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P22756

- GRIK1_RAT

UniProt

P22756 - GRIK1_RAT

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Protein

Glutamate receptor ionotropic, kainate 1

Gene

Grik1

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

Functioni

Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei538 – 5381Glutamate2 Publications
Binding sitei753 – 7531Glutamate2 Publications

GO - Molecular functioni

  1. drug binding Source: RGD
  2. extracellular-glutamate-gated ion channel activity Source: RGD
  3. glutamate binding Source: RGD
  4. ionotropic glutamate receptor activity Source: RGD
  5. kainate selective glutamate receptor activity Source: RGD
  6. protein homodimerization activity Source: RGD
  7. voltage-gated cation channel activity Source: RGD

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: RGD
  2. ion transmembrane transport Source: GOC
  3. negative regulation of synaptic transmission, GABAergic Source: RGD
  4. negative regulation of synaptic transmission, glutamatergic Source: RGD
  5. nervous system development Source: RGD
  6. positive regulation of synaptic transmission, GABAergic Source: RGD
  7. regulation of ion transmembrane transport Source: GOC
  8. regulation of short-term neuronal synaptic plasticity Source: RGD
  9. regulation of synaptic plasticity Source: UniProtKB
  10. synaptic transmission Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Protein family/group databases

TCDBi1.A.10.1.5. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, kainate 1
Short name:
GluK1
Alternative name(s):
Glutamate receptor 5
Short name:
GluR-5
Short name:
GluR5
Gene namesi
Name:Grik1
Synonyms:Glur5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 11

Organism-specific databases

RGDi2732. Grik1.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. dendrite Source: RGD
  3. ionotropic glutamate receptor complex Source: RGD
  4. kainate selective glutamate receptor complex Source: RefGenome
  5. neuronal cell body Source: RGD
  6. postsynaptic membrane Source: RefGenome
  7. presynaptic membrane Source: RefGenome
  8. receptor complex Source: UniProtKB
  9. 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 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 949919Glutamate receptor ionotropic, kainate 1PRO_0000011543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
Modified residuei725 – 7251Phosphoserine; by PKCSequence Analysis
Modified residuei761 – 7611Phosphothreonine; by PKCSequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP22756.
PRIDEiP22756.

PTM databases

PhosphoSiteiP22756.

Expressioni

Tissue specificityi

Expressed in subsets of neurons throughout the developing and adult central and peripheral nervous systems. In the CNS principally in the medial amygdaloid nuclei, medial habenulae, pyriform and cingulate cortices, and Purkinje cell layer. Also highly expressed in embryonic and adult dorsal root ganglia.

Gene expression databases

ExpressionAtlasiP22756. baseline and differential.
GenevestigatoriP22756.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers (Probable). The unedited version (Q) assembles into a functional kainate-gated homomeric channel, whereas the edited version (R) is unable to produce channel activity when expressed alone. Both edited and unedited versions can form functional channels with GRIK4 and GRIK5. Interacts with KLHL17.4 PublicationsCurated

Protein-protein interaction databases

BioGridi248193. 4 interactions.
DIPiDIP-29257N.
STRINGi10116.ENSRNOP00000045594.

Structurei

Secondary structure

1
949
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi449 – 4535
Turni457 – 4593
Beta strandi460 – 4623
Helixi471 – 4744
Beta strandi475 – 4773
Helixi478 – 49013
Beta strandi494 – 4985
Helixi515 – 5217
Beta strandi526 – 5283
Helixi536 – 5394
Beta strandi542 – 5443
Beta strandi548 – 5514
Beta strandi553 – 5597
Helixi671 – 6755
Beta strandi678 – 6836
Helixi689 – 6968
Helixi700 – 70910
Beta strandi716 – 7205
Helixi721 – 73010
Beta strandi731 – 7388
Helixi739 – 74810
Beta strandi752 – 7565
Beta strandi762 – 7643
Beta strandi767 – 7693
Helixi774 – 78714
Helixi790 – 7989
Helixi806 – 8149

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TXFX-ray2.10A446-559[»]
A682-821[»]
1VSOX-ray1.85A445-559[»]
A682-820[»]
1YCJX-ray1.95A/B445-559[»]
2F34X-ray1.74A/B446-559[»]
A/B682-821[»]
2F35X-ray1.87A/B446-559[»]
A/B682-821[»]
2F36X-ray2.11A/B/C/D446-559[»]
A/B/C/D682-821[»]
2OJTX-ray1.95A/B446-559[»]
A/B682-821[»]
2PBWX-ray2.50A/B445-559[»]
A/B682-820[»]
2QS1X-ray1.80A/B446-559[»]
A/B682-821[»]
2QS2X-ray1.80A/B446-559[»]
A/B682-821[»]
2QS3X-ray1.76A/B446-559[»]
A/B682-821[»]
2QS4X-ray1.58A/B/C/D446-559[»]
A/B/C/D682-821[»]
2WKYX-ray2.20A/B445-559[»]
A/B667-821[»]
3C31X-ray1.49A/B446-559[»]
A/B682-821[»]
3C32X-ray1.72A/B446-559[»]
A/B682-821[»]
3C33X-ray1.72A/B446-559[»]
A/B682-821[»]
3C34X-ray1.82A/B446-559[»]
A/B682-821[»]
3C35X-ray1.97A/B446-559[»]
A/B682-821[»]
3C36X-ray1.68A/B446-559[»]
A/B682-821[»]
3GBAX-ray1.35A/B/C/D445-559[»]
A/B/C/D682-820[»]
3GBBX-ray2.10A/B445-559[»]
A/B682-820[»]
3S2VX-ray2.50A/B445-559[»]
A/B682-820[»]
4DLDX-ray2.00A/B445-559[»]
A/B682-820[»]
4E0XX-ray2.00A/B682-820[»]
ProteinModelPortaliP22756.
SMRiP22756. Positions 445-559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22756.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 576546ExtracellularSequence AnalysisAdd
BLAST
Topological domaini598 – 65356CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini675 – 834160ExtracellularSequence AnalysisAdd
BLAST
Topological domaini856 – 94994CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei577 – 59721HelicalSequence AnalysisAdd
BLAST
Transmembranei654 – 67421HelicalSequence AnalysisAdd
BLAST
Transmembranei835 – 85521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni531 – 5333Glutamate binding
Regioni704 – 7052Glutamate binding

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234371.
HOVERGENiHBG051839.
InParanoidiP22756.
KOiK05201.
PhylomeDBiP22756.

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.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Glur5-2C (identifier: P22756-1) [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
MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP
60 70 80 90 100
VNVEELAFKF AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL
110 120 130 140 150
ALGVAALFGP SHSSSVSAVQ SICNALEVPH IQTRWKHPSV DSRDLFYINL
160 170 180 190 200
YPDYAAISRA VLDLVLYYNW KTVTVVYEDS TGLIRLQELI KAPSRYNIKI
210 220 230 240 250
KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL KQILFMGMMT
260 270 280 290 300
EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME
310 320 330 340 350
RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR
360 370 380 390 400
HKPCALGPRF MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT
410 420 430 440 450
EKASGEVSKH LYKVWKKIGI WNSNSGLNMT DGNRDRSNNI TDSLANRTLI
460 470 480 490 500
VTTILEEPYV MYRKSDKPLY GNDRFEAYCL DLLKELSNIL GFLYDVKLVP
510 520 530 540 550
DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK VIDFSKPFMT
560 570 580 590 600
LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
610 620 630 640 650
PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI
660 670 680 690 700
VGGIWWFFTL IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV
710 720 730 740 750
RDGSTMTFFK KSKISTYEKM WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL
760 770 780 790 800
LMESTSIEYV TQRNCNLTQI GGLIDSKGYG VGTPIGSPYR DKITIAILQL
810 820 830 840 850
QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI VLAAGLVLSV
860 870 880 890 900
FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL
910 920 930 940
SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA
Length:949
Mass (Da):107,840
Last modified:November 1, 1995 - v3
Checksum:i020660BDD00054E0
GO
Isoform Glur5-2 (identifier: P22756-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     402-416: Missing.
     870-898: Missing.

Show »
Length:905
Mass (Da):102,646
Checksum:iB674CECB3FB60F47
GO
Isoform Glur5-2A (identifier: P22756-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     870-871: KG → HY
     872-949: Missing.

Show »
Length:871
Mass (Da):98,853
Checksum:iCC3EEB35068FDB54
GO
Isoform Glur5-2B (identifier: P22756-4) [UniParc]FASTAAdd to Basket

Also known as: Glur5-1

The sequence of this isoform differs from the canonical sequence as follows:
     870-898: Missing.

Show »
Length:920
Mass (Da):104,388
Checksum:i4609F0CDF337B3D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821K → L in AAA02874. (PubMed:1977421)Curated
Sequence conflicti354 – 3552CA → WR in AAA02874. (PubMed:1977421)Curated
Sequence conflicti477 – 4771A → G in AAA02874. (PubMed:1977421)Curated

RNA editingi

Partially edited.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti636 – 6361Q → R in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei402 – 41615Missing in isoform Glur5-2. CuratedVSP_000129Add
BLAST
Alternative sequencei870 – 89829Missing in isoform Glur5-2B and isoform Glur5-2. CuratedVSP_000130Add
BLAST
Alternative sequencei870 – 8712KG → HY in isoform Glur5-2A. CuratedVSP_000131
Alternative sequencei872 – 94978Missing in isoform Glur5-2A. CuratedVSP_000132Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83560 mRNA. Translation: AAA02873.1.
M83561 mRNA. Translation: AAA02874.1.
Z11712 mRNA. Translation: CAA77775.1.
Z11713 mRNA. Translation: CAA77776.1.
Z11714 mRNA. Translation: CAA77777.1.
PIRiS19808.
RefSeqiNP_001104584.1. NM_001111114.1.
NP_001104587.1. NM_001111117.1.
NP_058937.1. NM_017241.2.
UniGeneiRn.10449.

Genome annotation databases

EnsembliENSRNOT00000042581; ENSRNOP00000050263; ENSRNOG00000001575.
ENSRNOT00000051060; ENSRNOP00000046164; ENSRNOG00000001575.
GeneIDi29559.
KEGGirno:29559.
UCSCiRGD:2732. rat. [P22756-1]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83560 mRNA. Translation: AAA02873.1 .
M83561 mRNA. Translation: AAA02874.1 .
Z11712 mRNA. Translation: CAA77775.1 .
Z11713 mRNA. Translation: CAA77776.1 .
Z11714 mRNA. Translation: CAA77777.1 .
PIRi S19808.
RefSeqi NP_001104584.1. NM_001111114.1.
NP_001104587.1. NM_001111117.1.
NP_058937.1. NM_017241.2.
UniGenei Rn.10449.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TXF X-ray 2.10 A 446-559 [» ]
A 682-821 [» ]
1VSO X-ray 1.85 A 445-559 [» ]
A 682-820 [» ]
1YCJ X-ray 1.95 A/B 445-559 [» ]
2F34 X-ray 1.74 A/B 446-559 [» ]
A/B 682-821 [» ]
2F35 X-ray 1.87 A/B 446-559 [» ]
A/B 682-821 [» ]
2F36 X-ray 2.11 A/B/C/D 446-559 [» ]
A/B/C/D 682-821 [» ]
2OJT X-ray 1.95 A/B 446-559 [» ]
A/B 682-821 [» ]
2PBW X-ray 2.50 A/B 445-559 [» ]
A/B 682-820 [» ]
2QS1 X-ray 1.80 A/B 446-559 [» ]
A/B 682-821 [» ]
2QS2 X-ray 1.80 A/B 446-559 [» ]
A/B 682-821 [» ]
2QS3 X-ray 1.76 A/B 446-559 [» ]
A/B 682-821 [» ]
2QS4 X-ray 1.58 A/B/C/D 446-559 [» ]
A/B/C/D 682-821 [» ]
2WKY X-ray 2.20 A/B 445-559 [» ]
A/B 667-821 [» ]
3C31 X-ray 1.49 A/B 446-559 [» ]
A/B 682-821 [» ]
3C32 X-ray 1.72 A/B 446-559 [» ]
A/B 682-821 [» ]
3C33 X-ray 1.72 A/B 446-559 [» ]
A/B 682-821 [» ]
3C34 X-ray 1.82 A/B 446-559 [» ]
A/B 682-821 [» ]
3C35 X-ray 1.97 A/B 446-559 [» ]
A/B 682-821 [» ]
3C36 X-ray 1.68 A/B 446-559 [» ]
A/B 682-821 [» ]
3GBA X-ray 1.35 A/B/C/D 445-559 [» ]
A/B/C/D 682-820 [» ]
3GBB X-ray 2.10 A/B 445-559 [» ]
A/B 682-820 [» ]
3S2V X-ray 2.50 A/B 445-559 [» ]
A/B 682-820 [» ]
4DLD X-ray 2.00 A/B 445-559 [» ]
A/B 682-820 [» ]
4E0X X-ray 2.00 A/B 682-820 [» ]
ProteinModelPortali P22756.
SMRi P22756. Positions 445-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248193. 4 interactions.
DIPi DIP-29257N.
STRINGi 10116.ENSRNOP00000045594.

Chemistry

BindingDBi P22756.
ChEMBLi CHEMBL2094119.
GuidetoPHARMACOLOGYi 450.

Protein family/group databases

TCDBi 1.A.10.1.5. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P22756.

Proteomic databases

PaxDbi P22756.
PRIDEi P22756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000042581 ; ENSRNOP00000050263 ; ENSRNOG00000001575 .
ENSRNOT00000051060 ; ENSRNOP00000046164 ; ENSRNOG00000001575 .
GeneIDi 29559.
KEGGi rno:29559.
UCSCi RGD:2732. rat. [P22756-1 ]

Organism-specific databases

CTDi 2897.
RGDi 2732. Grik1.

Phylogenomic databases

eggNOGi NOG316680.
GeneTreei ENSGT00760000118920.
HOGENOMi HOG000234371.
HOVERGENi HBG051839.
InParanoidi P22756.
KOi K05201.
PhylomeDBi P22756.

Miscellaneous databases

EvolutionaryTracei P22756.
NextBioi 609606.
PROi P22756.

Gene expression databases

ExpressionAtlasi P22756. baseline and differential.
Genevestigatori P22756.

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. "A glutamate receptor channel with high affinity for domoate and kainate."
    Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B., Seeburg P.H.
    EMBO J. 11:1651-1656(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain.
  2. "Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development."
    Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A., Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.
    Neuron 5:583-595(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway."
    Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J.
    J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLHL17.
  4. "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].
    Tissue: Brain.
  5. "Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate."
    Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S.
    FEBS Lett. 579:1154-1160(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH GLUTAMATE, SUBUNIT.
  6. "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity."
    Mayer M.L.
    Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
  7. "Crystal structures of the kainate receptor GluR5 ligand binding core dimer with novel GluR5-selective antagonists."
    Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.
    J. Neurosci. 26:2852-2861(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302 AND UBP310, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiGRIK1_RAT
AccessioniPrimary (citable) accession number: P22756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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 > CNQX = DNQX > AMPA > dihydrokainate > NMDA.

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