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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei520 – 5201Glutamate1 Publication
Binding sitei525 – 5251Glutamate1 Publication
Binding sitei739 – 7391Glutamate1 Publication

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

  • negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
  • regulation of membrane potential Source: MGI
  • synaptic transmission 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 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 563532ExtracellularAdd
BLAST
Transmembranei564 – 58421HelicalSequence analysisAdd
BLAST
Topological domaini585 – 63652CytoplasmicSequence analysisAdd
BLAST
Transmembranei637 – 65721HelicalSequence analysisAdd
BLAST
Topological domaini658 – 820163ExtracellularSequence analysisAdd
BLAST
Transmembranei821 – 84121HelicalSequence analysisAdd
BLAST
Topological domaini842 – 91978CytoplasmicSequence analysisAdd
BLAST

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

ChEMBLiCHEMBL2094119.
GuidetoPHARMACOLOGYi452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 919888Glutamate receptor ionotropic, kainate 3PRO_0000011548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence analysis
Disulfide bondi99 ↔ 3501 Publication
Glycosylationi278 – 2781N-linked (GlcNAc...)1 Publication
Glycosylationi381 – 3811N-linked (GlcNAc...)1 Publication
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence analysis
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence analysis
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence analysis
Modified residuei869 – 8691PhosphoserineBy similarity
Cross-linki887 – 887Glycyl 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.

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

BindingDBiP42264.

Structurei

Secondary structure

1
919
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 439Combined sources
Helixi47 – 493Combined sources
Helixi55 – 6915Combined sources
Beta strandi71 – 744Combined sources
Beta strandi78 – 869Combined sources
Helixi91 – 10414Combined sources
Beta strandi113 – 1153Combined sources
Helixi118 – 12811Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi148 – 1547Combined sources
Helixi156 – 16914Combined sources
Beta strandi173 – 1819Combined sources
Helixi184 – 1874Combined sources
Helixi189 – 1924Combined sources
Turni195 – 1973Combined sources
Beta strandi201 – 2066Combined sources
Helixi215 – 2239Combined sources
Beta strandi228 – 2336Combined sources
Helixi235 – 24713Combined sources
Beta strandi256 – 2594Combined sources
Helixi264 – 2663Combined sources
Turni270 – 2756Combined sources
Beta strandi278 – 2836Combined sources
Helixi290 – 30213Combined sources
Helixi321 – 33919Combined sources
Beta strandi350 – 3523Combined sources
Helixi359 – 36810Combined sources
Beta strandi370 – 3734Combined sources
Beta strandi376 – 3794Combined sources
Turni382 – 3843Combined sources
Beta strandi392 – 3987Combined sources
Beta strandi401 – 4099Combined sources
Turni410 – 4123Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi436 – 4405Combined sources
Turni444 – 4463Combined sources
Beta strandi447 – 4493Combined sources
Helixi458 – 4614Combined sources
Beta strandi462 – 4643Combined sources
Helixi465 – 47713Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi496 – 4983Combined sources
Helixi502 – 5087Combined sources
Beta strandi513 – 5208Combined sources
Helixi523 – 5264Combined sources
Beta strandi529 – 5313Combined sources
Beta strandi535 – 5384Combined sources
Beta strandi540 – 5467Combined sources
Helixi673 – 6775Combined sources
Beta strandi680 – 6856Combined sources
Helixi691 – 6988Combined sources
Helixi702 – 71110Combined sources
Turni715 – 7173Combined sources
Beta strandi718 – 7214Combined sources
Helixi722 – 73110Combined sources
Beta strandi732 – 7398Combined sources
Helixi740 – 74910Combined sources
Beta strandi753 – 7575Combined sources
Beta strandi763 – 7708Combined sources
Helixi776 – 78813Combined sources
Helixi791 – 80010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 426-548, 665-807.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni690 – 6923Glutamate binding

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181T → I (PubMed:1371217).Curated
Sequence conflicti290 – 2901A → P in AAC80577 (PubMed:1371217).Curated
Sequence conflicti341 – 3411S → P in AAC80577 (PubMed:1371217).Curated
Sequence conflicti355 – 3551P → A in AAC80577 (PubMed:1371217).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei856 – 91964RSFCS…APVFP → VRPWRRLRWTGKEALFLQHS GRRDPLLPHLPAASQAQATA SYDGQDRCGYQHAHL in isoform GluR7B. 1 PublicationVSP_000135Add
BLAST

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
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. Positions 426-548, 665-807.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048216.

Chemistry

BindingDBiP42264.
ChEMBLiCHEMBL2094119.
GuidetoPHARMACOLOGYi452.

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...

Publicationsi

  1. "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] (ISOFORM GLUR7A).
    Tissue: Brain.
  2. Sprengel R.
    Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional kainate receptor subunits with a low sensitivity to glutamate."
    Schiffer H.H., Swanson G.T., Heinemann S.F.
    Neuron 19:1141-1146(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLUR7B).
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Cloning of a putative glutamate receptor: a low affinity kainate-binding subunit."
    Bettler B., Egebjerg J., Sharma G., Pecht G., Hermans-Borgmeyer I., Moll C., Stevens C.F., Heinemann S.F.
    Neuron 8:257-265(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-919 (ISOFORM GLUR7A).
  5. "Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1."
    El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.
    Eur. J. Neurosci. 12:4215-4221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCABP.
  6. "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 (2.75 ANGSTROMS) OF 32-423, PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, MEMBRANE TOPOLOGY, DISULFIDE BOND, GLYCOSYLATION AT ASN-70; ASN-278 AND ASN-381, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Binding site and interlobe interactions of the ionotropic glutamate receptor GluK3 ligand binding domain revealed by high resolution crystal structure in complex with (S)-glutamate."
    Venskutonyte R., Frydenvang K., Gajhede M., Bunch L., Pickering D.S., Kastrup J.S.
    J. Struct. Biol. 176:307-314(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 432-806 IN COMPLEX WITH GLUTAMATE, FUNCTION, SUBUNIT.

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: July 6, 2016
This is version 148 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.