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P22756

- GRIK1_RAT

UniProt

P22756 - GRIK1_RAT

Protein

Glutamate receptor ionotropic, kainate 1

Gene

Grik1

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 3 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Ionotropic glutamate receptor. 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. May be involved in the transmission of light information from the retina to the hypothalamus.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei538 – 5381Glutamate2 Publications
    Binding sitei753 – 7531Glutamate2 Publications

    GO - Molecular functioni

    1. drug binding Source: RGD
    2. extracellular-glutamate-gated ion channel activity Source: RGD
    3. glutamate binding Source: RGD
    4. ionotropic glutamate receptor activity Source: RGD
    5. kainate selective glutamate receptor activity Source: RGD
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: RGD
    8. voltage-gated cation channel activity Source: RGD

    GO - Biological processi

    1. ionotropic glutamate receptor signaling pathway Source: RGD
    2. ion transmembrane transport Source: GOC
    3. negative regulation of synaptic transmission, GABAergic Source: RGD
    4. negative regulation of synaptic transmission, glutamatergic Source: RGD
    5. nervous system development Source: RGD
    6. positive regulation of synaptic transmission, GABAergic Source: RGD
    7. regulation of ion transmembrane transport Source: GOC
    8. regulation of short-term neuronal synaptic plasticity Source: RGD
    9. regulation of synaptic plasticity Source: UniProtKB
    10. synaptic transmission Source: UniProtKB

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Protein family/group databases

    TCDBi1.A.10.1.5. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, kainate 1
    Short name:
    GluK1
    Alternative name(s):
    Glutamate receptor 5
    Short name:
    GluR-5
    Short name:
    GluR5
    Gene namesi
    Name:Grik1
    Synonyms:Glur5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 11

    Organism-specific databases

    RGDi2732. Grik1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dendrite Source: RGD
    3. ionotropic glutamate receptor complex Source: RGD
    4. kainate selective glutamate receptor complex Source: RefGenome
    5. neuronal cell body Source: RGD
    6. postsynaptic membrane Source: RefGenome
    7. presynaptic membrane Source: RefGenome
    8. receptor complex Source: UniProtKB
    9. 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 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 949919Glutamate receptor ionotropic, kainate 1PRO_0000011543Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
    Modified residuei725 – 7251Phosphoserine; by PKCSequence Analysis
    Modified residuei761 – 7611Phosphothreonine; by PKCSequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP22756.
    PRIDEiP22756.

    PTM databases

    PhosphoSiteiP22756.

    Expressioni

    Tissue specificityi

    Expressed in subsets of neurons throughout the developing and adult central and peripheral nervous systems. In the CNS principally in the medial amygdaloid nuclei, medial habenulae, pyriform and cingulate cortices, and Purkinje cell layer. Also highly expressed in embryonic and adult dorsal root ganglia.

    Gene expression databases

    GenevestigatoriP22756.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers Probable. The unedited version (Q) assembles into a functional kainate-gated homomeric channel, whereas the edited version (R) is unable to produce channel activity when expressed alone. Both edited and unedited versions can form functional channels with GRIK4 and GRIK5. Interacts with KLHL17.4 PublicationsCurated

    Protein-protein interaction databases

    BioGridi248193. 4 interactions.
    DIPiDIP-29257N.
    STRINGi10116.ENSRNOP00000045594.

    Structurei

    Secondary structure

    1
    949
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi449 – 4535
    Turni457 – 4593
    Beta strandi460 – 4623
    Helixi471 – 4744
    Beta strandi475 – 4773
    Helixi478 – 49013
    Beta strandi494 – 4985
    Helixi515 – 5217
    Beta strandi526 – 5283
    Helixi536 – 5394
    Beta strandi542 – 5443
    Beta strandi548 – 5514
    Beta strandi553 – 5597
    Helixi671 – 6755
    Beta strandi678 – 6836
    Helixi689 – 6968
    Helixi700 – 70910
    Beta strandi716 – 7205
    Helixi721 – 73010
    Beta strandi731 – 7388
    Helixi739 – 74810
    Beta strandi752 – 7565
    Beta strandi762 – 7643
    Beta strandi767 – 7693
    Helixi774 – 78714
    Helixi790 – 7989
    Helixi806 – 8149

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TXFX-ray2.10A446-559[»]
    A682-821[»]
    1VSOX-ray1.85A445-559[»]
    A682-820[»]
    1YCJX-ray1.95A/B445-559[»]
    2F34X-ray1.74A/B446-559[»]
    A/B682-821[»]
    2F35X-ray1.87A/B446-559[»]
    A/B682-821[»]
    2F36X-ray2.11A/B/C/D446-559[»]
    A/B/C/D682-821[»]
    2OJTX-ray1.95A/B446-559[»]
    A/B682-821[»]
    2PBWX-ray2.50A/B445-559[»]
    A/B682-820[»]
    2QS1X-ray1.80A/B446-559[»]
    A/B682-821[»]
    2QS2X-ray1.80A/B446-559[»]
    A/B682-821[»]
    2QS3X-ray1.76A/B446-559[»]
    A/B682-821[»]
    2QS4X-ray1.58A/B/C/D446-559[»]
    A/B/C/D682-821[»]
    2WKYX-ray2.20A/B445-559[»]
    A/B667-806[»]
    A/B682-821[»]
    3C31X-ray1.49A/B446-559[»]
    A/B682-821[»]
    3C32X-ray1.72A/B446-559[»]
    A/B682-821[»]
    3C33X-ray1.72A/B446-559[»]
    A/B682-821[»]
    3C34X-ray1.82A/B446-559[»]
    A/B682-821[»]
    3C35X-ray1.97A/B446-559[»]
    A/B682-821[»]
    3C36X-ray1.68A/B446-559[»]
    A/B682-821[»]
    3GBAX-ray1.35A/B/C/D445-559[»]
    A/B/C/D682-820[»]
    3GBBX-ray2.10A/B445-559[»]
    A/B682-820[»]
    3S2VX-ray2.50A/B445-559[»]
    A/B682-820[»]
    4DLDX-ray2.00A/B445-559[»]
    A/B667-820[»]
    4E0XX-ray2.00A/B682-820[»]
    ProteinModelPortaliP22756.
    SMRiP22756. Positions 445-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22756.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 576546ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini598 – 65356CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini675 – 834160ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini856 – 94994CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei577 – 59721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei654 – 67421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei835 – 85521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni531 – 5333Glutamate binding
    Regioni704 – 7052Glutamate binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    GeneTreeiENSGT00740000114953.
    HOGENOMiHOG000234371.
    HOVERGENiHBG051839.
    InParanoidiP22756.
    KOiK05201.
    PhylomeDBiP22756.

    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Glur5-2C (identifier: P22756-1) [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

    MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP    50
    VNVEELAFKF AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL 100
    ALGVAALFGP SHSSSVSAVQ SICNALEVPH IQTRWKHPSV DSRDLFYINL 150
    YPDYAAISRA VLDLVLYYNW KTVTVVYEDS TGLIRLQELI KAPSRYNIKI 200
    KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL KQILFMGMMT 250
    EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME 300
    RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR 350
    HKPCALGPRF MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT 400
    EKASGEVSKH LYKVWKKIGI WNSNSGLNMT DGNRDRSNNI TDSLANRTLI 450
    VTTILEEPYV MYRKSDKPLY GNDRFEAYCL DLLKELSNIL GFLYDVKLVP 500
    DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK VIDFSKPFMT 550
    LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT 600
    PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI 650
    VGGIWWFFTL IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV 700
    RDGSTMTFFK KSKISTYEKM WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL 750
    LMESTSIEYV TQRNCNLTQI GGLIDSKGYG VGTPIGSPYR DKITIAILQL 800
    QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI VLAAGLVLSV 850
    FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL 900
    SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA 949
    Length:949
    Mass (Da):107,840
    Last modified:November 1, 1995 - v3
    Checksum:i020660BDD00054E0
    GO
    Isoform Glur5-2 (identifier: P22756-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         402-416: Missing.
         870-898: Missing.

    Show »
    Length:905
    Mass (Da):102,646
    Checksum:iB674CECB3FB60F47
    GO
    Isoform Glur5-2A (identifier: P22756-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         870-871: KG → HY
         872-949: Missing.

    Show »
    Length:871
    Mass (Da):98,853
    Checksum:iCC3EEB35068FDB54
    GO
    Isoform Glur5-2B (identifier: P22756-4) [UniParc]FASTAAdd to Basket

    Also known as: Glur5-1

    The sequence of this isoform differs from the canonical sequence as follows:
         870-898: Missing.

    Show »
    Length:920
    Mass (Da):104,388
    Checksum:i4609F0CDF337B3D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti282 – 2821K → L in AAA02874. (PubMed:1977421)Curated
    Sequence conflicti354 – 3552CA → WR in AAA02874. (PubMed:1977421)Curated
    Sequence conflicti477 – 4771A → G in AAA02874. (PubMed:1977421)Curated

    RNA editingi

    Partially edited.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti636 – 6361Q → R in RNA edited version.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei402 – 41615Missing in isoform Glur5-2. CuratedVSP_000129Add
    BLAST
    Alternative sequencei870 – 89829Missing in isoform Glur5-2B and isoform Glur5-2. CuratedVSP_000130Add
    BLAST
    Alternative sequencei870 – 8712KG → HY in isoform Glur5-2A. CuratedVSP_000131
    Alternative sequencei872 – 94978Missing in isoform Glur5-2A. CuratedVSP_000132Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83560 mRNA. Translation: AAA02873.1.
    M83561 mRNA. Translation: AAA02874.1.
    Z11712 mRNA. Translation: CAA77775.1.
    Z11713 mRNA. Translation: CAA77776.1.
    Z11714 mRNA. Translation: CAA77777.1.
    PIRiS19808.
    RefSeqiNP_001104584.1. NM_001111114.1.
    NP_001104587.1. NM_001111117.1.
    NP_058937.1. NM_017241.2.
    UniGeneiRn.10449.

    Genome annotation databases

    EnsembliENSRNOT00000042581; ENSRNOP00000050263; ENSRNOG00000001575.
    ENSRNOT00000051060; ENSRNOP00000046164; ENSRNOG00000001575.
    GeneIDi29559.
    KEGGirno:29559.
    UCSCiRGD:2732. rat. [P22756-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83560 mRNA. Translation: AAA02873.1 .
    M83561 mRNA. Translation: AAA02874.1 .
    Z11712 mRNA. Translation: CAA77775.1 .
    Z11713 mRNA. Translation: CAA77776.1 .
    Z11714 mRNA. Translation: CAA77777.1 .
    PIRi S19808.
    RefSeqi NP_001104584.1. NM_001111114.1.
    NP_001104587.1. NM_001111117.1.
    NP_058937.1. NM_017241.2.
    UniGenei Rn.10449.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TXF X-ray 2.10 A 446-559 [» ]
    A 682-821 [» ]
    1VSO X-ray 1.85 A 445-559 [» ]
    A 682-820 [» ]
    1YCJ X-ray 1.95 A/B 445-559 [» ]
    2F34 X-ray 1.74 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2F35 X-ray 1.87 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2F36 X-ray 2.11 A/B/C/D 446-559 [» ]
    A/B/C/D 682-821 [» ]
    2OJT X-ray 1.95 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2PBW X-ray 2.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    2QS1 X-ray 1.80 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2QS2 X-ray 1.80 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2QS3 X-ray 1.76 A/B 446-559 [» ]
    A/B 682-821 [» ]
    2QS4 X-ray 1.58 A/B/C/D 446-559 [» ]
    A/B/C/D 682-821 [» ]
    2WKY X-ray 2.20 A/B 445-559 [» ]
    A/B 667-806 [» ]
    A/B 682-821 [» ]
    3C31 X-ray 1.49 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3C32 X-ray 1.72 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3C33 X-ray 1.72 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3C34 X-ray 1.82 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3C35 X-ray 1.97 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3C36 X-ray 1.68 A/B 446-559 [» ]
    A/B 682-821 [» ]
    3GBA X-ray 1.35 A/B/C/D 445-559 [» ]
    A/B/C/D 682-820 [» ]
    3GBB X-ray 2.10 A/B 445-559 [» ]
    A/B 682-820 [» ]
    3S2V X-ray 2.50 A/B 445-559 [» ]
    A/B 682-820 [» ]
    4DLD X-ray 2.00 A/B 445-559 [» ]
    A/B 667-820 [» ]
    4E0X X-ray 2.00 A/B 682-820 [» ]
    ProteinModelPortali P22756.
    SMRi P22756. Positions 445-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248193. 4 interactions.
    DIPi DIP-29257N.
    STRINGi 10116.ENSRNOP00000045594.

    Chemistry

    BindingDBi P22756.
    ChEMBLi CHEMBL2094119.
    GuidetoPHARMACOLOGYi 450.

    Protein family/group databases

    TCDBi 1.A.10.1.5. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei P22756.

    Proteomic databases

    PaxDbi P22756.
    PRIDEi P22756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000042581 ; ENSRNOP00000050263 ; ENSRNOG00000001575 .
    ENSRNOT00000051060 ; ENSRNOP00000046164 ; ENSRNOG00000001575 .
    GeneIDi 29559.
    KEGGi rno:29559.
    UCSCi RGD:2732. rat. [P22756-1 ]

    Organism-specific databases

    CTDi 2897.
    RGDi 2732. Grik1.

    Phylogenomic databases

    eggNOGi NOG316680.
    GeneTreei ENSGT00740000114953.
    HOGENOMi HOG000234371.
    HOVERGENi HBG051839.
    InParanoidi P22756.
    KOi K05201.
    PhylomeDBi P22756.

    Miscellaneous databases

    EvolutionaryTracei P22756.
    NextBioi 609606.
    PROi P22756.

    Gene expression databases

    Genevestigatori P22756.

    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. "A glutamate receptor channel with high affinity for domoate and kainate."
      Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B., Seeburg P.H.
      EMBO J. 11:1651-1656(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      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].
      Tissue: Brain.
    3. "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway."
      Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J.
      J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KLHL17.
    4. "High-affinity kainate and domoate receptors in rat brain."
      Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.
      FEBS Lett. 307:139-143(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    5. "Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate."
      Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S.
      FEBS Lett. 579:1154-1160(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH GLUTAMATE, SUBUNIT.
    6. "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity."
      Mayer M.L.
      Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
    7. "Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists."
      Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.
      J. Neurosci. 26:2852-2861(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302 AND UBP310, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiGRIK1_RAT
    AccessioniPrimary (citable) accession number: P22756
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 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 domoate > kainate > L-glutamate = quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.

    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