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Protein

Glutamate receptor 2

Gene

Gria2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (PubMed:16037816).15 Publications

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei471Glutamate1 Publication1
Binding sitei501Kainate; via amide nitrogen1 Publication1
Binding sitei506Glutamate1 Publication1
Binding sitei506Kainate1 Publication1
Sitei654Crucial to convey clamshell closure to channel opening1 Publication1
Binding sitei675Kainate; via amide nitrogen1 Publication1
Binding sitei676Kainate; via amide nitrogen1 Publication1
Binding sitei726Glutamate1 Publication1
Binding sitei726Kainate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 2Curated
Short name:
GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name:
GluA21 Publication
Gene namesi
Name:Gria2Imported
Synonyms:Glur2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61862 Gria2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 543ExtracellularAdd BLAST522
Transmembranei544 – 564HelicalAdd BLAST21
Topological domaini565 – 591CytoplasmicAdd BLAST27
Intramembranei592 – 607Helical; Pore-formingAdd BLAST16
Intramembranei608 – 6103
Topological domaini611 – 616Cytoplasmic6
Transmembranei617 – 637HelicalAdd BLAST21
Topological domaini638 – 812ExtracellularAdd BLAST175
Transmembranei813 – 833Helical; Name=M4Add BLAST21
Topological domaini834 – 883CytoplasmicAdd BLAST50

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi504L → Y: Promotes dimerization. Strongly reduced desensitization. 1 Publication1
Mutagenesisi775N → D: Increases rate of desensitization. 1 Publication1
Mutagenesisi851 – 852NP → AA: Strongly reduces interaction with NSF. 1 Publication2

Chemistry databases

ChEMBLiCHEMBL3503
GuidetoPHARMACOLOGYi445

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001153522 – 883Glutamate receptor 2Add BLAST862

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi78 ↔ 330
Glycosylationi256N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi370N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi610S-palmitoyl cysteineBy similarity1
Modified residuei683Phosphoserine; by PKC1 Publication1
Modified residuei717Phosphoserine; by PKG1 Publication1
Disulfide bondi739 ↔ 794
Lipidationi836S-palmitoyl cysteineBy similarity1
Modified residuei860PhosphoserineBy similarity1
Modified residuei863PhosphoserineBy similarity1
Modified residuei876Phosphotyrosine1 Publication1
Modified residuei880PhosphoserineBy similarity1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP19491
PRIDEiP19491

PTM databases

iPTMnetiP19491
PhosphoSitePlusiP19491
SwissPalmiP19491

Expressioni

Tissue specificityi

Detected in forebrain. Detected in dendrites of neuronal cells.3 Publications

Developmental stagei

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).1 Publication

Interactioni

Subunit structurei

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 (PubMed:27756895). 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. Interacts with OLFM2 (By similarity). Interacts with AP4B1, AP4E1 and AP4M1; probably indirect it mediates the somatodendritic localization of GRIA2 in neurons (By similarity). Forms a complex with NSG1, GRIA2 and STX12; controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (PubMed:16037816).By similarity18 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei474Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei681Interaction with the cone snail toxin Con-ikot-ikot1 Publication1
Sitei773Interaction with the cone snail toxin Con-ikot-ikot1 Publication1

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248250, 9 interactors
CORUMiP19491
DIPiDIP-30952N
ELMiP19491
IntActiP19491, 27 interactors
MINTiP19491
STRINGi10116.ENSRNOP00000062152

Chemistry databases

BindingDBiP19491

Structurei

Secondary structure

1883
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP19491
SMRiP19491
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19491

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni499 – 501Glutamate binding3
Regioni675 – 676Glutamate binding2

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
HOGENOMiHOG000234372
HOVERGENiHBG051839
InParanoidiP19491
KOiK05198
PhylomeDBiP19491

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Flop (identifier: P19491-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ
60 70 80 90 100
FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI
110 120 130 140 150
TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY
160 170 180 190 200
LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE
210 220 230 240 250
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI
260 270 280 290 300
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
310 320 330 340 350
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ
360 370 380 390 400
VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT
410 420 430 440 450
ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA
460 470 480 490 500
AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL
510 520 530 540 550
TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI
560 570 580 590 600
VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
610 620 630 640 650
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM
660 670 680 690 700
VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP
710 720 730 740 750
SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS
760 770 780 790 800
KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD
810 820 830 840 850
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK
860 870 880
NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI
Length:883
Mass (Da):98,688
Last modified:July 15, 1998 - v2
Checksum:iDEFA817027C1CCD1
GO
Isoform Flip (identifier: P19491-2) [UniParc]FASTAAdd to basket

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

Show »
Length:883
Mass (Da):98,745
Checksum:i3B70561B4F9E1C61
GO
Isoform 3 (identifier: P19491-3) [UniParc]FASTAAdd to basket
Also known as: Long

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

Show »
Length:901
Mass (Da):100,409
Checksum:i13CE9B51B120A799
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LNE4F1LNE4_RAT
Glutamate receptor 2
Gria2
883Annotation score:
G3V914G3V914_RAT
Glutamate receptor 2
Gria2
883Annotation score:

RNA editingi

Edited at position 607.1 Publication
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).By similarity

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti607Q → R in RNA edited version. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000111765 – 766NA → TP in isoform Flip. 3 Publications2
Alternative sequenceiVSP_000112775N → S in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000113779L → V in isoform Flip. 3 Publications1
Alternative sequenceiVSP_000114796 – 800SGGGD → AKDSG in isoform Flip. 3 Publications5
Alternative sequenceiVSP_029310848 – 883VAKNP…ESVKI → MTLSDVMRSKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiS13677
RefSeqiNP_001077280.1, NM_001083811.1
NP_058957.1, NM_017261.2
UniGeneiRn.91361

Genome annotation databases

GeneIDi29627
KEGGirno:29627
UCSCiRGD:61862 rat [P19491-1]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiS13677
RefSeqiNP_001077280.1, NM_001083811.1
NP_058957.1, NM_017261.2
UniGeneiRn.91361

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Q30X-ray2.03B/D/F414-527[»]
B/D/F653-794[»]
4U1OX-ray1.85A413-527[»]
A653-796[»]
4U1WX-ray3.25A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U1XX-ray3.30A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1YX-ray3.90A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-847[»]
4U1ZX-ray1.94A413-527[»]
A653-796[»]
4U21X-ray1.39A/B413-527[»]
A/B654-796[»]
4U22X-ray1.44A413-527[»]
A653-796[»]
4U23X-ray1.67A413-527[»]
A653-796[»]
4U2PX-ray3.24A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2QX-ray3.52A/B/C/D25-412[»]
A/B/C/D414-622[»]
A/B/C/D624-847[»]
4U2RX-ray1.41A/B/C/D413-527[»]
A/B/C/D653-796[»]
4U4FX-ray4.79A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4GX-ray4.49A/B/C/D25-412[»]
A/B/C/D414-847[»]
4U4SX-ray1.90A/B413-527[»]
A/B653-796[»]
4U4XX-ray1.56A/B413-527[»]
A/B653-796[»]
4U5BX-ray3.50A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5CX-ray3.69A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5DX-ray3.58A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5EX-ray3.51A/B/C/D25-412[»]
A/B/C/D414-555[»]
A/B/C/D557-602[»]
A/B/C/D604-622[»]
A/B/C/D624-850[»]
4U5FX-ray3.70A/B/C/D25-412[»]
A/B/C/D414-850[»]
4UQ6electron microscopy12.80A/B/C/D22-847[»]
4UQJelectron microscopy10.40A/B/C/D22-847[»]
4UQKelectron microscopy16.40A/B/C/D22-847[»]
4X48X-ray1.89A/B/C413-527[»]
A/B/C653-796[»]
4YMAX-ray1.90A/B413-527[»]
A/B653-797[»]
4YU0X-ray1.26A/B413-527[»]
A/B653-796[»]
4Z0IX-ray1.45A/B413-527[»]
A/B653-796[»]
5BUUX-ray2.07A/B413-527[»]
A/B653-796[»]
5CBRX-ray2.00A413-527[»]
A653-797[»]
5CBSX-ray1.80A/B/C/D413-527[»]
A/B/C/D653-797[»]
5ELVX-ray1.92A/B413-527[»]
A/B653-797[»]
5FHMX-ray1.55A/B413-527[»]
A/B653-797[»]
5FHNX-ray1.60A413-527[»]
A653-797[»]
5FHOX-ray2.30A/B/C/D413-527[»]
A/B/C/D653-797[»]
5FTHX-ray2.90A/B/C404-527[»]
A/B/C653-795[»]
5FTIX-ray1.35A/B404-527[»]
A/B653-795[»]
5FWXX-ray2.50A/C25-400[»]
5FWYX-ray2.12A/C25-400[»]
5IDEelectron microscopy8.25A/C23-883[»]
5IDFelectron microscopy10.31A/C23-883[»]
5JEIX-ray1.23A413-527[»]
A653-797[»]
5KBSelectron microscopy8.70A/B/C/D25-847[»]
5KBTelectron microscopy6.40A/B/C/D25-847[»]
5KBUelectron microscopy7.80A/B/C/D25-847[»]
5KBVelectron microscopy6.80A/B/C/D25-412[»]
A/B/C/D414-847[»]
5KK2electron microscopy7.30A/B/C/D1-883[»]
5L1BX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1EX-ray4.37A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1FX-ray4.00A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1GX-ray4.51A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5L1HX-ray3.80A/B/C/D25-412[»]
A/B/C/D414-565[»]
A/B/C/D588-847[»]
5N6PX-ray2.80A25-400[»]
5NG9X-ray1.15A413-527[»]
A653-797[»]
5NIHX-ray1.30A/B413-527[»]
A/B653-797[»]
5NS9X-ray1.44A/B413-527[»]
A/B653-797[»]
5O9AX-ray1.78A/B/C/D413-527[»]
A/B/C/D653-797[»]
5OEWX-ray2.00A/B/C413-527[»]
A/B/C653-797[»]
5VHWelectron microscopy7.80A/B/C/D25-847[»]
5VHXelectron microscopy8.30A/B/C/D/E25-847[»]
5VHYelectron microscopy4.60A/B/C/D/E/F25-847[»]
5VHZelectron microscopy8.40A/B/C/D/E/F25-847[»]
5VOTelectron microscopy4.90A/B/C/D1-883[»]
5VOUelectron microscopy6.40A/B/C/D1-883[»]
5VOVelectron microscopy7.70A/B/C/D1-883[»]
5WEKelectron microscopy4.60A/B/C/D25-847[»]
5WELelectron microscopy4.40A/B/C/D25-847[»]
5WEMelectron microscopy6.10A/B/C/D25-847[»]
5WENelectron microscopy6.80A/B/C/D25-847[»]
5WEOelectron microscopy4.20A/B/C/D25-847[»]
6DLZelectron microscopy3.90A/B/C/D25-847[»]
6DM0electron microscopy4.40A/B/C/D25-847[»]
6DM1electron microscopy4.20A/B/C/D25-847[»]
6DM2electron microscopy4.60A/B/C/D25-847[»]
ProteinModelPortaliP19491
SMRiP19491
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248250, 9 interactors
CORUMiP19491
DIPiDIP-30952N
ELMiP19491
IntActiP19491, 27 interactors
MINTiP19491
STRINGi10116.ENSRNOP00000062152

Chemistry databases

BindingDBiP19491
ChEMBLiCHEMBL3503
GuidetoPHARMACOLOGYi445

PTM databases

iPTMnetiP19491
PhosphoSitePlusiP19491
SwissPalmiP19491

Proteomic databases

PaxDbiP19491
PRIDEiP19491

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29627
KEGGirno:29627
UCSCiRGD:61862 rat [P19491-1]

Organism-specific databases

CTDi2891
RGDi61862 Gria2

Phylogenomic databases

eggNOGiKOG1054 Eukaryota
ENOG410XPSH LUCA
HOGENOMiHOG000234372
HOVERGENiHBG051839
InParanoidiP19491
KOiK05198
PhylomeDBiP19491

Miscellaneous databases

EvolutionaryTraceiP19491
PROiPR:P19491

Family and domain databases

InterProiView protein in InterPro
IPR001828 ANF_lig-bd_rcpt
IPR019594 Glu/Gly-bd
IPR001508 Iono_rcpt_met
IPR001320 Iontro_rcpt
IPR028082 Peripla_BP_I
PfamiView protein in Pfam
PF01094 ANF_receptor, 1 hit
PF00060 Lig_chan, 1 hit
PF10613 Lig_chan-Glu_bd, 1 hit
PRINTSiPR00177 NMDARECEPTOR
SMARTiView protein in SMART
SM00918 Lig_chan-Glu_bd, 1 hit
SM00079 PBPe, 1 hit
SUPFAMiSSF53822 SSF53822, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGRIA2_RAT
AccessioniPrimary (citable) accession number: P19491
Secondary accession number(s): Q9R174
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: November 7, 2018
This is version 212 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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