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P19493

- GRIA4_RAT

UniProt

P19493 - GRIA4_RAT

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Protein

Glutamate receptor 4

Gene

Gria4

Organism
Rattus norvegicus (Rat)
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 sitei472 – 4721Glutamate3 Publications
Binding sitei507 – 5071Glutamate3 Publications
Binding sitei727 – 7271GlutamateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: GOC
  2. ion transmembrane transport Source: GOC
  3. positive regulation of synaptic transmission, glutamatergic Source: UniProtKB
  4. regulation of synapse structure and activity Source: UniProtKB
  5. regulation of synaptic transmission Source: UniProtKB
  6. response to fungicide Source: RGD
  7. synaptic transmission 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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi61863. Gria4.

Subcellular locationi

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

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: UniProtKB
  4. ionotropic glutamate receptor complex Source: UniProtKB
  5. kainate selective glutamate receptor complex Source: UniProtKB
  6. neuronal cell body Source: UniProtKB
  7. postsynaptic density Source: UniProtKB
  8. postsynaptic membrane Source: RefGenome
  9. synapse Source: UniProtKB
  10. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi407 – 4071N → Q: No effect on surface expression and channel activity; when associated with Q-414. 1 Publication
Mutagenesisi414 – 4141N → Q: No effect on surface expression and channel activity; when associated with Q-407. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 902882Glutamate receptor 4PRO_0000011540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi84 ↔ 331By similarity
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)1 Publication
Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
Lipidationi611 – 6111S-palmitoyl cysteineBy similarity
Disulfide bondi740 ↔ 7951 Publication
Lipidationi837 – 8371S-palmitoyl cysteineBy similarity
Modified residuei862 – 8621Phosphoserine; by PKC/PRKCG1 Publication

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

PaxDbiP19493.
PRIDEiP19493.

PTM databases

PhosphoSiteiP19493.

Expressioni

Tissue specificityi

Detected in cerebellum (at protein level).

Gene expression databases

GenevestigatoriP19493.

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 interactions.
MINTiMINT-86166.

Structurei

Secondary structure

1
902
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 339
Helixi38 – 5215
Turni57 – 593
Beta strandi61 – 7010
Helixi76 – 8813
Beta strandi92 – 965
Turni100 – 1023
Helixi103 – 11210
Beta strandi116 – 1194
Beta strandi129 – 1335
Helixi139 – 14810
Beta strandi153 – 1586
Helixi165 – 17511
Turni176 – 1783
Beta strandi180 – 1856
Helixi191 – 20414
Beta strandi208 – 2125
Helixi215 – 22814
Beta strandi236 – 2394
Beta strandi241 – 2433
Helixi244 – 2463
Helixi250 – 2556
Beta strandi258 – 2636
Helixi270 – 27910
Turni284 – 2863
Turni288 – 2914
Helixi296 – 31722
Helixi342 – 3509
Beta strandi353 – 3564
Beta strandi359 – 3635
Beta strandi373 – 3808
Beta strandi383 – 3919
Turni392 – 3943
Beta strandi395 – 3984
Beta strandi416 – 4216
Turni425 – 4273
Beta strandi428 – 4303
Helixi434 – 4363
Helixi439 – 4424
Beta strandi443 – 4453
Helixi446 – 45813
Beta strandi461 – 4666
Turni477 – 4793
Helixi484 – 4907
Beta strandi495 – 4973
Helixi505 – 5084
Beta strandi511 – 5133
Beta strandi517 – 5204
Beta strandi522 – 5276
Helixi658 – 6625
Beta strandi665 – 6706
Beta strandi672 – 6754
Helixi676 – 6838
Helixi687 – 69812
Beta strandi705 – 7073
Helixi708 – 71710
Turni718 – 7203
Beta strandi721 – 7277
Helixi728 – 7358
Beta strandi742 – 7465
Beta strandi752 – 7543
Beta strandi757 – 7593
Helixi765 – 77713
Helixi780 – 78910
Turni790 – 7923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP19493.
SMRiP19493. Positions 413-528, 653-796.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19493.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 544523ExtracellularBy similarityAdd
BLAST
Topological domaini566 – 59227CytoplasmicBy similarityAdd
BLAST
Topological domaini612 – 6176CytoplasmicBy similarity
Topological domaini639 – 813175ExtracellularBy similarityAdd
BLAST
Topological domaini835 – 90268CytoplasmicBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei593 – 60816Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei609 – 6113By similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei545 – 56521HelicalBy similarityAdd
BLAST
Transmembranei618 – 63821HelicalBy similarityAdd
BLAST
Transmembranei814 – 83421Helical; Name=M4By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 5023Glutamate binding
Regioni676 – 6772Glutamate 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.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP19493.
KOiK05200.
PhylomeDBiP19493.

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 (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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1122SA → RR in AAA41242. (PubMed:1977421)Curated
Sequence conflicti454 – 4541I → S in AAA41242. (PubMed:1977421)Curated
Sequence conflicti734 – 7341T → I in AAA41242. (PubMed:1977421)Curated
Sequence conflicti855 – 8551T → I in AAA41242. (PubMed:1977421)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei765 – 7673GNA → RTP in isoform 2. 2 PublicationsVSP_000123
Alternative sequencei776 – 7805NEQGL → SEAGV in isoform 2. 2 PublicationsVSP_000124
Alternative sequencei797 – 8015SGGGD → PKDSG in isoform 2. 2 PublicationsVSP_000125
Alternative sequencei849 – 90254LTFSE…ASDLP → VAKSAQTFNPTSSQNTHNLA TYREGYNVYGTESIKI in isoform 3. 1 PublicationVSP_000126Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M36421 mRNA. Translation: AAA41246.1 .
M85037 mRNA. Translation: AAA41242.1 .
M38063 mRNA. Translation: AAA63481.1 .
S94371 mRNA. Translation: AAB21763.1 .
PIRi A44839.
D40170.
RefSeqi NP_001106655.1. NM_001113184.1.
NP_058959.2. NM_017263.2.
UniGenei Rn.10938.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EN3 X-ray 2.43 A 416-528 [» ]
A 654-795 [» ]
3EPE X-ray 1.85 A/B 416-528 [» ]
A/B 654-795 [» ]
3FAS X-ray 1.40 A/B 415-528 [» ]
A/B 654-796 [» ]
3FAT X-ray 1.90 A/B/C 415-528 [» ]
A/B/C 654-796 [» ]
3KEI X-ray 1.90 A/B 416-528 [» ]
A/B 654-795 [» ]
3KFM X-ray 2.20 A 416-528 [» ]
A 654-795 [» ]
4GPA X-ray 2.25 A 22-401 [» ]
ProteinModelPortali P19493.
SMRi P19493. Positions 413-528, 653-796.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41142N.
IntActi P19493. 5 interactions.
MINTi MINT-86166.

Chemistry

BindingDBi P19493.
ChEMBLi CHEMBL2096669.
GuidetoPHARMACOLOGYi 447.

Protein family/group databases

TCDBi 1.A.10.1.2. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P19493.

Proteomic databases

PaxDbi P19493.
PRIDEi P19493.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29629.
KEGGi rno:29629.
UCSCi RGD:61863. rat. [P19493-1 ]

Organism-specific databases

CTDi 2893.
RGDi 61863. Gria4.

Phylogenomic databases

eggNOGi NOG316680.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
InParanoidi P19493.
KOi K05200.
PhylomeDBi P19493.

Miscellaneous databases

EvolutionaryTracei P19493.
NextBioi 609852.

Gene expression databases

Genevestigatori P19493.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
  3. "Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS."
    Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.
    Science 249:1580-1585(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Molecular cloning and development analysis of a new glutamate receptor subunit isoform in cerebellum."
    Gallo V., Upson L.M., Hayes W.P., Vyklicky L. Jr., Winters C.A., Buonanno A.
    J. Neurosci. 12:1010-1023(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Strain: Sprague-Dawley.
    Tissue: Brain.
  5. "Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain."
    Pasternack A., Coleman S.K., Fethiere J., Madden D.R., LeCaer J.P., Rossier J., Pasternack M., Keinaenen K.
    J. Neurochem. 84:1184-1192(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-407 AND ASN-414, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF ASN-407 AND ASN-414.
  6. "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKCABP (ISOFORM 3).
  7. "Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation."
    Correia S.S., Duarte C.B., Faro C.J., Pires E.V., Carvalho A.L.
    J. Biol. Chem. 278:6307-6313(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-862, INTERACTION WITH PRKCG, SUBCELLULAR LOCATION.
  8. "Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein."
    Coleman S.K., Cai C., Mottershead D.G., Haapalahti J.-P., Keinaenen K.
    J. Neurosci. 23:798-806(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPB41L1.
  9. "AMPA receptor subunit-specific regulation by a distinct family of type II TARPs."
    Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.
    Neuron 59:986-996(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACNG5.
  10. "Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
    Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
    Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACNG5.
  11. "Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors."
    Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.
    Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Correlating AMPA receptor activation and cleft closure across subunits: crystal structures of the GluR4 ligand-binding domain in complex with full and partial agonists."
    Gill A., Birdsey-Benson A., Jones B.L., Henderson L.P., Madden D.R.
    Biochemistry 47:13831-13841(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE AND DIHYDROKAINIC ACID, FUNCTION, SUBUNIT.
  13. "Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4."
    Kasper C., Frydenvang K., Naur P., Gajhede M., Pickering D.S., Kastrup J.S.
    FEBS Lett. 582:4089-4094(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 415-796 IN COMPLEX WITH GLUTAMATE, AMPA BINDING, DISULFIDE BOND.
  14. "Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors."
    Birdsey-Benson A., Gill A., Henderson L.P., Madden D.R.
    J. Neurosci. 30:1463-1470(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 416-795 IN COMPLEX WITH GLUTAMATE AND DIHYDROKAINIC ACID, FUNCTION.

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: October 29, 2014
This is version 142 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

External Data

Dasty 3