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P19492

- GRIA3_RAT

UniProt

P19492 - GRIA3_RAT

Protein

Glutamate receptor 3

Gene

Gria3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    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
    5. protein 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

    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

    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.
    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

    MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ    50
    LYNTNQNTTE KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD 100
    QMSMNTLTSF CGALHTSFVT PSFPTDADVQ FVIQMRPALK GAILSLLSYY 150
    KWEKFVYLYD TERGFSVLQA IMEAAVQNNW QVTARSVGNI KDVQEFRRII 200
    EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM LANLGFTDIL 250
    LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT 300
    SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER 350
    ALKMVQVQGM TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV 400
    PFSDQQISND SSSSENRTIV VTTILESPYV MYKKNHEQLE GNERYEGYCV 450
    DLAYEIAKHV RIKYKLSIVG DGKYGARDPE TKIWNGMVGE LVYGRADIAV 500
    APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 550
    MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF 600
    NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL 650
    TVERMVSPIE SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM 700
    KSAEPSVFTK TTADGVARVR KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG 750
    GNLDSKGYGV ATPKGSALGN AVNLAVLKLN EQGLLDKLKN KWWYDKGECG 800
    SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF CYKSRAESKR 850
    MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI 888
    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.
    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 1, 2014
    This is version 146 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