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P19493

- GRIA4_RAT

UniProt

P19493 - GRIA4_RAT

Protein

Glutamate receptor 4

Gene

Gria4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (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 sitei472 – 4721Glutamate3 Publications
    Binding sitei507 – 5071Glutamate3 Publications
    Binding sitei727 – 7271GlutamateBy similarity

    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: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. ionotropic glutamate receptor signaling pathway Source: GOC
    2. ion transmembrane transport Source: GOC
    3. positive regulation of synaptic transmission, glutamatergic Source: UniProtKB
    4. regulation of synapse structure and activity Source: UniProtKB
    5. regulation of synaptic transmission Source: UniProtKB
    6. response to fungicide Source: RGD
    7. synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Protein family/group databases

    TCDBi1.A.10.1.2. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor 4
    Short name:
    GluR-4
    Short name:
    GluR4
    Alternative name(s):
    AMPA-selective glutamate receptor 4
    GluR-D
    Glutamate receptor ionotropic, AMPA 4
    Short name:
    GluA4
    Gene namesi
    Name:Gria4
    Synonyms:Glur4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61863. Gria4.

    Subcellular locationi

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

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. dendrite Source: UniProtKB
    4. ionotropic glutamate receptor complex Source: UniProtKB
    5. kainate selective glutamate receptor complex Source: UniProtKB
    6. neuronal cell body Source: UniProtKB
    7. postsynaptic density Source: UniProtKB
    8. postsynaptic membrane Source: RefGenome
    9. synapse Source: UniProtKB
    10. terminal bouton Source: RGD

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi407 – 4071N → Q: No effect on surface expression and channel activity; when associated with Q-414. 1 Publication
    Mutagenesisi414 – 4141N → Q: No effect on surface expression and channel activity; when associated with Q-407. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 902882Glutamate receptor 4PRO_0000011540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi84 ↔ 331By similarity
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication
    Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
    Lipidationi611 – 6111S-palmitoyl cysteineBy similarity
    Disulfide bondi740 ↔ 7951 Publication
    Lipidationi837 – 8371S-palmitoyl cysteineBy similarity
    Modified residuei862 – 8621Phosphoserine; by PKC/PRKCG1 Publication

    Post-translational modificationi

    Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.By similarity
    Phosphorylated at Ser-862 by PRKCG; phosphorylation increases plasma membrane-associated GRI4 expression.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP19493.
    PRIDEiP19493.

    PTM databases

    PhosphoSiteiP19493.

    Expressioni

    Tissue specificityi

    Detected in cerebellum (at protein level).

    Gene expression databases

    GenevestigatoriP19493.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with EPB41L1 via its C-terminus. Isoform 3 interacts with PRKCABP. Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 and PRKCG.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Grip1P978793EBI-7761834,EBI-936113
    Mapk8P491852EBI-7761834,EBI-7456505

    Protein-protein interaction databases

    DIPiDIP-41142N.
    IntActiP19493. 5 interactions.
    MINTiMINT-86166.

    Structurei

    Secondary structure

    1
    902
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 339
    Helixi38 – 5215
    Turni57 – 593
    Beta strandi61 – 7010
    Helixi76 – 8813
    Beta strandi92 – 965
    Turni100 – 1023
    Helixi103 – 11210
    Beta strandi116 – 1194
    Beta strandi129 – 1335
    Helixi139 – 14810
    Beta strandi153 – 1586
    Helixi165 – 17511
    Turni176 – 1783
    Beta strandi180 – 1856
    Helixi191 – 20414
    Beta strandi208 – 2125
    Helixi215 – 22814
    Beta strandi236 – 2394
    Beta strandi241 – 2433
    Helixi244 – 2463
    Helixi250 – 2556
    Beta strandi258 – 2636
    Helixi270 – 27910
    Turni284 – 2863
    Turni288 – 2914
    Helixi296 – 31722
    Helixi342 – 3509
    Beta strandi353 – 3564
    Beta strandi359 – 3635
    Beta strandi373 – 3808
    Beta strandi383 – 3919
    Turni392 – 3943
    Beta strandi395 – 3984
    Beta strandi416 – 4216
    Turni425 – 4273
    Beta strandi428 – 4303
    Helixi434 – 4363
    Helixi439 – 4424
    Beta strandi443 – 4453
    Helixi446 – 45813
    Beta strandi461 – 4666
    Turni477 – 4793
    Helixi484 – 4907
    Beta strandi495 – 4973
    Helixi505 – 5084
    Beta strandi511 – 5133
    Beta strandi517 – 5204
    Beta strandi522 – 5276
    Helixi658 – 6625
    Beta strandi665 – 6706
    Beta strandi672 – 6754
    Helixi676 – 6838
    Helixi687 – 69812
    Beta strandi705 – 7073
    Helixi708 – 71710
    Turni718 – 7203
    Beta strandi721 – 7277
    Helixi728 – 7358
    Beta strandi742 – 7465
    Beta strandi752 – 7543
    Beta strandi757 – 7593
    Helixi765 – 77713
    Helixi780 – 78910
    Turni790 – 7923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EN3X-ray2.43A416-528[»]
    A654-795[»]
    3EPEX-ray1.85A/B416-528[»]
    A/B654-795[»]
    3FASX-ray1.40A/B415-528[»]
    A/B654-796[»]
    3FATX-ray1.90A/B/C415-528[»]
    A/B/C654-796[»]
    3KEIX-ray1.90A/B416-528[»]
    A/B654-795[»]
    3KFMX-ray2.20A416-528[»]
    A654-795[»]
    4GPAX-ray2.25A22-401[»]
    ProteinModelPortaliP19493.
    SMRiP19493. Positions 413-528, 653-796.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19493.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 544523ExtracellularBy similarityAdd
    BLAST
    Topological domaini566 – 59227CytoplasmicBy similarityAdd
    BLAST
    Topological domaini612 – 6176CytoplasmicBy similarity
    Topological domaini639 – 813175ExtracellularBy similarityAdd
    BLAST
    Topological domaini835 – 90268CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei593 – 60816Helical; Pore-formingBy similarityAdd
    BLAST
    Intramembranei609 – 6113By similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei545 – 56521HelicalBy similarityAdd
    BLAST
    Transmembranei618 – 63821HelicalBy similarityAdd
    BLAST
    Transmembranei814 – 83421Helical; Name=M4By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni500 – 5023Glutamate binding
    Regioni676 – 6772Glutamate 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.
    InParanoidiP19493.
    KOiK05200.
    PhylomeDBiP19493.

    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 (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. Align

    Isoform 1 (identifier: P19493-1) [UniParc]FASTAAdd to Basket

    Also known as: Flop

    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

    MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL    50
    HNTSPNASEA PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK 100
    RSVHTLTSFC SALHISLITP SFPTEGESQF VLQLRPSLRG ALLSLLDHYE 150
    WNCFVFLYDT DRGYSILQAI MEKAGQNGWH VSAICVENFN DVSYRQLLEE 200
    LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA NLGFKDISLE 250
    RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL 300
    TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK 350
    QVRIQGLTGN VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ 400
    DMPTLGNDTA AIENRTVVVT TIMESPYVMY KKNHEMFEGN DKYEGYCVDL 450
    ASEIAKHIGI KYKIAIVPDG KYGARDADTK IWNGMVGELV YGKAEIAIAP 500
    LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL DPLAYEIWMC 550
    IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW 600
    FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 650
    MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE 700
    PSVFTRTTAE GVARVRKSKG KFAFLLESTM NEYTEQRKPC DTMKVGGNLD 750
    SKGYGVATPK GSSLGNAVNL AVLKLNEQGL LDKLKNKWWY DKGECGSGGG 800
    DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS RAEAKRMKLT 850
    FSEATRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD 900
    LP 902
    Length:902
    Mass (Da):100,758
    Last modified:February 1, 1991 - v1
    Checksum:i873D1B4C710C4459
    GO
    Isoform 2 (identifier: P19493-2) [UniParc]FASTAAdd to Basket

    Also known as: Flip

    The sequence of this isoform differs from the canonical sequence as follows:
         765-767: GNA → RTP
         776-780: NEQGL → SEAGV
         797-801: SGGGD → PKDSG

    Show »
    Length:902
    Mass (Da):100,883
    Checksum:iEB2AEF26FD237199
    GO
    Isoform 3 (identifier: P19493-3) [UniParc]FASTAAdd to Basket

    Also known as: 4C flop

    The sequence of this isoform differs from the canonical sequence as follows:
         849-902: LTFSEATRNK...GLAVIASDLP → VAKSAQTFNP...NVYGTESIKI

    Show »
    Length:884
    Mass (Da):99,184
    Checksum:i00B47FD9B55E38C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1122SA → RR in AAA41242. (PubMed:1977421)Curated
    Sequence conflicti454 – 4541I → S in AAA41242. (PubMed:1977421)Curated
    Sequence conflicti734 – 7341T → I in AAA41242. (PubMed:1977421)Curated
    Sequence conflicti855 – 8551T → I in AAA41242. (PubMed:1977421)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei765 – 7673GNA → RTP in isoform 2. 2 PublicationsVSP_000123
    Alternative sequencei776 – 7805NEQGL → SEAGV in isoform 2. 2 PublicationsVSP_000124
    Alternative sequencei797 – 8015SGGGD → PKDSG in isoform 2. 2 PublicationsVSP_000125
    Alternative sequencei849 – 90254LTFSE…ASDLP → VAKSAQTFNPTSSQNTHNLA TYREGYNVYGTESIKI in isoform 3. 1 PublicationVSP_000126Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36421 mRNA. Translation: AAA41246.1.
    M85037 mRNA. Translation: AAA41242.1.
    M38063 mRNA. Translation: AAA63481.1.
    S94371 mRNA. Translation: AAB21763.1.
    PIRiA44839.
    D40170.
    RefSeqiNP_001106655.1. NM_001113184.1.
    NP_058959.2. NM_017263.2.
    UniGeneiRn.10938.

    Genome annotation databases

    GeneIDi29629.
    KEGGirno:29629.
    UCSCiRGD:61863. rat. [P19493-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36421 mRNA. Translation: AAA41246.1 .
    M85037 mRNA. Translation: AAA41242.1 .
    M38063 mRNA. Translation: AAA63481.1 .
    S94371 mRNA. Translation: AAB21763.1 .
    PIRi A44839.
    D40170.
    RefSeqi NP_001106655.1. NM_001113184.1.
    NP_058959.2. NM_017263.2.
    UniGenei Rn.10938.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EN3 X-ray 2.43 A 416-528 [» ]
    A 654-795 [» ]
    3EPE X-ray 1.85 A/B 416-528 [» ]
    A/B 654-795 [» ]
    3FAS X-ray 1.40 A/B 415-528 [» ]
    A/B 654-796 [» ]
    3FAT X-ray 1.90 A/B/C 415-528 [» ]
    A/B/C 654-796 [» ]
    3KEI X-ray 1.90 A/B 416-528 [» ]
    A/B 654-795 [» ]
    3KFM X-ray 2.20 A 416-528 [» ]
    A 654-795 [» ]
    4GPA X-ray 2.25 A 22-401 [» ]
    ProteinModelPortali P19493.
    SMRi P19493. Positions 413-528, 653-796.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-41142N.
    IntActi P19493. 5 interactions.
    MINTi MINT-86166.

    Chemistry

    BindingDBi P19493.
    ChEMBLi CHEMBL2096669.
    GuidetoPHARMACOLOGYi 447.

    Protein family/group databases

    TCDBi 1.A.10.1.2. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei P19493.

    Proteomic databases

    PaxDbi P19493.
    PRIDEi P19493.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29629.
    KEGGi rno:29629.
    UCSCi RGD:61863. rat. [P19493-1 ]

    Organism-specific databases

    CTDi 2893.
    RGDi 61863. Gria4.

    Phylogenomic databases

    eggNOGi NOG316680.
    HOGENOMi HOG000234372.
    HOVERGENi HBG051839.
    InParanoidi P19493.
    KOi K05200.
    PhylomeDBi P19493.

    Miscellaneous databases

    EvolutionaryTracei P19493.
    NextBioi 609852.

    Gene expression databases

    Genevestigatori P19493.

    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] (ISOFORM 1).
      Tissue: Brain.
    2. "Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development."
      Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A., Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.
      Neuron 5:583-595(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "Molecular cloning and development analysis of a new glutamate receptor subunit isoform in cerebellum."
      Gallo V., Upson L.M., Hayes W.P., Vyklicky L. Jr., Winters C.A., Buonanno A.
      J. Neurosci. 12:1010-1023(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    5. "Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain."
      Pasternack A., Coleman S.K., Fethiere J., Madden D.R., LeCaer J.P., Rossier J., Pasternack M., Keinaenen K.
      J. Neurochem. 84:1184-1192(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-407 AND ASN-414, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF ASN-407 AND ASN-414.
    6. "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 (ISOFORM 3).
    7. "Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation."
      Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.
      J. Biol. Chem. 278:6307-6313(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-862, INTERACTION WITH PRKCG, SUBCELLULAR LOCATION.
    8. "Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein."
      Coleman S.K., Cai C., Mottershead D.G., Haapalahti J.-P., Keinaenen K.
      J. Neurosci. 23:798-806(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPB41L1.
    9. "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.
    10. "Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
      Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
      Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNG5.
    11. "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.
    12. "Correlating AMPA receptor activation and cleft closure across subunits: crystal structures of the GluR4 ligand-binding domain in complex with full and partial agonists."
      Gill A., Birdsey-Benson A., Jones B.L., Henderson L.P., Madden D.R.
      Biochemistry 47:13831-13841(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE AND DIHYDROKAINIC ACID, FUNCTION, SUBUNIT.
    13. "Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4."
      Kasper C., Frydenvang K., Naur P., Gajhede M., Pickering D.S., Kastrup J.S.
      FEBS Lett. 582:4089-4094(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 415-796 IN COMPLEX WITH GLUTAMATE, AMPA BINDING, DISULFIDE BOND.
    14. "Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors."
      Birdsey-Benson A., Gill A., Henderson L.P., Madden D.R.
      J. Neurosci. 30:1463-1470(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE AND DIHYDROKAINIC ACID, FUNCTION.

    Entry informationi

    Entry nameiGRIA4_RAT
    AccessioniPrimary (citable) accession number: P19493
    Secondary accession number(s): Q64241
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 141 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, Direct protein sequencing, 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