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Q9Z2W9

- GRIA3_MOUSE

UniProt

Q9Z2W9 - GRIA3_MOUSE

Protein

Glutamate receptor 3

Gene

Gria3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 – 4741Glutamate1 Publication
    Binding sitei509 – 5091Glutamate1 Publication
    Binding sitei731 – 7311Glutamate1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. ionotropic glutamate receptor signaling pathway Source: RefGenome
    2. ion transmembrane transport Source: RefGenome
    3. 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, Kiaa4184
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:95810. Gria3.

    Subcellular locationi

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

    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: RefGenome
    4. membrane Source: MGI
    5. postsynaptic membrane Source: MGI

    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_0000042230Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi85 ↔ 334By similarity
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
    Lipidationi615 – 6151S-palmitoyl cysteineBy similarity
    Disulfide bondi744 ↔ 7991 Publication
    Lipidationi841 – 8411S-palmitoyl cysteine1 Publication
    Modified residuei871 – 8711Phosphotyrosine1 Publication
    Modified residuei881 – 8811Phosphotyrosine1 Publication

    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

    MaxQBiQ9Z2W9.
    PaxDbiQ9Z2W9.
    PRIDEiQ9Z2W9.

    PTM databases

    PhosphoSiteiQ9Z2W9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z2W9.
    BgeeiQ9Z2W9.
    CleanExiMM_GRIA3.
    GenevestigatoriQ9Z2W9.

    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 By similarity. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi207340. 2 interactions.
    IntActiQ9Z2W9. 4 interactions.
    MINTiMINT-4131411.

    Structurei

    Secondary structure

    1
    888
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi662 – 6665
    Beta strandi669 – 6768
    Helixi680 – 6878
    Helixi691 – 70212
    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
    3LSWX-ray1.75A658-799[»]
    3LSXX-ray2.01A658-799[»]
    ProteinModelPortaliQ9Z2W9.
    SMRiQ9Z2W9. Positions 26-843.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z2W9.

    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.
    GeneTreeiENSGT00740000115362.
    HOGENOMiHOG000234372.
    HOVERGENiHBG051839.
    KOiK05199.
    OrthoDBiEOG7C2R0J.
    TreeFamiTF315232.

    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 Flip (identifier: Q9Z2W9-1) [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 GAILSLLGYY 150
    KWEKFVYLYD TERGFSILQA IMEAAVQNNW QVTARSVGNI KDIQEFRRII 200
    EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM LANLGFTDIV 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 ATPKGSALRT PVNLAVLKLS EQGILDKLKN KWWYDKGECG 800
    AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF CYKSRAESKR 850
    MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI 888
    Length:888
    Mass (Da):100,527
    Last modified:July 27, 2011 - v2
    Checksum:i9F68C5D80E81DC02
    GO
    Isoform Flop (identifier: Q9Z2W9-2)

    Sequence is not available
    Length:
    Mass (Da):

    Sequence cautioni

    The sequence BAD90527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3001T → I in BAD90527. 1 PublicationCurated
    Sequence conflicti769 – 7691R → G in BAA37124. 1 PublicationCurated
    Sequence conflicti769 – 7691R → G in BAE06153. 1 PublicationCurated
    Sequence conflicti769 – 7691R → G in AAL90768. (PubMed:11471062)Curated
    Sequence conflicti769 – 7691R → G in AAL90769. (PubMed:11471062)Curated
    Sequence conflicti769 – 7691R → G in BAD90527. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022342 mRNA. Translation: BAA37124.1.
    AB079072 mRNA. Translation: BAE06153.1.
    AF483494 mRNA. Translation: AAL90768.1.
    AF483495 mRNA. Translation: AAL90769.1.
    AK220530 mRNA. Translation: BAD90527.1. Different initiation.
    CH466570 Genomic DNA. Translation: EDL29035.1.
    AL672290, AL672232 Genomic DNA. Translation: CAQ11290.1.
    AL672232, AL672290 Genomic DNA. Translation: CAQ12028.1.
    BC129855 mRNA. Translation: AAI29856.1.
    CCDSiCCDS30097.1. [Q9Z2W9-1]
    RefSeqiNP_001268858.1. NM_001281929.1.
    NP_001277380.1. NM_001290451.1.
    NP_058582.3. NM_016886.4.
    XP_006541583.1. XM_006541520.1. [Q9Z2W9-1]
    UniGeneiMm.327681.

    Genome annotation databases

    EnsembliENSMUST00000076349; ENSMUSP00000075687; ENSMUSG00000001986. [Q9Z2W9-1]
    GeneIDi53623.
    KEGGimmu:53623.
    UCSCiuc009tal.2. mouse. [Q9Z2W9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022342 mRNA. Translation: BAA37124.1 .
    AB079072 mRNA. Translation: BAE06153.1 .
    AF483494 mRNA. Translation: AAL90768.1 .
    AF483495 mRNA. Translation: AAL90769.1 .
    AK220530 mRNA. Translation: BAD90527.1 . Different initiation.
    CH466570 Genomic DNA. Translation: EDL29035.1 .
    AL672290 , AL672232 Genomic DNA. Translation: CAQ11290.1 .
    AL672232 , AL672290 Genomic DNA. Translation: CAQ12028.1 .
    BC129855 mRNA. Translation: AAI29856.1 .
    CCDSi CCDS30097.1. [Q9Z2W9-1 ]
    RefSeqi NP_001268858.1. NM_001281929.1.
    NP_001277380.1. NM_001290451.1.
    NP_058582.3. NM_016886.4.
    XP_006541583.1. XM_006541520.1. [Q9Z2W9-1 ]
    UniGenei Mm.327681.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LSW X-ray 1.75 A 658-799 [» ]
    3LSX X-ray 2.01 A 658-799 [» ]
    ProteinModelPortali Q9Z2W9.
    SMRi Q9Z2W9. Positions 26-843.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207340. 2 interactions.
    IntActi Q9Z2W9. 4 interactions.
    MINTi MINT-4131411.

    Chemistry

    BindingDBi Q9Z2W9.
    ChEMBLi CHEMBL2096617.
    GuidetoPHARMACOLOGYi 446.

    PTM databases

    PhosphoSitei Q9Z2W9.

    Proteomic databases

    MaxQBi Q9Z2W9.
    PaxDbi Q9Z2W9.
    PRIDEi Q9Z2W9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000076349 ; ENSMUSP00000075687 ; ENSMUSG00000001986 . [Q9Z2W9-1 ]
    GeneIDi 53623.
    KEGGi mmu:53623.
    UCSCi uc009tal.2. mouse. [Q9Z2W9-1 ]

    Organism-specific databases

    CTDi 2892.
    MGIi MGI:95810. Gria3.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG316680.
    GeneTreei ENSGT00740000115362.
    HOGENOMi HOG000234372.
    HOVERGENi HBG051839.
    KOi K05199.
    OrthoDBi EOG7C2R0J.
    TreeFami TF315232.

    Miscellaneous databases

    EvolutionaryTracei Q9Z2W9.
    NextBioi 310361.
    PROi Q9Z2W9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2W9.
    Bgeei Q9Z2W9.
    CleanExi MM_GRIA3.
    Genevestigatori Q9Z2W9.

    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. "Mouse glutamate receptor channel alpha3 subunit."
      Sakimura K., Yamazaki M.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    2. "Expression of AMPA-selective glutamate receptors in mouse spinal cord."
      Doi Y., Nishizawa M., Minami T., Ito S.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ddY.
      Tissue: Spinal cord.
    3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ILS and ISS.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites."
      Hayashi T., Rumbaugh G., Huganir R.L.
      Neuron 47:709-723(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-841.
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-871 AND TYR-881, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "Piracetam defines a new binding site for allosteric modulators of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors."
      Ahmed A.H., Oswald R.E.
      J. Med. Chem. 53:2197-2203(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 658-799 IN COMPLEX WITH GLUTAMATE, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiGRIA3_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2W9
    Secondary accession number(s): A2VDF4, Q5DTJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3