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Protein

Glutamate receptor ionotropic, kainate 4

Gene

Grik4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • ionotropic glutamate receptor activity Source: RGD
  • kainate selective glutamate receptor activity Source: RGD

GO - Biological processi

  • chemical synaptic transmission Source: RGD
  • ion transport Source: RGD
  • response to corticosteroid Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, kainate 4
Short name:
GluK4
Alternative name(s):
Glutamate receptor KA-1
Short name:
KA1
Gene namesi
Name:Grik4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2734. Grik4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 545ExtracellularSequence analysisAdd BLAST525
Transmembranei546 – 566HelicalSequence analysisAdd BLAST21
Topological domaini567 – 623CytoplasmicSequence analysisAdd BLAST57
Transmembranei624 – 644HelicalSequence analysisAdd BLAST21
Topological domaini645 – 804ExtracellularSequence analysisAdd BLAST160
Transmembranei805 – 825HelicalSequence analysisAdd BLAST21
Topological domaini826 – 956CytoplasmicSequence analysisAdd BLAST131

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: RGD
  • ionotropic glutamate receptor complex Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3044.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001155121 – 956Glutamate receptor ionotropic, kainate 4Add BLAST936

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Glycosylationi220N-linked (GlcNAc...)Sequence analysis1
Glycosylationi272N-linked (GlcNAc...)Sequence analysis1
Glycosylationi286N-linked (GlcNAc...)Sequence analysis1
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi415N-linked (GlcNAc...)Sequence analysis1
Glycosylationi479N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ01812.
PRIDEiQ01812.

Expressioni

Tissue specificityi

Strong expression in hippocampal CA3 pyramidal cells. Low expression in hippocampal dentate granule cells, in layers II, V and VI of the cortex, and in cerebellar Purkinje cells. No expression in the striatum, reticular thalamus, hypothalamus or amygdaloid complex.

Developmental stagei

Expressed at embryonic day 15 in brain and spinal cord. At embryonic day 19 expression accumulates in the hippocampal formation. Prominent expression in the subicular cortex at postnatal days P1, P8 and P15 but then markedly reduced in the adult.

Gene expression databases

BgeeiENSRNOG00000030910.

Interactioni

Subunit structurei

Forms a heteromeric channel with GRIK1 or GRIK3.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047794.

Chemistry databases

BindingDBiQ01812.

Structurei

Secondary structure

1956
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi418 – 422Combined sources5
Turni426 – 428Combined sources3
Beta strandi429 – 431Combined sources3
Helixi435 – 437Combined sources3
Helixi440 – 443Combined sources4
Beta strandi444 – 446Combined sources3
Helixi447 – 459Combined sources13
Beta strandi463 – 467Combined sources5
Helixi484 – 490Combined sources7
Beta strandi495 – 497Combined sources3
Helixi505 – 508Combined sources4
Beta strandi511 – 513Combined sources3
Beta strandi517 – 520Combined sources4
Beta strandi522 – 526Combined sources5
Helixi656 – 660Combined sources5
Beta strandi663 – 668Combined sources6
Helixi674 – 680Combined sources7
Helixi685 – 696Combined sources12
Beta strandi703 – 705Combined sources3
Helixi706 – 715Combined sources10
Beta strandi716 – 723Combined sources8
Helixi724 – 732Combined sources9
Beta strandi737 – 739Combined sources3
Beta strandi747 – 749Combined sources3
Beta strandi752 – 754Combined sources3
Helixi760 – 772Combined sources13
Helixi775 – 784Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IKBX-ray2.05A415-526[»]
A652-790[»]
ProteinModelPortaliQ01812.
SMRiQ01812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi862 – 865Poly-Arg4

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1052. Eukaryota.
ENOG410XQQV. LUCA.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiQ01812.
KOiK05204.
PhylomeDBiQ01812.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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.

Q01812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRVSAPLVL LPAWLLMVAC SPHSLRIAAI LDDPMECSRG ERLSITLAKN
60 70 80 90 100
RINRAPERLG KAKVEVDIFE LLRDSEYETA ETMCQILPKG VVAVLGPSSS
110 120 130 140 150
PASSSIISNI CGEKEVPHFK VAPEEFVRFQ LQRFTTLNLH PSNTDISVAV
160 170 180 190 200
AGILNFFNCT TACLICAKAE CLLNLEKLLR QFLISKDTLS VRMLDDTRDP
210 220 230 240 250
TPLLKEIRDD KTATIIIHAN ASMSHTILLK AAELGMVSAY YTYIFTNLEF
260 270 280 290 300
SLQRMDSLVD DRVNILGFSI FNQSHAFFQE FSQSLNQSWQ ENCDHVPFTG
310 320 330 340 350
PALSSALLFD AVYAVVTAVQ ELNRSQEIGV KPLSCGSAQI WQHGTSLMNY
360 370 380 390 400
LRMVELEGLT GHIEFNSKGQ RSNYALKILQ FTRNGFRQIG QWHVAEGLSM
410 420 430 440 450
DSRLYASNIS DSLFNTTLVV TTILENPYLM LKGNHQDMEG NDRYEGFCVD
460 470 480 490 500
MLKELAEILR FNYKIRLVGD GVYGVPEANG TWTGMVGELI ARKADLAVAG
510 520 530 540 550
LTITAEREKV IDFSKPFMTL GISILYRVHM GRRPGYFSSL DPFSPGVWLF
560 570 580 590 600
MLLAYLAVSC VLFLVARLTP YEWYSPHPCA QGRCNLLVNQ YSLGNSLWFP
610 620 630 640 650
VGGFMQQGST IAPRALSTRC VSGVWWAFTL IIISSYTANL AAFLTVQRME
660 670 680 690 700
VPIESVDDLA DQTAIEYGTI HGGSSMTFFQ NSRYQTYQRM WNYMYSKQPS
710 720 730 740 750
VFVKSTEEGI ARVLNSNYAF LLESTMNEYY RQRNCNLTQI GGLLDTKGYG
760 770 780 790 800
IGMPVGSVFR DEFDLAILQL QENNRLEILK RKWWEGGKCP KEEDHRAKGL
810 820 830 840 850
GMENIGGIFV VLICGLIVAI FMAMLEFLWT LRHSEASEVS VCQEMMTELR
860 870 880 890 900
SIILCQDNIH PRRRRSGGLP PQPPVLEERR PRGTATLSNG KLCGAGEPDQ
910 920 930 940 950
LAQRLAQEAA LVARGCTHIR VCPECRRFQG LRARPSPARS EESLEWDKTT

NSSEPE
Length:956
Mass (Da):107,223
Last modified:November 1, 1996 - v1
Checksum:i970C9D72C8D74700
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti539S → F in AAA17830 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59996 mRNA. Translation: CAA42615.1.
U08257 mRNA. Translation: AAA17830.1.
PIRiJS0685.
RefSeqiNP_036704.1. NM_012572.1.
XP_017450943.1. XM_017595454.1.
XP_017450944.1. XM_017595455.1.
UniGeneiRn.10049.

Genome annotation databases

GeneIDi24406.
KEGGirno:24406.
UCSCiRGD:2734. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59996 mRNA. Translation: CAA42615.1.
U08257 mRNA. Translation: AAA17830.1.
PIRiJS0685.
RefSeqiNP_036704.1. NM_012572.1.
XP_017450943.1. XM_017595454.1.
XP_017450944.1. XM_017595455.1.
UniGeneiRn.10049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IKBX-ray2.05A415-526[»]
A652-790[»]
ProteinModelPortaliQ01812.
SMRiQ01812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047794.

Chemistry databases

BindingDBiQ01812.
ChEMBLiCHEMBL3044.

Proteomic databases

PaxDbiQ01812.
PRIDEiQ01812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24406.
KEGGirno:24406.
UCSCiRGD:2734. rat.

Organism-specific databases

CTDi2900.
RGDi2734. Grik4.

Phylogenomic databases

eggNOGiKOG1052. Eukaryota.
ENOG410XQQV. LUCA.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiQ01812.
KOiK05204.
PhylomeDBiQ01812.

Miscellaneous databases

PROiQ01812.

Gene expression databases

BgeeiENSRNOG00000030910.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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.
ProtoNetiSearch...

Entry informationi

Entry nameiGRIK4_RAT
AccessioniPrimary (citable) accession number: Q01812
Secondary accession number(s): Q62642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.