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Q63273

- GRIK5_RAT

UniProt

Q63273 - GRIK5_RAT

Protein

Glutamate receptor ionotropic, kainate 5

Gene

Grik5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA.

    GO - Molecular functioni

    1. extracellular-glutamate-gated ion channel activity Source: RefGenome
    2. glutamate receptor activity Source: UniProtKB
    3. identical protein binding Source: UniProtKB
    4. kainate selective glutamate receptor activity Source: RGD
    5. PDZ domain binding Source: UniProtKB
    6. protein binding Source: RGD
    7. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to glucose stimulus Source: RGD
    2. establishment of localization in cell Source: UniProtKB
    3. ionotropic glutamate receptor signaling pathway Source: GOC
    4. ion transmembrane transport Source: GOC
    5. positive regulation of neuron apoptotic process Source: RGD
    6. protein retention in ER lumen Source: UniProtKB
    7. receptor clustering Source: UniProtKB
    8. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    9. regulation of synaptic vesicle fusion to presynaptic membrane Source: Ensembl
    10. signal transduction Source: GOC
    11. synaptic transmission Source: RGD
    12. synaptic transmission, glutamatergic Source: RefGenome

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_196422. Activation of Ca-permeable Kainate Receptor.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, kainate 5
    Short name:
    GluK5
    Alternative name(s):
    Glutamate receptor KA-2
    Short name:
    KA2
    Gene namesi
    Name:Grik5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi2735. Grik5.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: RGD
    2. cell junction Source: UniProtKB-KW
    3. dendrite Source: UniProtKB
    4. endoplasmic reticulum Source: Ensembl
    5. ionotropic glutamate receptor complex Source: UniProtKB
    6. kainate selective glutamate receptor complex Source: RefGenome
    7. neuronal cell body Source: RGD
    8. neuron projection Source: RGD
    9. perikaryon Source: RGD
    10. postsynaptic density Source: RGD
    11. postsynaptic membrane Source: RefGenome
    12. presynaptic membrane Source: RefGenome
    13. 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 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 979965Glutamate receptor ionotropic, kainate 5PRO_0000011554Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 292
    Disulfide bondi83 ↔ 334
    Disulfide bondi165 ↔ 170
    Glycosylationi219 – 2191N-linked (GlcNAc...)1 Publication
    Glycosylationi271 – 2711N-linked (GlcNAc...)1 Publication
    Glycosylationi285 – 2851N-linked (GlcNAc...)1 Publication
    Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication
    Glycosylationi372 – 3721N-linked (GlcNAc...)1 Publication
    Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi478 – 4781N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ63273.
    PRIDEiQ63273.

    PTM databases

    PhosphoSiteiQ63273.

    Expressioni

    Tissue specificityi

    High expression in the cerebral cortex, pyriform cortex, caudate-putamen, hippocampal complex, medial habenulata and granule cell layer of the cerebellum. Weak expression in globus pallidus, thalamus, colliculi and the reticular thalamic nucleus.

    Developmental stagei

    From embryonic day 14 through postnatal day 1, high expression in spinal cord, brain and some areas of the PNS. At E17 and E19, high expression in spinal cord, mesencephalon and telencephalic structures as in olfactory neurons and in nasal epithelium. Strong expression also in the pituitary.

    Gene expression databases

    GenevestigatoriQ63273.

    Interactioni

    Subunit structurei

    Tetramer of two or more different subunits. Associates with GRIK1 (both edited and unedited versions), GRIK2, or GRIK3 to form functional channels. Homomeric associations do not produce any channel activity.1 Publication

    Protein-protein interaction databases

    BioGridi246572. 1 interaction.

    Structurei

    Secondary structure

    1
    979
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 308
    Beta strandi34 – 374
    Helixi40 – 5314
    Beta strandi62 – 698
    Beta strandi71 – 733
    Helixi75 – 8511
    Helixi86 – 883
    Helixi100 – 11314
    Beta strandi117 – 1193
    Helixi129 – 1346
    Beta strandi136 – 1394
    Helixi142 – 15514
    Beta strandi161 – 1677
    Helixi170 – 1734
    Helixi175 – 1839
    Beta strandi184 – 1863
    Beta strandi188 – 1925
    Helixi200 – 20910
    Beta strandi212 – 2187
    Helixi220 – 23213
    Turni233 – 2364
    Beta strandi237 – 2393
    Beta strandi241 – 2444
    Helixi249 – 2513
    Turni255 – 2573
    Beta strandi263 – 2686
    Helixi277 – 28812
    Turni289 – 2913
    Helixi294 – 2963
    Helixi302 – 32120
    Turni322 – 3243
    Helixi343 – 3508
    Beta strandi355 – 3573
    Beta strandi360 – 3623
    Beta strandi374 – 3818
    Beta strandi384 – 3929

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OM0X-ray1.40A20-406[»]
    3OM1X-ray1.68A/B20-406[»]
    3QLUX-ray2.91A/B20-406[»]
    3QLVX-ray3.94A/B/E/G/I20-406[»]
    ProteinModelPortaliQ63273.
    SMRiQ63273. Positions 22-828.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini15 – 544530ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini566 – 62257CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini644 – 803160ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini825 – 979155CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei545 – 56521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei623 – 64321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei804 – 82421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi860 – 8667Poly-Arg

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    GeneTreeiENSGT00740000114953.
    HOGENOMiHOG000234371.
    HOVERGENiHBG051839.
    InParanoidiQ63273.
    KOiK05205.
    OMAiGLNCNLT.
    OrthoDBiEOG71G9W6.
    PhylomeDBiQ63273.
    TreeFamiTF334668.

    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q63273-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAELLLLLI VAFANPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ    50
    INGIIEVPAK ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP 100
    ASASTVSHIC GEKEIPHIKV GPEETPRLQY LRFASVSLYP SNEDVSLAVS 150
    RILKSFNYPS ASLICAKAEC LLRLEELVRG FLISKETLSV RMLDDSRDPT 200
    PLLKEIRDDK VSTIIIDANA SISHLVLRKA SELGMTSAFY KYILTTMDFP 250
    ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYPGP 300
    ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL 350
    RMVEYDGLTG RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN 400
    ATTLDINLSQ TLANKTLVVT TILENPYVMR RPNFQALSGN ERFEGFCVDM 450
    LRELAELLRF RYRLRLVEDG LYGAPEPNGS WTGMVGELIN RKADLAVAAF 500
    TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD PFSPAVWLFM 550
    LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV 600
    GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV 650
    PVESADDLAD QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV 700
    FVKSTEEGIA RVLNSRYAFL LESTMNEYHR RLNCNLTQIG GLLDTKGYGI 750
    GMPLGSPFRD EITLAILQLQ ENNRLEILKR KWWEGGRCPK EEDHRAKGLG 800
    MENIGGIFVV LICGLIIAVF VAVMEFIWST RRSAESEEVS VCQEMLQELR 850
    HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG 900
    AHGGPQRLLD DPGPPGGPRP QAPTPCTHVR VCQECRRIQA LRASGAGAPP 950
    RGLGTPAEAT SPPRPRPGPT GPRELTEHE 979
    Length:979
    Mass (Da):109,276
    Last modified:November 1, 1996 - v1
    Checksum:i313E2862746474B1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti887 – 8871N → G1 PublicationCurated
    Sequence conflicti889 – 8891K → R1 PublicationCurated
    Sequence conflicti910 – 9101D → N in AAA17831. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11581 mRNA. Translation: CAA77667.1.
    U08258 mRNA. Translation: AAA17831.1.
    PIRiJH0592.
    RefSeqiNP_113696.1. NM_031508.2.
    UniGeneiRn.74042.

    Genome annotation databases

    EnsembliENSRNOT00000027578; ENSRNOP00000027578; ENSRNOG00000020310.
    GeneIDi24407.
    KEGGirno:24407.
    UCSCiRGD:2735. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11581 mRNA. Translation: CAA77667.1 .
    U08258 mRNA. Translation: AAA17831.1 .
    PIRi JH0592.
    RefSeqi NP_113696.1. NM_031508.2.
    UniGenei Rn.74042.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OM0 X-ray 1.40 A 20-406 [» ]
    3OM1 X-ray 1.68 A/B 20-406 [» ]
    3QLU X-ray 2.91 A/B 20-406 [» ]
    3QLV X-ray 3.94 A/B/E/G/I 20-406 [» ]
    ProteinModelPortali Q63273.
    SMRi Q63273. Positions 22-828.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246572. 1 interaction.

    Chemistry

    BindingDBi Q63273.
    ChEMBLi CHEMBL4041.
    GuidetoPHARMACOLOGYi 454.

    PTM databases

    PhosphoSitei Q63273.

    Proteomic databases

    PaxDbi Q63273.
    PRIDEi Q63273.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000027578 ; ENSRNOP00000027578 ; ENSRNOG00000020310 .
    GeneIDi 24407.
    KEGGi rno:24407.
    UCSCi RGD:2735. rat.

    Organism-specific databases

    CTDi 2901.
    RGDi 2735. Grik5.

    Phylogenomic databases

    eggNOGi NOG316680.
    GeneTreei ENSGT00740000114953.
    HOGENOMi HOG000234371.
    HOVERGENi HBG051839.
    InParanoidi Q63273.
    KOi K05205.
    OMAi GLNCNLT.
    OrthoDBi EOG71G9W6.
    PhylomeDBi Q63273.
    TreeFami TF334668.

    Enzyme and pathway databases

    Reactomei REACT_196422. Activation of Ca-permeable Kainate Receptor.

    Miscellaneous databases

    NextBioi 603217.
    PROi Q63273.

    Gene expression databases

    Genevestigatori Q63273.

    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. "The KA-2 subunit of excitatory amino acid receptors shows widespread expression in brain and forms ion channels with distantly related subunits."
      Herb A., Burnashev N., Werner P., Sakmann B., Wisden W., Seeburg P.H.
      Neuron 8:775-785(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. Boulter J., Pecht G.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. "Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains."
      Kumar J., Mayer M.L.
      J. Mol. Biol. 404:680-696(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-406, GLYCOSYLATION AT ASN-219; ASN-271; ASN-285; ASN-322 AND ASN-372, DISULFIDE BONDS.
    4. "Structure and assembly mechanism for heteromeric kainate receptors."
      Kumar J., Schuck P., Mayer M.L.
      Neuron 71:319-331(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 20-406 IN COMPLEX WITH GRIK2, DISULFIDE BONDS, SUBUNIT.

    Entry informationi

    Entry nameiGRIK5_RAT
    AccessioniPrimary (citable) accession number: Q63273
    Secondary accession number(s): Q62643
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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