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UniProtKB - P19490 (GRIA1_RAT)

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Protein

Glutamate receptor 1

Gene

Gria1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. 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.2 Publications

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei464GlutamateBy similarity1
Binding sitei499GlutamateBy similarity1
Binding sitei719GlutamateBy similarity1

GO - Molecular functioni

  • adenylate cyclase binding Source: RGD
  • AMPA glutamate receptor activity Source: UniProtKB
  • amyloid-beta binding Source: ARUK-UCL
  • beta-2 adrenergic receptor binding Source: ARUK-UCL
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • G-protein alpha-subunit binding Source: RGD
  • G-protein beta-subunit binding Source: RGD
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor activity Source: RGD
  • myosin V binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein C-terminus binding Source: ARUK-UCL
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: RGD
  • protein kinase binding Source: RGD
  • scaffold protein binding Source: SynGO-UCL
  • small GTPase binding Source: RGD
Complete GO annotation...

GO - Biological processi

  • cellular response to amine stimulus Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • long-term memory Source: RGD
  • modulation of synaptic transmission Source: UniProtKB
  • neuronal action potential Source: UniProtKB
  • positive regulation of membrane potential Source: RGD
  • positive regulation of synaptic transmission Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • regulation of receptor recycling Source: UniProtKB
  • regulation of synaptic plasticity Source: UniProtKB
  • response to arsenic-containing substance Source: RGD
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to electrical stimulus Source: RGD
  • response to estradiol Source: RGD
  • response to fungicide Source: RGD
  • response to lithium ion Source: UniProtKB
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to toxic substance Source: RGD
  • spinal cord development Source: RGD
  • synaptic transmission, glutamatergic Source: UniProtKB
Complete GO annotation...

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Protein family/group databases

TCDBi1.A.10.1.1. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 1
Short name:
GluR-1
Alternative name(s):
AMPA-selective glutamate receptor 1
GluR-A
GluR-K1
Glutamate receptor ionotropic, AMPA 1
Short name:
GluA1
Gene namesi
Name:Gria1
Synonyms:Glur1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621531. Gria1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 536ExtracellularBy similarityAdd BLAST518
Transmembranei537 – 557HelicalBy similarityAdd BLAST21
Topological domaini558 – 584CytoplasmicBy similarityAdd BLAST27
Intramembranei585 – 600Helical; Pore-formingBy similarityAdd BLAST16
Intramembranei601 – 603By similarity3
Topological domaini604 – 609CytoplasmicBy similarity6
Transmembranei610 – 630HelicalBy similarityAdd BLAST21
Topological domaini631 – 805ExtracellularBy similarityAdd BLAST175
Transmembranei806 – 826Helical; Name=M4By similarityAdd BLAST21
Topological domaini827 – 907CytoplasmicBy similarityAdd BLAST81

GO - Cellular componenti

  • AMPA glutamate receptor complex Source: UniProtKB
  • asymmetric synapse Source: RGD
  • cell junction Source: UniProtKB-KW
  • cell surface Source: RGD
  • cytosol Source: RGD
  • dendrite Source: ARUK-UCL
  • dendritic shaft Source: UniProtKB
  • dendritic spine Source: ARUK-UCL
  • early endosome Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • excitatory synapse Source: BHF-UCL
  • ionotropic glutamate receptor complex Source: UniProtKB
  • neuromuscular junction Source: RGD
  • neuronal cell body Source: UniProtKB
  • neuron projection Source: RGD
  • neuron spine Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • protein complex Source: RGD
  • synapse Source: SynGO-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi645S → A: No effect on phosphorylation by CaMK2. 1 Publication1
Mutagenesisi849S → A: Abolishes phosphorylation by CaMK2. 1 Publication1
Mutagenesisi855R → A: Decreases binding efficiency to PRKG2. 1
Mutagenesisi855R → E: Abolishes binding to PRKG2. 1 Publication1
Mutagenesisi863S → A: Decreases synaptic insertion during chemical-induced long term potentiation. 1 Publication1
Mutagenesisi905T → A: Loss of interaction with DLG1. 1 Publication1
Mutagenesisi907L → A: Loss of interaction with DLG1. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3753.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001153119 – 907Glutamate receptor 1Add BLAST889

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi63N-linked (GlcNAc...) asparagine1
Disulfide bondi75 ↔ 3231 Publication
Glycosylationi249N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi257N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi363N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi603S-palmitoyl cysteineBy similarity1
Modified residuei645Phosphoserine1 Publication1
Modified residuei710Phosphoserine; by PKC1 Publication1
Disulfide bondi732 ↔ 787By similarity
Lipidationi829S-palmitoyl cysteineBy similarity1
Modified residuei849Phosphoserine; by PKC, PKA and CAMK22 Publications1
Modified residuei863Phosphoserine; by PKC, PKA and PKG/PRKG22 Publications1

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity).By similarity
Phosphorylated at Ser-645 (PubMed:7877986). Phosphorylated at Ser-710 by PKC (PubMed:8848293). Phosphorylated at Ser-849 by PKC, PKA and CAMK2 (PubMed:9405465). Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (PubMed:9405465, PubMed:18031684).4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiP19490.

PTM databases

iPTMnetiP19490.
PhosphoSitePlusiP19490.
SwissPalmiP19490.

Expressioni

Tissue specificityi

Detected in cerebellum (at protein level).1 Publication

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with DLG1 via its C-terminus. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with HIP1, RASGRF2, SYNDIG1 and LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain) (PubMed:12070168, PubMed:16630835, PubMed:16793768, PubMed:17069616, PubMed:18817736, PubMed:19234459, PubMed:19265014, PubMed:20805473, PubMed:21639859, PubMed:9677374). Interacts with PRKG2 (PubMed:18031684).11 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • adenylate cyclase binding Source: RGD
  • beta-2 adrenergic receptor binding Source: ARUK-UCL
  • G-protein alpha-subunit binding Source: RGD
  • G-protein beta-subunit binding Source: RGD
  • identical protein binding Source: IntAct
  • myosin V binding Source: RGD
  • PDZ domain binding Source: RGD
  • protein C-terminus binding Source: ARUK-UCL
  • protein domain specific binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: RGD
  • protein kinase binding Source: RGD
  • scaffold protein binding Source: SynGO-UCL
  • small GTPase binding Source: RGD
Complete GO annotation...

Protein-protein interaction databases

BioGridi248399. 10 interactors.
DIPiDIP-30929N.
ELMiP19490.
IntActiP19490. 18 interactors.
MINTiMINT-726538.

Chemistry databases

BindingDBiP19490.

Structurei

Secondary structure

1907
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 32Combined sources10
Beta strandi34 – 36Combined sources3
Helixi37 – 46Combined sources10
Beta strandi51 – 61Combined sources11
Helixi67 – 79Combined sources13
Beta strandi85 – 87Combined sources3
Helixi91 – 104Combined sources14
Beta strandi108 – 110Combined sources3
Beta strandi122 – 124Combined sources3
Helixi130 – 139Combined sources10
Beta strandi144 – 149Combined sources6
Helixi156 – 168Combined sources13
Beta strandi171 – 176Combined sources6
Helixi177 – 179Combined sources3
Helixi183 – 187Combined sources5
Turni188 – 191Combined sources4
Beta strandi196 – 203Combined sources8
Helixi206 – 208Combined sources3
Helixi209 – 218Combined sources10
Beta strandi225 – 233Combined sources9
Helixi235 – 237Combined sources3
Helixi240 – 245Combined sources6
Beta strandi250 – 254Combined sources5
Helixi261 – 276Combined sources16
Helixi288 – 309Combined sources22
Helixi334 – 342Combined sources9
Beta strandi346 – 348Combined sources3
Beta strandi351 – 353Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi366 – 372Combined sources7
Beta strandi375 – 383Combined sources9
Turni384 – 386Combined sources3
Beta strandi387 – 390Combined sources4
Beta strandi905 – 907Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AWWX-ray2.21C890-907[»]
2G2LX-ray2.35C/D890-907[»]
3SAJX-ray2.50A/B/C/D22-392[»]
ProteinModelPortaliP19490.
SMRiP19490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19490.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni492 – 494Glutamate bindingBy similarity3
Regioni668 – 669Glutamate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi904 – 907PDZ-binding4

Domaini

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

Sequence similaritiesi

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA1 subfamily. [View classification]Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG051839.
InParanoidiP19490.
KOiK05197.
PhylomeDBiP19490.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
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: P19490-1) [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
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT 
        60         70         80         90        100
EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF 
       110        120        130        140        150
CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ EALISIIDHY KWQTFVYIYD 
       160        170        180        190        200
ADRGLSVLQR VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV 
       210        220        230        240        250
VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV 
       260        270        280        290        300
TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 
       310        320        330        340        350
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT 
       360        370        380        390        400
GNVQFNEKGR RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD 
       410        420        430        440        450
NSSVQNRTYI VTTILEDPYV MLKKNANQFE GNDRYEGYCV ELAAEIAKHV 
       460        470        480        490        500
GYSYRLEIVS DGKYGARDPD TKAWNGMVGE LVYGRADVAV APLTITLVRE 
       510        520        530        540        550
EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV 
       560        570        580        590        600
SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 
       610        620        630        640        650
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA 
       660        670        680        690        700
EDLAKQTEIA YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT 
       710        720        730        740        750
EEGMIRVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT 
       760        770        780        790        800
PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKDKTSA 
       810        820        830        840        850
LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI 
       860        870        880        890        900
NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM 

PLGATGL
Length:907
Mass (Da):101,579
Last modified:May 16, 2006 - v2
Checksum:i2D4CFA7CCD532838
GO
Isoform Flip (identifier: P19490-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     758-758: N → G
     768-768: N → S
     772-772: L → V
     778-778: N → S
     790-793: GGGD → KDSG

Show »
Length:907
Mass (Da):101,555
Checksum:i5FA3091114C0BA6B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti67S → T in AAA63479 (PubMed:1699275).Curated1
Sequence conflicti248A → R in AAA63479 (PubMed:1699275).Curated1
Sequence conflicti698R → L in AAA63479 (PubMed:1699275).Curated1

Polymorphismi

Both variants Ser-710 and Thr-710 are phosphorylated at this position.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti710S → T2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000097758N → G in isoform Flip. 1 Publication1
Alternative sequenceiVSP_000098768N → S in isoform Flip. 1 Publication1
Alternative sequenceiVSP_000099772L → V in isoform Flip. 1 Publication1
Alternative sequenceiVSP_000100778N → S in isoform Flip. 1 Publication1
Alternative sequenceiVSP_000101790 – 793GGGD → KDSG in isoform Flip. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17184 mRNA. Translation: CAA35050.1.
M36418 mRNA. Translation: AAA41243.2.
M38060 mRNA. Translation: AAA63479.1.
PIRiA40170.
S07059. ACRTK1.
RefSeqiNP_113796.1. NM_031608.1. [P19490-1]
UniGeneiRn.29971.

Genome annotation databases

GeneIDi50592.
KEGGirno:50592.
UCSCiRGD:621531. rat. [P19490-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGRIA1_RAT
AccessioniPrimary (citable) accession number: P19490
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 16, 2006
Last modified: August 30, 2017
This is version 176 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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