTD

29627.

RGD

61862. Gria2.

Phylogenomic databases

eggNOG

roNOG15544.

HOVERGEN

P19491.

Gene expression databases

ArrayExpress

P19491.

Genevestigator

P19491.

GermOnline

ENSRNOG00000028589. Rattus norvegicus.

Family and domain databases

InterPro

IPR001828. ANF_lig_bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR015683. Glutamate_receptor-rel.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
[Graphical view]

PANTHER

PTHR18966. Glut_Rec_Related. 1 hit.

Pfam

PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]

PRINTS

PR00177. NMDARECEPTOR.

SMART

SM00079. PBPe. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00606. Cyclothiazide.

NextBio

609842.

Entry information

Entry name

GRIA2_RAT

Accession

Primary (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:	February 9, 2010
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)