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P19492

- GRIA3_RAT

UniProt

P19492 - GRIA3_RAT

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Protein

Glutamate receptor 3

Gene

Gria3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei474 – 4741Glutamate2 Publications
Binding sitei509 – 5091Glutamate2 Publications
Binding sitei731 – 7311Glutamate2 Publications

GO - Molecular functioni

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: RGD
  2. extracellular-glutamate-gated ion channel activity Source: RefGenome
  3. ionotropic glutamate receptor activity Source: RGD
  4. PDZ domain binding Source: UniProtKB

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: GOC
  2. ion transmembrane transport Source: GOC
  3. regulation of receptor recycling Source: UniProtKB
  4. response to fungicide Source: RGD
  5. response to lithium ion Source: UniProtKB
  6. synaptic transmission, glutamatergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 3
Short name:
GluR-3
Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name:
GluA3
Gene namesi
Name:Gria3
Synonyms:Glur3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi70958. Gria3.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression.

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
  2. asymmetric synapse Source: RGD
  3. cell junction Source: UniProtKB-KW
  4. dendrite Source: RGD
  5. dendritic shaft Source: RGD
  6. dendritic spine Source: UniProtKB
  7. ionotropic glutamate receptor complex Source: UniProtKB
  8. neuronal cell body Source: RGD
  9. perikaryon Source: RGD
  10. postsynaptic density Source: UniProtKB
  11. postsynaptic membrane Source: RefGenome
  12. protein complex Source: UniProtKB
  13. synaptic cleft Source: RGD
  14. terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 888866Glutamate receptor 3PRO_0000011537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi85 ↔ 334
Glycosylationi260 – 2601N-linked (GlcNAc...)1 Publication
Glycosylationi374 – 3741N-linked (GlcNAc...)1 Publication
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Lipidationi615 – 6151S-palmitoyl cysteineBy similarity
Disulfide bondi744 ↔ 799
Lipidationi841 – 8411S-palmitoyl cysteineBy similarity
Modified residuei871 – 8711PhosphotyrosineBy similarity
Modified residuei881 – 8811PhosphotyrosineBy similarity

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-841 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

PaxDbiP19492.
PRIDEiP19492.

PTM databases

PhosphoSiteiP19492.

Expressioni

Gene expression databases

GenevestigatoriP19492.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grip1P978793EBI-77764,EBI-936113
Pick1Q9EP807EBI-77764,EBI-77728

Protein-protein interaction databases

BioGridi248251. 1 interaction.
DIPiDIP-30954N.
IntActiP19492. 8 interactions.
MINTiMINT-86220.
STRINGi10116.ENSRNOP00000010367.

Structurei

Secondary structure

1
888
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 349
Helixi39 – 5315
Turni58 – 603
Beta strandi62 – 7110
Helixi77 – 8812
Turni89 – 913
Beta strandi95 – 973
Turni101 – 1033
Helixi104 – 11411
Beta strandi118 – 1203
Beta strandi130 – 1345
Helixi140 – 15011
Beta strandi154 – 1596
Helixi166 – 17712
Beta strandi181 – 1866
Helixi194 – 20411
Turni205 – 2073
Beta strandi210 – 2156
Helixi217 – 23014
Beta strandi238 – 2414
Helixi246 – 2483
Helixi252 – 2565
Beta strandi260 – 2667
Helixi272 – 28110
Turni286 – 2883
Beta strandi292 – 2954
Helixi299 – 32022
Beta strandi336 – 3383
Turni342 – 3454
Helixi346 – 3538
Beta strandi357 – 3593
Beta strandi362 – 3643
Beta strandi370 – 3723
Beta strandi377 – 3837
Beta strandi386 – 3949
Turni395 – 3973
Beta strandi398 – 4003
Beta strandi418 – 4236
Turni427 – 4293
Beta strandi430 – 4323
Helixi436 – 4383
Helixi441 – 4444
Beta strandi445 – 4473
Helixi448 – 46013
Beta strandi463 – 4686
Turni479 – 4813
Helixi486 – 4927
Beta strandi497 – 4993
Helixi507 – 5104
Beta strandi513 – 5153
Beta strandi519 – 5224
Beta strandi524 – 5296
Helixi662 – 6665
Beta strandi669 – 6768
Helixi680 – 6878
Helixi691 – 70212
Turni704 – 7063
Beta strandi708 – 7114
Helixi712 – 72110
Turni722 – 7243
Beta strandi725 – 7317
Helixi732 – 7398
Beta strandi746 – 7505
Beta strandi756 – 7583
Beta strandi761 – 7633
Helixi769 – 78113
Helixi784 – 79310
Turni794 – 7963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DLNX-ray1.91A416-530[»]
A658-799[»]
3DP4X-ray2.11A416-530[»]
A658-799[»]
3LSWX-ray1.75A417-530[»]
3LSXX-ray2.01A417-530[»]
3M3FX-ray2.50A417-530[»]
A658-799[»]
3M3KX-ray1.79A/C/E417-530[»]
A/C/E658-799[»]
3O21X-ray2.20A/B/C/D23-403[»]
3P3WX-ray4.20A/B/C/D23-403[»]
3RT6X-ray2.84B417-530[»]
B658-799[»]
3RT8X-ray2.43A417-530[»]
A658-799[»]
4F1YX-ray1.79A/C417-530[»]
A/C658-799[»]
4F22X-ray2.06A417-530[»]
A658-799[»]
4F29X-ray1.75A417-530[»]
A658-799[»]
4F2OX-ray1.91A417-530[»]
A658-799[»]
4F2QX-ray2.20A417-530[»]
A658-799[»]
4F31X-ray2.29B/D417-530[»]
B/D658-799[»]
4F39X-ray1.83A417-530[»]
A658-799[»]
4F3BX-ray1.82A417-530[»]
A658-799[»]
4F3GX-ray2.06A417-530[»]
A658-799[»]
ProteinModelPortaliP19492.
SMRiP19492. Positions 415-530, 657-800.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19492.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 546524ExtracellularBy similarityAdd
BLAST
Topological domaini568 – 59629CytoplasmicBy similarityAdd
BLAST
Topological domaini616 – 6216CytoplasmicBy similarity
Topological domaini643 – 817175ExtracellularBy similarityAdd
BLAST
Topological domaini839 – 88850CytoplasmicBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei597 – 61216Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei613 – 6153By similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei547 – 56721HelicalBy similarityAdd
BLAST
Transmembranei622 – 64221HelicalBy similarityAdd
BLAST
Transmembranei818 – 83821Helical; Name=M4By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 5043Glutamate binding
Regioni680 – 6812Glutamate binding

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

eggNOGiNOG316680.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19492.
KOiK05199.
PhylomeDBiP19492.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Flop (identifier: P19492-1) [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
MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ
60 70 80 90 100
LYNTNQNTTE KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD
110 120 130 140 150
QMSMNTLTSF CGALHTSFVT PSFPTDADVQ FVIQMRPALK GAILSLLSYY
160 170 180 190 200
KWEKFVYLYD TERGFSVLQA IMEAAVQNNW QVTARSVGNI KDVQEFRRII
210 220 230 240 250
EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM LANLGFTDIL
260 270 280 290 300
LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT
310 320 330 340 350
SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER
360 370 380 390 400
ALKMVQVQGM TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV
410 420 430 440 450
PFSDQQISND SSSSENRTIV VTTILESPYV MYKKNHEQLE GNERYEGYCV
460 470 480 490 500
DLAYEIAKHV RIKYKLSIVG DGKYGARDPE TKIWNGMVGE LVYGRADIAV
510 520 530 540 550
APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
560 570 580 590 600
MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF
610 620 630 640 650
NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL
660 670 680 690 700
TVERMVSPIE SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM
710 720 730 740 750
KSAEPSVFTK TTADGVARVR KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG
760 770 780 790 800
GNLDSKGYGV ATPKGSALGN AVNLAVLKLN EQGLLDKLKN KWWYDKGECG
810 820 830 840 850
SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF CYKSRAESKR
860 870 880
MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
Length:888
Mass (Da):100,373
Last modified:February 1, 1991 - v1
Checksum:i2981616375661703
GO
Isoform Flip (identifier: P19492-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     770-771: NA → TP
     780-780: N → S
     784-784: L → I
     801-805: SGGGD → AKDSG

Show »
Length:888
Mass (Da):100,444
Checksum:iD53A3C20BFB3F620
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti517 – 5182KP → NA(PubMed:2168579)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei770 – 7712NA → TP in isoform Flip. CuratedVSP_000119
Alternative sequencei780 – 7801N → S in isoform Flip. CuratedVSP_000120
Alternative sequencei784 – 7841L → I in isoform Flip. CuratedVSP_000121
Alternative sequencei801 – 8055SGGGD → AKDSG in isoform Flip. CuratedVSP_000122

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36420 mRNA. Translation: AAA41245.1.
X54656 mRNA. Translation: CAA38466.1.
M38062 mRNA. Translation: AAA63480.1.
M85036 mRNA. Translation: AAA41241.2.
PIRiC40170.
RefSeqiNP_001106213.1. NM_001112742.1.
NP_116785.2. NM_032990.2.
UniGeneiRn.74049.

Genome annotation databases

GeneIDi29628.
KEGGirno:29628.
UCSCiRGD:70958. rat. [P19492-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M36420 mRNA. Translation: AAA41245.1 .
X54656 mRNA. Translation: CAA38466.1 .
M38062 mRNA. Translation: AAA63480.1 .
M85036 mRNA. Translation: AAA41241.2 .
PIRi C40170.
RefSeqi NP_001106213.1. NM_001112742.1.
NP_116785.2. NM_032990.2.
UniGenei Rn.74049.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DLN X-ray 1.91 A 416-530 [» ]
A 658-799 [» ]
3DP4 X-ray 2.11 A 416-530 [» ]
A 658-799 [» ]
3LSW X-ray 1.75 A 417-530 [» ]
3LSX X-ray 2.01 A 417-530 [» ]
3M3F X-ray 2.50 A 417-530 [» ]
A 658-799 [» ]
3M3K X-ray 1.79 A/C/E 417-530 [» ]
A/C/E 658-799 [» ]
3O21 X-ray 2.20 A/B/C/D 23-403 [» ]
3P3W X-ray 4.20 A/B/C/D 23-403 [» ]
3RT6 X-ray 2.84 B 417-530 [» ]
B 658-799 [» ]
3RT8 X-ray 2.43 A 417-530 [» ]
A 658-799 [» ]
4F1Y X-ray 1.79 A/C 417-530 [» ]
A/C 658-799 [» ]
4F22 X-ray 2.06 A 417-530 [» ]
A 658-799 [» ]
4F29 X-ray 1.75 A 417-530 [» ]
A 658-799 [» ]
4F2O X-ray 1.91 A 417-530 [» ]
A 658-799 [» ]
4F2Q X-ray 2.20 A 417-530 [» ]
A 658-799 [» ]
4F31 X-ray 2.29 B/D 417-530 [» ]
B/D 658-799 [» ]
4F39 X-ray 1.83 A 417-530 [» ]
A 658-799 [» ]
4F3B X-ray 1.82 A 417-530 [» ]
A 658-799 [» ]
4F3G X-ray 2.06 A 417-530 [» ]
A 658-799 [» ]
ProteinModelPortali P19492.
SMRi P19492. Positions 415-530, 657-800.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248251. 1 interaction.
DIPi DIP-30954N.
IntActi P19492. 8 interactions.
MINTi MINT-86220.
STRINGi 10116.ENSRNOP00000010367.

Chemistry

BindingDBi P19492.
ChEMBLi CHEMBL2093871.
GuidetoPHARMACOLOGYi 446.

PTM databases

PhosphoSitei P19492.

Proteomic databases

PaxDbi P19492.
PRIDEi P19492.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29628.
KEGGi rno:29628.
UCSCi RGD:70958. rat. [P19492-1 ]

Organism-specific databases

CTDi 2892.
RGDi 70958. Gria3.

Phylogenomic databases

eggNOGi NOG316680.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
InParanoidi P19492.
KOi K05199.
PhylomeDBi P19492.

Miscellaneous databases

EvolutionaryTracei P19492.
NextBioi 609848.

Gene expression databases

Genevestigatori P19492.

Family and domain databases

InterProi IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view ]
PRINTSi PR00177. NMDARECEPTOR.
SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
    Strain: Sprague-Dawley.
    Tissue: Forebrain.
  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] (VARIANT FLIP).
    Tissue: Brain cortex and Hippocampus.
  4. "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).
    Tissue: Brain.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. "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: SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Structure of the S1S2 glutamate binding domain of GLuR3."
    Ahmed A.H., Wang Q., Sondermann H., Oswald R.E.
    Proteins 75:628-637(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 407-800 IN COMPLEX WITH GLUTAMATE, DISULFIDE BOND.
  11. "Molecular mechanism of flop selectivity and subsite recognition for an AMPA receptor allosteric modulator: structures of GluA2 and GluA3 in complexes with PEPA."
    Ahmed A.H., Ptak C.P., Oswald R.E.
    Biochemistry 49:2843-2850(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 417-799 IN COMPLEX WITH GLUTAMATE, DISULFIDE BOND.
  12. "Dynamics and allosteric potential of the AMPA receptor N-terminal domain."
    Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I., Greger I.H.
    EMBO J. 30:972-982(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-403, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-260 AND ASN-374.

Entry informationi

Entry nameiGRIA3_RAT
AccessioniPrimary (citable) accession number: P19492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3