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Protein

Glutamate receptor 4

Gene

Gria4

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 similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei472Glutamate3 Publications1
Binding sitei507Glutamate3 Publications1
Binding sitei727GlutamateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • chemical synaptic transmission Source: RGD
  • modulation of synaptic transmission Source: UniProtKB
  • positive regulation of synaptic transmission, glutamatergic Source: UniProtKB
  • regulation of synapse structure or activity Source: UniProtKB
  • response to fungicide Source: RGD
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.10.1.2. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 4
Short name:
GluR-4
Short name:
GluR4
Alternative name(s):
AMPA-selective glutamate receptor 4
GluR-D
Glutamate receptor ionotropic, AMPA 4
Short name:
GluA4
Gene namesi
Name:Gria4
Synonyms:Glur4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61863. Gria4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 544ExtracellularBy similarityAdd BLAST523
Transmembranei545 – 565HelicalBy similarityAdd BLAST21
Topological domaini566 – 592CytoplasmicBy similarityAdd BLAST27
Intramembranei593 – 608Helical; Pore-formingBy similarityAdd BLAST16
Intramembranei609 – 611By similarity3
Topological domaini612 – 617CytoplasmicBy similarity6
Transmembranei618 – 638HelicalBy similarityAdd BLAST21
Topological domaini639 – 813ExtracellularBy similarityAdd BLAST175
Transmembranei814 – 834Helical; Name=M4By similarityAdd BLAST21
Topological domaini835 – 902CytoplasmicBy similarityAdd BLAST68

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • dendrite Source: UniProtKB
  • ionotropic glutamate receptor complex Source: UniProtKB
  • kainate selective glutamate receptor complex Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
  • synapse Source: UniProtKB
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi407N → Q: No effect on surface expression and channel activity; when associated with Q-414. 1 Publication1
Mutagenesisi414N → Q: No effect on surface expression and channel activity; when associated with Q-407. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3505.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001154021 – 902Glutamate receptor 4Add BLAST882

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi56N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi84 ↔ 331By similarity
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi371N-linked (GlcNAc...)Sequence analysis1
Glycosylationi407N-linked (GlcNAc...)1 Publication1
Glycosylationi414N-linked (GlcNAc...)1 Publication1
Lipidationi611S-palmitoyl cysteineBy similarity1
Disulfide bondi740 ↔ 7951 Publication
Lipidationi837S-palmitoyl cysteineBy similarity1
Modified residuei862Phosphoserine; by PKC/PRKCG1 Publication1

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-611 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-837 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).By similarity
Phosphorylated at Ser-862 by PRKCG; phosphorylation increases plasma membrane-associated GRI4 expression.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiP19493.

PTM databases

iPTMnetiP19493.
PhosphoSitePlusiP19493.
SwissPalmiP19493.
UniCarbKBiP19493.

Expressioni

Tissue specificityi

Detected in cerebellum (at protein level).

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with EPB41L1 via its C-terminus. Isoform 3 interacts with PRKCABP. Found in a complex with GRIA1, GRIA2, GRIA3, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 and PRKCG.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grip1P978793EBI-7761834,EBI-936113
Mapk8P491852EBI-7761834,EBI-7456505

Protein-protein interaction databases

DIPiDIP-41142N.
IntActiP19493. 5 interactors.
MINTiMINT-86166.

Chemistry databases

BindingDBiP19493.

Structurei

Secondary structure

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 33Combined sources9
Helixi38 – 52Combined sources15
Turni57 – 59Combined sources3
Beta strandi61 – 70Combined sources10
Helixi76 – 88Combined sources13
Beta strandi92 – 96Combined sources5
Turni100 – 102Combined sources3
Helixi103 – 112Combined sources10
Beta strandi116 – 119Combined sources4
Beta strandi129 – 133Combined sources5
Helixi139 – 148Combined sources10
Beta strandi153 – 158Combined sources6
Helixi165 – 175Combined sources11
Turni176 – 178Combined sources3
Beta strandi180 – 185Combined sources6
Helixi191 – 204Combined sources14
Beta strandi208 – 212Combined sources5
Helixi215 – 228Combined sources14
Beta strandi236 – 239Combined sources4
Beta strandi241 – 243Combined sources3
Helixi244 – 246Combined sources3
Helixi250 – 255Combined sources6
Beta strandi258 – 263Combined sources6
Helixi270 – 279Combined sources10
Turni284 – 286Combined sources3
Turni288 – 291Combined sources4
Helixi296 – 317Combined sources22
Helixi342 – 350Combined sources9
Beta strandi353 – 356Combined sources4
Beta strandi359 – 363Combined sources5
Beta strandi367 – 369Combined sources3
Beta strandi373 – 380Combined sources8
Beta strandi383 – 391Combined sources9
Turni392 – 394Combined sources3
Beta strandi395 – 398Combined sources4
Beta strandi416 – 421Combined sources6
Turni425 – 427Combined sources3
Beta strandi428 – 430Combined sources3
Helixi434 – 436Combined sources3
Helixi439 – 442Combined sources4
Beta strandi443 – 445Combined sources3
Helixi446 – 458Combined sources13
Beta strandi461 – 466Combined sources6
Turni477 – 479Combined sources3
Helixi484 – 490Combined sources7
Beta strandi495 – 497Combined sources3
Helixi505 – 508Combined sources4
Beta strandi511 – 513Combined sources3
Beta strandi517 – 520Combined sources4
Beta strandi522 – 527Combined sources6
Helixi658 – 662Combined sources5
Beta strandi665 – 670Combined sources6
Beta strandi672 – 675Combined sources4
Helixi676 – 683Combined sources8
Helixi687 – 698Combined sources12
Beta strandi705 – 707Combined sources3
Helixi708 – 717Combined sources10
Turni718 – 720Combined sources3
Beta strandi721 – 727Combined sources7
Helixi728 – 735Combined sources8
Beta strandi742 – 746Combined sources5
Beta strandi752 – 754Combined sources3
Beta strandi757 – 759Combined sources3
Helixi765 – 777Combined sources13
Helixi780 – 789Combined sources10
Turni790 – 792Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EN3X-ray2.43A416-528[»]
A654-795[»]
3EPEX-ray1.85A/B416-528[»]
A/B654-795[»]
3FASX-ray1.40A/B415-528[»]
A/B654-796[»]
3FATX-ray1.90A/B/C415-528[»]
A/B/C654-796[»]
3KEIX-ray1.90A/B416-528[»]
A/B654-795[»]
3KFMX-ray2.20A416-528[»]
A654-795[»]
4GPAX-ray2.25A22-401[»]
5FWXX-ray2.50B/D22-401[»]
ProteinModelPortaliP19493.
SMRiP19493.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19493.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni500 – 502Glutamate binding3
Regioni676 – 677Glutamate 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

HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19493.
KOiK05200.
PhylomeDBiP19493.

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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19493-1) [UniParc]FASTAAdd to basket
Also known as: Flop

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
MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL
60 70 80 90 100
HNTSPNASEA PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK
110 120 130 140 150
RSVHTLTSFC SALHISLITP SFPTEGESQF VLQLRPSLRG ALLSLLDHYE
160 170 180 190 200
WNCFVFLYDT DRGYSILQAI MEKAGQNGWH VSAICVENFN DVSYRQLLEE
210 220 230 240 250
LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA NLGFKDISLE
260 270 280 290 300
RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL
310 320 330 340 350
TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK
360 370 380 390 400
QVRIQGLTGN VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ
410 420 430 440 450
DMPTLGNDTA AIENRTVVVT TIMESPYVMY KKNHEMFEGN DKYEGYCVDL
460 470 480 490 500
ASEIAKHIGI KYKIAIVPDG KYGARDADTK IWNGMVGELV YGKAEIAIAP
510 520 530 540 550
LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL DPLAYEIWMC
560 570 580 590 600
IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW
610 620 630 640 650
FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER
660 670 680 690 700
MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE
710 720 730 740 750
PSVFTRTTAE GVARVRKSKG KFAFLLESTM NEYTEQRKPC DTMKVGGNLD
760 770 780 790 800
SKGYGVATPK GSSLGNAVNL AVLKLNEQGL LDKLKNKWWY DKGECGSGGG
810 820 830 840 850
DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS RAEAKRMKLT
860 870 880 890 900
FSEATRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD

LP
Length:902
Mass (Da):100,758
Last modified:February 1, 1991 - v1
Checksum:i873D1B4C710C4459
GO
Isoform 2 (identifier: P19493-2) [UniParc]FASTAAdd to basket
Also known as: Flip

The sequence of this isoform differs from the canonical sequence as follows:
     765-767: GNA → RTP
     776-780: NEQGL → SEAGV
     797-801: SGGGD → PKDSG

Show »
Length:902
Mass (Da):100,883
Checksum:iEB2AEF26FD237199
GO
Isoform 3 (identifier: P19493-3) [UniParc]FASTAAdd to basket
Also known as: 4C flop

The sequence of this isoform differs from the canonical sequence as follows:
     849-902: LTFSEATRNK...GLAVIASDLP → VAKSAQTFNP...NVYGTESIKI

Show »
Length:884
Mass (Da):99,184
Checksum:i00B47FD9B55E38C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111 – 112SA → RR in AAA41242 (PubMed:1977421).Curated2
Sequence conflicti454I → S in AAA41242 (PubMed:1977421).Curated1
Sequence conflicti734T → I in AAA41242 (PubMed:1977421).Curated1
Sequence conflicti855T → I in AAA41242 (PubMed:1977421).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000123765 – 767GNA → RTP in isoform 2. 2 Publications3
Alternative sequenceiVSP_000124776 – 780NEQGL → SEAGV in isoform 2. 2 Publications5
Alternative sequenceiVSP_000125797 – 801SGGGD → PKDSG in isoform 2. 2 Publications5
Alternative sequenceiVSP_000126849 – 902LTFSE…ASDLP → VAKSAQTFNPTSSQNTHNLA TYREGYNVYGTESIKI in isoform 3. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36421 mRNA. Translation: AAA41246.1.
M85037 mRNA. Translation: AAA41242.1.
M38063 mRNA. Translation: AAA63481.1.
S94371 mRNA. Translation: AAB21763.1.
PIRiA44839.
D40170.
RefSeqiNP_001106655.1. NM_001113184.1.
NP_058959.2. NM_017263.2.
UniGeneiRn.10938.

Genome annotation databases

GeneIDi29629.
KEGGirno:29629.
UCSCiRGD:61863. rat. [P19493-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36421 mRNA. Translation: AAA41246.1.
M85037 mRNA. Translation: AAA41242.1.
M38063 mRNA. Translation: AAA63481.1.
S94371 mRNA. Translation: AAB21763.1.
PIRiA44839.
D40170.
RefSeqiNP_001106655.1. NM_001113184.1.
NP_058959.2. NM_017263.2.
UniGeneiRn.10938.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EN3X-ray2.43A416-528[»]
A654-795[»]
3EPEX-ray1.85A/B416-528[»]
A/B654-795[»]
3FASX-ray1.40A/B415-528[»]
A/B654-796[»]
3FATX-ray1.90A/B/C415-528[»]
A/B/C654-796[»]
3KEIX-ray1.90A/B416-528[»]
A/B654-795[»]
3KFMX-ray2.20A416-528[»]
A654-795[»]
4GPAX-ray2.25A22-401[»]
5FWXX-ray2.50B/D22-401[»]
ProteinModelPortaliP19493.
SMRiP19493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41142N.
IntActiP19493. 5 interactors.
MINTiMINT-86166.

Chemistry databases

BindingDBiP19493.
ChEMBLiCHEMBL3505.

Protein family/group databases

TCDBi1.A.10.1.2. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

iPTMnetiP19493.
PhosphoSitePlusiP19493.
SwissPalmiP19493.
UniCarbKBiP19493.

Proteomic databases

PRIDEiP19493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29629.
KEGGirno:29629.
UCSCiRGD:61863. rat. [P19493-1]

Organism-specific databases

CTDi2893.
RGDi61863. Gria4.

Phylogenomic databases

HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19493.
KOiK05200.
PhylomeDBiP19493.

Miscellaneous databases

EvolutionaryTraceiP19493.
PROiP19493.

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 nameiGRIA4_RAT
AccessioniPrimary (citable) accession number: P19493
Secondary accession number(s): Q64241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 161 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, 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.