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Q63273

- GRIK5_RAT

UniProt

Q63273 - GRIK5_RAT

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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

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. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 544530ExtracellularSequence AnalysisAdd
BLAST
Transmembranei545 – 56521HelicalSequence AnalysisAdd
BLAST
Topological domaini566 – 62257CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei623 – 64321HelicalSequence AnalysisAdd
BLAST
Topological domaini644 – 803160ExtracellularSequence AnalysisAdd
BLAST
Transmembranei804 – 82421HelicalSequence AnalysisAdd
BLAST
Topological domaini825 – 979155CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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 – 308Combined sources
Beta strandi34 – 374Combined sources
Helixi40 – 5314Combined sources
Beta strandi62 – 698Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 8511Combined sources
Helixi86 – 883Combined sources
Helixi100 – 11314Combined sources
Beta strandi117 – 1193Combined sources
Helixi129 – 1346Combined sources
Beta strandi136 – 1394Combined sources
Helixi142 – 15514Combined sources
Beta strandi161 – 1677Combined sources
Helixi170 – 1734Combined sources
Helixi175 – 1839Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi188 – 1925Combined sources
Helixi200 – 20910Combined sources
Beta strandi212 – 2187Combined sources
Helixi220 – 23213Combined sources
Turni233 – 2364Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi241 – 2444Combined sources
Helixi249 – 2513Combined sources
Turni255 – 2573Combined sources
Beta strandi263 – 2686Combined sources
Helixi277 – 28812Combined sources
Turni289 – 2913Combined sources
Helixi294 – 2963Combined sources
Helixi302 – 32120Combined sources
Turni322 – 3243Combined sources
Helixi343 – 3508Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi374 – 3818Combined sources
Beta strandi384 – 3929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 22-825.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118920.
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

        10         20         30         40         50
MPAELLLLLI VAFANPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ
60 70 80 90 100
INGIIEVPAK ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP
110 120 130 140 150
ASASTVSHIC GEKEIPHIKV GPEETPRLQY LRFASVSLYP SNEDVSLAVS
160 170 180 190 200
RILKSFNYPS ASLICAKAEC LLRLEELVRG FLISKETLSV RMLDDSRDPT
210 220 230 240 250
PLLKEIRDDK VSTIIIDANA SISHLVLRKA SELGMTSAFY KYILTTMDFP
260 270 280 290 300
ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYPGP
310 320 330 340 350
ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL
360 370 380 390 400
RMVEYDGLTG RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN
410 420 430 440 450
ATTLDINLSQ TLANKTLVVT TILENPYVMR RPNFQALSGN ERFEGFCVDM
460 470 480 490 500
LRELAELLRF RYRLRLVEDG LYGAPEPNGS WTGMVGELIN RKADLAVAAF
510 520 530 540 550
TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD PFSPAVWLFM
560 570 580 590 600
LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV
610 620 630 640 650
GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV
660 670 680 690 700
PVESADDLAD QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV
710 720 730 740 750
FVKSTEEGIA RVLNSRYAFL LESTMNEYHR RLNCNLTQIG GLLDTKGYGI
760 770 780 790 800
GMPLGSPFRD EITLAILQLQ ENNRLEILKR KWWEGGRCPK EEDHRAKGLG
810 820 830 840 850
MENIGGIFVV LICGLIIAVF VAVMEFIWST RRSAESEEVS VCQEMLQELR
860 870 880 890 900
HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG
910 920 930 940 950
AHGGPQRLLD DPGPPGGPRP QAPTPCTHVR VCQECRRIQA LRASGAGAPP
960 970
RGLGTPAEAT SPPRPRPGPT GPRELTEHE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 22-825.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246572. 1 interaction.

Chemistry

BindingDBi Q63273.
ChEMBLi CHEMBL2094119.
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 ENSGT00760000118920.
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: November 26, 2014
This is version 128 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