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Protein

Glutamate receptor 3

Gene

Gria3

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. 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)DescriptionActionsGraphical viewLength
Binding sitei474Glutamate2 Publications1
Binding sitei509Glutamate2 Publications1
Binding sitei731Glutamate2 Publications1

GO - Molecular functioni

  • AMPA glutamate receptor activity Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • ionotropic glutamate receptor activity Source: RGD
  • PDZ domain binding Source: UniProtKB

GO - Biological processi

  • regulation of receptor recycling Source: UniProtKB
  • response to fungicide Source: RGD
  • response to lithium ion Source: UniProtKB
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi70958. Gria3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 546ExtracellularBy similarityAdd BLAST524
Transmembranei547 – 567HelicalBy similarityAdd BLAST21
Topological domaini568 – 596CytoplasmicBy similarityAdd BLAST29
Intramembranei597 – 612Helical; Pore-formingBy similarityAdd BLAST16
Intramembranei613 – 615By similarity3
Topological domaini616 – 621CytoplasmicBy similarity6
Transmembranei622 – 642HelicalBy similarityAdd BLAST21
Topological domaini643 – 817ExtracellularBy similarityAdd BLAST175
Transmembranei818 – 838Helical; Name=M4By similarityAdd BLAST21
Topological domaini839 – 888CytoplasmicBy similarityAdd BLAST50

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: UniProtKB
  • asymmetric synapse Source: RGD
  • cell junction Source: UniProtKB-KW
  • dendrite Source: RGD
  • dendritic shaft Source: RGD
  • dendritic spine Source: UniProtKB
  • ionotropic glutamate receptor complex Source: UniProtKB
  • neuronal cell body Source: RGD
  • perikaryon Source: RGD
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
  • protein complex Source: UniProtKB
  • synaptic cleft Source: RGD
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001153723 – 888Glutamate receptor 3Add BLAST866

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi85 ↔ 334
Glycosylationi260N-linked (GlcNAc...)1 Publication1
Glycosylationi374N-linked (GlcNAc...)1 Publication1
Glycosylationi409N-linked (GlcNAc...)Sequence analysis1
Glycosylationi416N-linked (GlcNAc...)Sequence analysis1
Lipidationi615S-palmitoyl cysteineBy similarity1
Modified residuei657PhosphoserineBy similarity1
Modified residuei722PhosphoserineBy similarity1
Disulfide bondi744 ↔ 799
Lipidationi841S-palmitoyl cysteineBy similarity1
Modified residuei871PhosphotyrosineBy similarity1
Modified residuei881PhosphotyrosineBy similarity1

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

PaxDbiP19492.
PRIDEiP19492.

PTM databases

iPTMnetiP19492.
PhosphoSitePlusiP19492.
SwissPalmiP19492.
UniCarbKBiP19492.

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. Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grip1P978793EBI-77764,EBI-936113
Pick1Q9EP807EBI-77764,EBI-77728

GO - Molecular functioni

  • PDZ domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi248251. 1 interactor.
DIPiDIP-30954N.
IntActiP19492. 8 interactors.
MINTiMINT-86220.
STRINGi10116.ENSRNOP00000031170.

Chemistry databases

BindingDBiP19492.

Structurei

Secondary structure

1888
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 34Combined sources9
Helixi39 – 53Combined sources15
Turni58 – 60Combined sources3
Beta strandi62 – 71Combined sources10
Helixi77 – 90Combined sources14
Beta strandi95 – 97Combined sources3
Turni101 – 103Combined sources3
Helixi104 – 114Combined sources11
Beta strandi118 – 120Combined sources3
Beta strandi130 – 134Combined sources5
Helixi140 – 149Combined sources10
Beta strandi154 – 159Combined sources6
Helixi166 – 178Combined sources13
Beta strandi181 – 186Combined sources6
Helixi193 – 205Combined sources13
Beta strandi210 – 215Combined sources6
Helixi217 – 229Combined sources13
Beta strandi238 – 241Combined sources4
Helixi246 – 248Combined sources3
Helixi252 – 257Combined sources6
Beta strandi260 – 266Combined sources7
Helixi272 – 281Combined sources10
Turni286 – 288Combined sources3
Beta strandi292 – 295Combined sources4
Helixi299 – 320Combined sources22
Beta strandi327 – 329Combined sources3
Beta strandi336 – 338Combined sources3
Helixi345 – 353Combined sources9
Beta strandi357 – 359Combined sources3
Beta strandi362 – 366Combined sources5
Beta strandi372 – 374Combined sources3
Beta strandi377 – 382Combined sources6
Beta strandi387 – 394Combined sources8
Turni395 – 397Combined sources3
Beta strandi398 – 401Combined sources4
Beta strandi418 – 423Combined sources6
Turni427 – 429Combined sources3
Beta strandi430 – 432Combined sources3
Helixi436 – 438Combined sources3
Helixi441 – 444Combined sources4
Beta strandi445 – 447Combined sources3
Helixi448 – 460Combined sources13
Beta strandi463 – 468Combined sources6
Turni479 – 481Combined sources3
Helixi486 – 492Combined sources7
Beta strandi497 – 499Combined sources3
Helixi507 – 510Combined sources4
Beta strandi513 – 515Combined sources3
Beta strandi519 – 522Combined sources4
Beta strandi524 – 529Combined sources6
Helixi662 – 666Combined sources5
Beta strandi669 – 676Combined sources8
Helixi680 – 687Combined sources8
Helixi691 – 702Combined sources12
Turni704 – 706Combined sources3
Beta strandi708 – 711Combined sources4
Helixi712 – 721Combined sources10
Turni722 – 724Combined sources3
Beta strandi725 – 731Combined sources7
Helixi732 – 739Combined sources8
Beta strandi746 – 750Combined sources5
Beta strandi756 – 758Combined sources3
Beta strandi761 – 763Combined sources3
Helixi769 – 781Combined sources13
Helixi784 – 793Combined sources10
Turni794 – 796Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLNX-ray1.91A416-530[»]
A658-799[»]
3DP4X-ray2.11A416-530[»]
A658-799[»]
3LSWX-ray1.75A417-530[»]
3LSXX-ray2.01A417-530[»]
3M3FX-ray2.50A417-530[»]
A658-799[»]
3M3KX-ray1.79A/C/E417-530[»]
A/C/E658-799[»]
3O21X-ray2.20A/B/C/D23-403[»]
3P3WX-ray4.20A/B/C/D23-403[»]
3RT6X-ray2.84B417-530[»]
B658-799[»]
3RT8X-ray2.43A417-530[»]
A658-799[»]
4F1YX-ray1.79A/C417-530[»]
A/C658-799[»]
4F22X-ray2.06A417-530[»]
A658-799[»]
4F29X-ray1.75A417-530[»]
A658-799[»]
4F2OX-ray1.91A417-530[»]
A658-799[»]
4F2QX-ray2.20A417-530[»]
A658-799[»]
4F31X-ray2.29B/D417-530[»]
B/D658-799[»]
4F39X-ray1.83A417-530[»]
A658-799[»]
4F3BX-ray1.82A417-530[»]
A658-799[»]
4F3GX-ray2.06A417-530[»]
A658-799[»]
5FWYX-ray2.12B/D23-403[»]
5IDEelectron microscopy8.25B/D24-888[»]
5IDFelectron microscopy10.31B/D24-888[»]
ProteinModelPortaliP19492.
SMRiP19492.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19492.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni502 – 504Glutamate binding3
Regioni680 – 681Glutamate binding2

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

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19492.
KOiK05199.
PhylomeDBiP19492.

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 Flop (identifier: P19492-1) [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 GAILSLLSYY
160 170 180 190 200
KWEKFVYLYD TERGFSVLQA IMEAAVQNNW QVTARSVGNI KDVQEFRRII
210 220 230 240 250
EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM LANLGFTDIL
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 ATPKGSALGN AVNLAVLKLN EQGLLDKLKN KWWYDKGECG
810 820 830 840 850
SGGGDSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF CYKSRAESKR
860 870 880
MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
Length:888
Mass (Da):100,373
Last modified:February 1, 1991 - v1
Checksum:i2981616375661703
GO
Isoform Flip (identifier: P19492-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     770-771: NA → TP
     780-780: N → S
     784-784: L → I
     801-805: SGGGD → AKDSG

Show »
Length:888
Mass (Da):100,444
Checksum:iD53A3C20BFB3F620
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti517 – 518KP → NA (PubMed:2168579).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000119770 – 771NA → TP in isoform Flip. Curated2
Alternative sequenceiVSP_000120780N → S in isoform Flip. Curated1
Alternative sequenceiVSP_000121784L → I in isoform Flip. Curated1
Alternative sequenceiVSP_000122801 – 805SGGGD → AKDSG in isoform Flip. Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36420 mRNA. Translation: AAA41245.1.
X54656 mRNA. Translation: CAA38466.1.
M38062 mRNA. Translation: AAA63480.1.
M85036 mRNA. Translation: AAA41241.2.
PIRiC40170.
RefSeqiNP_001106213.1. NM_001112742.1.
NP_116785.2. NM_032990.2.
UniGeneiRn.74049.

Genome annotation databases

GeneIDi29628.
KEGGirno:29628.
UCSCiRGD:70958. rat. [P19492-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36420 mRNA. Translation: AAA41245.1.
X54656 mRNA. Translation: CAA38466.1.
M38062 mRNA. Translation: AAA63480.1.
M85036 mRNA. Translation: AAA41241.2.
PIRiC40170.
RefSeqiNP_001106213.1. NM_001112742.1.
NP_116785.2. NM_032990.2.
UniGeneiRn.74049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLNX-ray1.91A416-530[»]
A658-799[»]
3DP4X-ray2.11A416-530[»]
A658-799[»]
3LSWX-ray1.75A417-530[»]
3LSXX-ray2.01A417-530[»]
3M3FX-ray2.50A417-530[»]
A658-799[»]
3M3KX-ray1.79A/C/E417-530[»]
A/C/E658-799[»]
3O21X-ray2.20A/B/C/D23-403[»]
3P3WX-ray4.20A/B/C/D23-403[»]
3RT6X-ray2.84B417-530[»]
B658-799[»]
3RT8X-ray2.43A417-530[»]
A658-799[»]
4F1YX-ray1.79A/C417-530[»]
A/C658-799[»]
4F22X-ray2.06A417-530[»]
A658-799[»]
4F29X-ray1.75A417-530[»]
A658-799[»]
4F2OX-ray1.91A417-530[»]
A658-799[»]
4F2QX-ray2.20A417-530[»]
A658-799[»]
4F31X-ray2.29B/D417-530[»]
B/D658-799[»]
4F39X-ray1.83A417-530[»]
A658-799[»]
4F3BX-ray1.82A417-530[»]
A658-799[»]
4F3GX-ray2.06A417-530[»]
A658-799[»]
5FWYX-ray2.12B/D23-403[»]
5IDEelectron microscopy8.25B/D24-888[»]
5IDFelectron microscopy10.31B/D24-888[»]
ProteinModelPortaliP19492.
SMRiP19492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248251. 1 interactor.
DIPiDIP-30954N.
IntActiP19492. 8 interactors.
MINTiMINT-86220.
STRINGi10116.ENSRNOP00000031170.

Chemistry databases

BindingDBiP19492.
ChEMBLiCHEMBL3504.

PTM databases

iPTMnetiP19492.
PhosphoSitePlusiP19492.
SwissPalmiP19492.
UniCarbKBiP19492.

Proteomic databases

PaxDbiP19492.
PRIDEiP19492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29628.
KEGGirno:29628.
UCSCiRGD:70958. rat. [P19492-1]

Organism-specific databases

CTDi2892.
RGDi70958. Gria3.

Phylogenomic databases

eggNOGiKOG1054. Eukaryota.
ENOG410XPSH. LUCA.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19492.
KOiK05199.
PhylomeDBiP19492.

Miscellaneous databases

EvolutionaryTraceiP19492.
PROiP19492.

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 nameiGRIA3_RAT
AccessioniPrimary (citable) accession number: P19492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 163 of the entry and version 1 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. 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.