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Q9Z2W9

- GRIA3_MOUSE

UniProt

Q9Z2W9 - GRIA3_MOUSE

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Protein

Glutamate receptor 3

Gene

Gria3

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei474 – 4741Glutamate1 Publication
Binding sitei509 – 5091Glutamate1 Publication
Binding sitei731 – 7311Glutamate1 Publication

GO - Molecular functioni

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
  2. extracellular-glutamate-gated ion channel activity Source: RefGenome

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: RefGenome
  2. ion transmembrane transport Source: RefGenome
  3. synaptic transmission, glutamatergic Source: RefGenome
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 3
Short name:
GluR-3
Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name:
GluA3
Gene namesi
Name:Gria3
Synonyms:Glur3, Kiaa4184
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:95810. Gria3.

Subcellular locationi

Cell membrane By similarity; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane By similarity; Multi-pass membrane protein By similarity
Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression.By similarity

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: RefGenome
  4. membrane Source: MGI
  5. postsynaptic membrane Source: MGI
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 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 888866Glutamate receptor 3PRO_0000042230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi85 ↔ 334By similarity
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Lipidationi615 – 6151S-palmitoyl cysteineBy similarity
Disulfide bondi744 ↔ 7991 Publication
Lipidationi841 – 8411S-palmitoyl cysteine1 Publication
Modified residuei871 – 8711Phosphotyrosine1 Publication
Modified residuei881 – 8811Phosphotyrosine1 Publication

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-615 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-841 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9Z2W9.
PaxDbiQ9Z2W9.
PRIDEiQ9Z2W9.

PTM databases

PhosphoSiteiQ9Z2W9.

Expressioni

Gene expression databases

BgeeiQ9Z2W9.
CleanExiMM_GRIA3.
ExpressionAtlasiQ9Z2W9. baseline and differential.
GenevestigatoriQ9Z2W9.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity). Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207340. 2 interactions.
IntActiQ9Z2W9. 4 interactions.
MINTiMINT-4131411.

Structurei

Secondary structure

1
888
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi662 – 6665
Beta strandi669 – 6768
Helixi680 – 6878
Helixi691 – 70212
Beta strandi708 – 7114
Helixi712 – 72110
Turni722 – 7243
Beta strandi725 – 7317
Helixi732 – 7398
Beta strandi746 – 7505
Beta strandi756 – 7583
Beta strandi761 – 7633
Helixi769 – 78113
Helixi784 – 79310
Turni794 – 7963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LSWX-ray1.75A658-799[»]
3LSXX-ray2.01A658-799[»]
ProteinModelPortaliQ9Z2W9.
SMRiQ9Z2W9. Positions 26-843.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z2W9.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 546524ExtracellularBy similarityAdd
BLAST
Topological domaini568 – 59629CytoplasmicBy similarityAdd
BLAST
Topological domaini616 – 6216CytoplasmicBy similarity
Topological domaini643 – 817175ExtracellularBy similarityAdd
BLAST
Topological domaini839 – 88850CytoplasmicBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei597 – 61216Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei613 – 6153By similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei547 – 56721HelicalBy similarityAdd
BLAST
Transmembranei622 – 64221HelicalBy similarityAdd
BLAST
Transmembranei818 – 83821Helical; Name=M4By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni502 – 5043Glutamate binding
Regioni680 – 6812Glutamate binding

Domaini

The M4 transmembrane segment mediates tetramerization and is required for cell surface expression.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiQ9Z2W9.
KOiK05199.
OrthoDBiEOG7C2R0J.
TreeFamiTF315232.

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 (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. Align

Isoform Flip (identifier: Q9Z2W9-1) [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
MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ
60 70 80 90 100
LYNTNQNTTE KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD
110 120 130 140 150
QMSMNTLTSF CGALHTSFVT PSFPTDADVQ FVIQMRPALK GAILSLLGYY
160 170 180 190 200
KWEKFVYLYD TERGFSILQA IMEAAVQNNW QVTARSVGNI KDIQEFRRII
210 220 230 240 250
EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM LANLGFTDIV
260 270 280 290 300
LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT
310 320 330 340 350
SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER
360 370 380 390 400
ALKMVQVQGM TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV
410 420 430 440 450
PFSDQQISND SSSSENRTIV VTTILESPYV MYKKNHEQLE GNERYEGYCV
460 470 480 490 500
DLAYEIAKHV RIKYKLSIVG DGKYGARDPE TKIWNGMVGE LVYGRADIAV
510 520 530 540 550
APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
560 570 580 590 600
MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF
610 620 630 640 650
NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL
660 670 680 690 700
TVERMVSPIE SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM
710 720 730 740 750
KSAEPSVFTK TTADGVARVR KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG
760 770 780 790 800
GNLDSKGYGV ATPKGSALRT PVNLAVLKLS EQGILDKLKN KWWYDKGECG
810 820 830 840 850
AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF CYKSRAESKR
860 870 880
MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
Length:888
Mass (Da):100,527
Last modified:July 27, 2011 - v2
Checksum:i9F68C5D80E81DC02
GO
Isoform Flop (identifier: Q9Z2W9-2)

Sequence is not available
Length:
Mass (Da):

Sequence cautioni

The sequence BAD90527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001T → I in BAD90527. 1 PublicationCurated
Sequence conflicti769 – 7691R → G in BAA37124. 1 PublicationCurated
Sequence conflicti769 – 7691R → G in BAE06153. 1 PublicationCurated
Sequence conflicti769 – 7691R → G in AAL90768. (PubMed:11471062)Curated
Sequence conflicti769 – 7691R → G in AAL90769. (PubMed:11471062)Curated
Sequence conflicti769 – 7691R → G in BAD90527. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB022342 mRNA. Translation: BAA37124.1.
AB079072 mRNA. Translation: BAE06153.1.
AF483494 mRNA. Translation: AAL90768.1.
AF483495 mRNA. Translation: AAL90769.1.
AK220530 mRNA. Translation: BAD90527.1. Different initiation.
CH466570 Genomic DNA. Translation: EDL29035.1.
AL672290, AL672232 Genomic DNA. Translation: CAQ11290.1.
AL672232, AL672290 Genomic DNA. Translation: CAQ12028.1.
BC129855 mRNA. Translation: AAI29856.1.
CCDSiCCDS30097.1. [Q9Z2W9-1]
RefSeqiNP_001268858.1. NM_001281929.1.
NP_001277380.1. NM_001290451.1.
NP_058582.3. NM_016886.4.
XP_006541583.1. XM_006541520.1. [Q9Z2W9-1]
UniGeneiMm.327681.

Genome annotation databases

EnsembliENSMUST00000076349; ENSMUSP00000075687; ENSMUSG00000001986. [Q9Z2W9-1]
GeneIDi53623.
KEGGimmu:53623.
UCSCiuc009tal.2. mouse. [Q9Z2W9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB022342 mRNA. Translation: BAA37124.1 .
AB079072 mRNA. Translation: BAE06153.1 .
AF483494 mRNA. Translation: AAL90768.1 .
AF483495 mRNA. Translation: AAL90769.1 .
AK220530 mRNA. Translation: BAD90527.1 . Different initiation.
CH466570 Genomic DNA. Translation: EDL29035.1 .
AL672290 , AL672232 Genomic DNA. Translation: CAQ11290.1 .
AL672232 , AL672290 Genomic DNA. Translation: CAQ12028.1 .
BC129855 mRNA. Translation: AAI29856.1 .
CCDSi CCDS30097.1. [Q9Z2W9-1 ]
RefSeqi NP_001268858.1. NM_001281929.1.
NP_001277380.1. NM_001290451.1.
NP_058582.3. NM_016886.4.
XP_006541583.1. XM_006541520.1. [Q9Z2W9-1 ]
UniGenei Mm.327681.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LSW X-ray 1.75 A 658-799 [» ]
3LSX X-ray 2.01 A 658-799 [» ]
ProteinModelPortali Q9Z2W9.
SMRi Q9Z2W9. Positions 26-843.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207340. 2 interactions.
IntActi Q9Z2W9. 4 interactions.
MINTi MINT-4131411.

Chemistry

BindingDBi Q9Z2W9.
ChEMBLi CHEMBL2096617.
GuidetoPHARMACOLOGYi 446.

PTM databases

PhosphoSitei Q9Z2W9.

Proteomic databases

MaxQBi Q9Z2W9.
PaxDbi Q9Z2W9.
PRIDEi Q9Z2W9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000076349 ; ENSMUSP00000075687 ; ENSMUSG00000001986 . [Q9Z2W9-1 ]
GeneIDi 53623.
KEGGi mmu:53623.
UCSCi uc009tal.2. mouse. [Q9Z2W9-1 ]

Organism-specific databases

CTDi 2892.
MGIi MGI:95810. Gria3.
Rougei Search...

Phylogenomic databases

eggNOGi NOG316680.
GeneTreei ENSGT00760000118920.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
InParanoidi Q9Z2W9.
KOi K05199.
OrthoDBi EOG7C2R0J.
TreeFami TF315232.

Miscellaneous databases

EvolutionaryTracei Q9Z2W9.
NextBioi 310361.
PROi Q9Z2W9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z2W9.
CleanExi MM_GRIA3.
ExpressionAtlasi Q9Z2W9. baseline and differential.
Genevestigatori Q9Z2W9.

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

« Hide 'large scale' publications
  1. "Mouse glutamate receptor channel alpha3 subunit."
    Sakimura K., Yamazaki M.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "Expression of AMPA-selective glutamate receptors in mouse spinal cord."
    Doi Y., Nishizawa M., Minami T., Ito S.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ddY.
    Tissue: Spinal cord.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ILS and ISS.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites."
    Hayashi T., Rumbaugh G., Huganir R.L.
    Neuron 47:709-723(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-841.
  9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-871 AND TYR-881, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "Piracetam defines a new binding site for allosteric modulators of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA) receptors."
    Ahmed A.H., Oswald R.E.
    J. Med. Chem. 53:2197-2203(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 658-799 IN COMPLEX WITH GLUTAMATE, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiGRIA3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2W9
Secondary accession number(s): A2VDF4, Q5DTJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 116 of the entry and version 2 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 AMPA (quisqualate) > glutamate > kainate.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3