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Protein

Glutamate receptor ionotropic, kainate 3

Gene

Grik3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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 >> AMPA = NMDA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei520Glutamate1 Publication1
Binding sitei525Glutamate1 Publication1
Binding sitei739Glutamate1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • chemical synaptic transmission Source: RGD
  • negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
  • regulation of membrane potential Source: MGI
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 3
Short name:
GluK3
Alternative name(s):
Glutamate receptor 7
Short name:
GluR-7
Short name:
GluR7
Gene namesi
Name:Grik3
Synonyms:Glur7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71027. Grik3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 563ExtracellularAdd BLAST532
Transmembranei564 – 584HelicalSequence analysisAdd BLAST21
Topological domaini585 – 636CytoplasmicSequence analysisAdd BLAST52
Transmembranei637 – 657HelicalSequence analysisAdd BLAST21
Topological domaini658 – 820ExtracellularSequence analysisAdd BLAST163
Transmembranei821 – 841HelicalSequence analysisAdd BLAST21
Topological domaini842 – 919CytoplasmicSequence analysisAdd BLAST78

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB
  • dendrite cytoplasm Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • 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

ChEMBLiCHEMBL3744.
GuidetoPHARMACOLOGYi452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000001154832 – 919Glutamate receptor ionotropic, kainate 3Add BLAST888

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi70N-linked (GlcNAc...)1 Publication1
Glycosylationi76N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi99 ↔ 3501 Publication
Glycosylationi278N-linked (GlcNAc...)1 Publication1
Glycosylationi381N-linked (GlcNAc...)1 Publication1
Glycosylationi415N-linked (GlcNAc...)Sequence analysis1
Glycosylationi426N-linked (GlcNAc...)Sequence analysis1
Glycosylationi433N-linked (GlcNAc...)Sequence analysis1
Glycosylationi548N-linked (GlcNAc...)Sequence analysis1
Modified residuei869PhosphoserineBy similarity1
Cross-linki887Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Mass spectrometry data suggest the protein is N-glycosylated at five distinct sites.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP42264.
PRIDEiP42264.

PTM databases

PhosphoSitePlusiP42264.

Expressioni

Tissue specificityi

Expressed in the deep cortical layers, dentate gyrus, reticular thalamic nucleus, mammillary bodies, pons, and cerebellum of the adult.

Developmental stagei

Expressed in both adult and embryonic CNS.

Interactioni

Subunit structurei

Homotetramer, and heterotetramer with GRIK4 or GRIK5. Homomeric GLUR7A and GLUR7B form functional kainate receptors. GLUR7A receptors have a very low sensitivity to glutamate. GLUR7A can also coassemble with either GRIK4 or GRIK5 to form heteromeric receptors. Interacts with PRKCABP. Interacts with NETO2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048216.

Chemistry databases

BindingDBiP42264.

Structurei

Secondary structure

1919
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 43Combined sources9
Helixi47 – 49Combined sources3
Helixi55 – 69Combined sources15
Beta strandi71 – 74Combined sources4
Beta strandi78 – 86Combined sources9
Helixi91 – 104Combined sources14
Beta strandi113 – 115Combined sources3
Helixi118 – 128Combined sources11
Beta strandi132 – 134Combined sources3
Beta strandi148 – 154Combined sources7
Helixi156 – 169Combined sources14
Beta strandi173 – 181Combined sources9
Helixi184 – 187Combined sources4
Helixi189 – 192Combined sources4
Turni195 – 197Combined sources3
Beta strandi201 – 206Combined sources6
Helixi215 – 223Combined sources9
Beta strandi228 – 233Combined sources6
Helixi235 – 247Combined sources13
Beta strandi256 – 259Combined sources4
Helixi264 – 266Combined sources3
Turni270 – 275Combined sources6
Beta strandi278 – 283Combined sources6
Helixi290 – 302Combined sources13
Helixi321 – 339Combined sources19
Beta strandi350 – 352Combined sources3
Helixi359 – 368Combined sources10
Beta strandi370 – 373Combined sources4
Beta strandi376 – 379Combined sources4
Turni382 – 384Combined sources3
Beta strandi392 – 398Combined sources7
Beta strandi401 – 409Combined sources9
Turni410 – 412Combined sources3
Beta strandi413 – 415Combined sources3
Beta strandi436 – 440Combined sources5
Turni444 – 446Combined sources3
Beta strandi447 – 449Combined sources3
Helixi458 – 461Combined sources4
Beta strandi462 – 464Combined sources3
Helixi465 – 477Combined sources13
Beta strandi481 – 485Combined sources5
Beta strandi496 – 498Combined sources3
Helixi502 – 508Combined sources7
Beta strandi513 – 520Combined sources8
Helixi523 – 526Combined sources4
Beta strandi529 – 531Combined sources3
Beta strandi535 – 538Combined sources4
Beta strandi540 – 546Combined sources7
Helixi673 – 677Combined sources5
Beta strandi680 – 685Combined sources6
Helixi691 – 698Combined sources8
Helixi702 – 711Combined sources10
Turni715 – 717Combined sources3
Beta strandi718 – 721Combined sources4
Helixi722 – 731Combined sources10
Beta strandi732 – 739Combined sources8
Helixi740 – 749Combined sources10
Beta strandi753 – 757Combined sources5
Beta strandi763 – 770Combined sources8
Helixi776 – 788Combined sources13
Helixi791 – 800Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OLZX-ray2.75A/B32-423[»]
3S9EX-ray1.60A/B432-546[»]
A/B669-806[»]
3U92X-ray1.90A/B433-546[»]
A/B669-807[»]
3U93X-ray1.88A/B433-546[»]
A/B669-807[»]
3U94X-ray1.96A/B/C/D433-546[»]
A/B/C/D669-807[»]
4E0WX-ray2.35A669-806[»]
4G8NX-ray2.30A432-546[»]
A669-806[»]
4IGRX-ray2.65A432-546[»]
A669-806[»]
4MH5X-ray1.65A432-546[»]
A669-806[»]
4NWCX-ray2.01A432-546[»]
A669-806[»]
4NWDX-ray2.60A432-546[»]
A669-806[»]
ProteinModelPortaliP42264.
SMRiP42264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni690 – 692Glutamate binding3

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiP42264.
KOiK05203.
PhylomeDBiP42264.

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.

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. AlignAdd to basket

Isoform GluR7A (identifier: P42264-1) [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

        10         20         30         40         50
MTAPWRRLRS LVWEYWAGFL VCAFWIPDSR GMPHVIRIGG IFEYADGPNA
60 70 80 90 100
QVMNAEEHAF RFSANIINRN RTLLPNTTLT YDIQRIHFHD SFEATKKACD
110 120 130 140 150
QLALGVVAIF GPSQGSCTNA VQSICNALEV PHIQLRWKHH PLDNKDTFYV
160 170 180 190 200
NLYPDYASLS HAILDLVQSL KWRSATVVYD DSTGLIRLQE LIMAPSRYNI
210 220 230 240 250
RLKIRQLPID SDDSRPLLKE MKRGREFRII FDCSHTMAAQ ILKQAMAMGM
260 270 280 290 300
MTEYYHFIFT TLDLYALDLE PYRYSGVNLT GFRILNVDNA HVSAIVEKWS
310 320 330 340 350
MERLQAAPRA ESGLLDGVMM TDAALLYDAV HIVSVCYQRA SQMTVNSLQC
360 370 380 390 400
HRHKPWRFGG RFMNFIKEAQ WEGLTGRIVF NKTSGLRTDF DLDIISLKED
410 420 430 440 450
GLEKVGVWSP ADGLNITEVA KGRGPNVTDS LTNRSLIVTT LLEEPFVMFR
460 470 480 490 500
KSDRTLYGND RFEGYCIDLL KELAHILGFS YEIRLVEDGK YGAQDDKGQW
510 520 530 540 550
NGMVKELIDH KADLAVAPLT ITHVREKAID FSKPFMTLGV SILYRKPNGT
560 570 580 590 600
NPSVFSFLNP LSPDIWMYVL LAYLGVSCVL FVIARFSPYE WYDAHPCNPG
610 620 630 640 650
SEVVENNFTL LNSFWFGMGS LMQQGSELMP KALSTRIIGG IWWFFTLIII
660 670 680 690 700
SSYTANLAAF LTVERMESPI DSADDLAKQT KIEYGAVKDG ATMTFFKKSK
710 720 730 740 750
ISTFEKMWAF MSSKPSALVK NNEEGIQRTL TADYALLMES TTIEYITQRN
760 770 780 790 800
CNLTQIGGLI DSKGYGIGTP MGSPYRDKIT IAILQLQEED KLHIMKEKWW
810 820 830 840 850
RGSGCPEEEN KEASALGIQK IGGIFIVLAA GLVLSVLVAV GEFIYKLRKT
860 870 880 890 900
AEREQRSFCS TVADEIRFSL TCQRRLKHKP QPPMMVKTDA VINMHTFNDR
910
RLPGKDSMSC STSLAPVFP
Length:919
Mass (Da):104,071
Last modified:November 1, 1995 - v1
Checksum:iC0739129ACF60258
GO
Isoform GluR7B (identifier: P42264-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     856-919: RSFCSTVADE...CSTSLAPVFP → VRPWRRLRWT...DRCGYQHAHL

Show »
Length:910
Mass (Da):103,110
Checksum:i9E5F936327334A52
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti118T → I (PubMed:1371217).Curated1
Sequence conflicti290A → P in AAC80577 (PubMed:1371217).Curated1
Sequence conflicti341S → P in AAC80577 (PubMed:1371217).Curated1
Sequence conflicti355P → A in AAC80577 (PubMed:1371217).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000135856 – 919RSFCS…APVFP → VRPWRRLRWTGKEALFLQHS GRRDPLLPHLPAASQAQATA SYDGQDRCGYQHAHL in isoform GluR7B. 1 PublicationAdd BLAST64

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11716 mRNA. Translation: CAA77779.1.
AF027331 mRNA. Translation: AAC53462.1.
M83552 mRNA. Translation: AAC80577.1.
PIRiI53474.
S19810.
RefSeqiNP_001106187.1. NM_001112716.1.
NP_852038.2. NM_181373.3.
UniGeneiRn.92477.

Genome annotation databases

GeneIDi298521.
KEGGirno:298521.
UCSCiRGD:71027. rat. [P42264-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11716 mRNA. Translation: CAA77779.1.
AF027331 mRNA. Translation: AAC53462.1.
M83552 mRNA. Translation: AAC80577.1.
PIRiI53474.
S19810.
RefSeqiNP_001106187.1. NM_001112716.1.
NP_852038.2. NM_181373.3.
UniGeneiRn.92477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OLZX-ray2.75A/B32-423[»]
3S9EX-ray1.60A/B432-546[»]
A/B669-806[»]
3U92X-ray1.90A/B433-546[»]
A/B669-807[»]
3U93X-ray1.88A/B433-546[»]
A/B669-807[»]
3U94X-ray1.96A/B/C/D433-546[»]
A/B/C/D669-807[»]
4E0WX-ray2.35A669-806[»]
4G8NX-ray2.30A432-546[»]
A669-806[»]
4IGRX-ray2.65A432-546[»]
A669-806[»]
4MH5X-ray1.65A432-546[»]
A669-806[»]
4NWCX-ray2.01A432-546[»]
A669-806[»]
4NWDX-ray2.60A432-546[»]
A669-806[»]
ProteinModelPortaliP42264.
SMRiP42264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048216.

Chemistry databases

BindingDBiP42264.
ChEMBLiCHEMBL3744.
GuidetoPHARMACOLOGYi452.

PTM databases

PhosphoSitePlusiP42264.

Proteomic databases

PaxDbiP42264.
PRIDEiP42264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi298521.
KEGGirno:298521.
UCSCiRGD:71027. rat. [P42264-1]

Organism-specific databases

CTDi2899.
RGDi71027. Grik3.

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiP42264.
KOiK05203.
PhylomeDBiP42264.

Miscellaneous databases

PROiP42264.

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 nameiGRIK3_RAT
AccessioniPrimary (citable) accession number: P42264
Secondary accession number(s): O35420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 151 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, Direct protein sequencing, 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.