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P19490 (GRIA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Gria1
Synonyms:Glur1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.17

Subunit structure

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). Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Ref.11 Ref.12 Ref.17

Tissue specificity

Detected in cerebellum (at protein level). Ref.11

Domain

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

Post-translational modification

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.

Polymorphism

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

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to amine stimulus

Inferred from expression pattern PubMed 19674091. Source: RGD

cellular response to amino acid stimulus

Inferred from expression pattern PubMed 19913087. Source: RGD

cellular response to dsRNA

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to organic cyclic compound

Inferred from expression pattern PubMed 20025928. Source: RGD

cellular response to peptide hormone stimulus

Inferred from expression pattern PubMed 20237279. Source: RGD

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay PubMed 17409242Ref.17. Source: GOC

long-term memory

Inferred from mutant phenotype PubMed 19547753. Source: RGD

neuronal action potential

Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB

positive regulation of membrane potential

Inferred from mutant phenotype PubMed 20165912. Source: RGD

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB

receptor internalization

Inferred from direct assay PubMed 11100149. Source: UniProtKB

regulation of receptor recycling

Inferred from mutant phenotype PubMed 11348590. Source: UniProtKB

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB

regulation of synaptic transmission

Inferred from direct assay PubMed 11348590. Source: UniProtKB

response to arsenic-containing substance

Inferred from expression pattern PubMed 19761793. Source: RGD

response to cocaine

Inferred from expression pattern PubMed 20600170. Source: RGD

response to drug

Inferred from expression pattern PubMed 19940171. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 20554014. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 19596275. Source: RGD

response to fungicide

Inferred from expression pattern PubMed 19591855. Source: RGD

response to lithium ion

Inferred from expression pattern PubMed 15269270. Source: UniProtKB

response to organic cyclic compound

Inferred from expression pattern PubMed 19940171. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 20554878. Source: RGD

response to toxic substance

Inferred from mutant phenotype PubMed 20165912. Source: RGD

spinal cord development

Inferred from expression pattern PubMed 19446017. Source: RGD

synaptic transmission, glutamatergic

Non-traceable author statement PubMed 15269270. Source: UniProtKB

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from direct assay Ref.17. Source: UniProtKB

asymmetric synapse

Inferred from direct assay PubMed 12077196. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 19321442. Source: RGD

cytosol

Inferred from direct assay PubMed 20165912. Source: RGD

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic shaft

Inferred from direct assay PubMed 11100149. Source: UniProtKB

dendritic spine

Inferred from direct assay PubMed 12077196PubMed 16338934. Source: RGD

early endosome

Inferred from direct assay PubMed 11100149. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

excitatory synapse

Inferred from direct assay PubMed 19730411. Source: BHF-UCL

ionotropic glutamate receptor complex

Traceable author statement PubMed 11836517. Source: UniProtKB

neuromuscular junction

Inferred from direct assay PubMed 19918122. Source: RGD

neuron projection

Inferred from direct assay PubMed 16338934. Source: RGD

neuron spine

Inferred from direct assay PubMed 20083202. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 11100149. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 20165912. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 12077196. Source: RGD

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein complex

Inferred from direct assay PubMed 17329210. Source: RGD

synapse

Inferred from mutant phenotype PubMed 12536214. Source: UniProtKB

   Molecular_functionG-protein alpha-subunit binding

Inferred from physical interaction PubMed 19942860. Source: RGD

G-protein beta-subunit binding

Inferred from direct assay PubMed 19942860. Source: RGD

PDZ domain binding

Inferred from physical interaction PubMed 16634638. Source: RGD

adenylate cyclase binding

Inferred from direct assay PubMed 19942860. Source: RGD

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from direct assay Ref.17. Source: UniProtKB

beta-2 adrenergic receptor binding

Inferred from physical interaction PubMed 19942860. Source: RGD

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 19461580PubMed 21317873. Source: IntAct

ionotropic glutamate receptor activity

Inferred from direct assay PubMed 17409242. Source: RGD

myosin V binding

Inferred from physical interaction PubMed 16338934. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 17194442. Source: RGD

protein homodimerization activity

Traceable author statement PubMed 11348590. Source: UniProtKB

protein kinase A binding

Inferred from direct assay PubMed 19942860. Source: RGD

protein kinase binding

Inferred from physical interaction PubMed 17329210. Source: RGD

small GTPase binding

Inferred from physical interaction PubMed 17194442. Source: RGD

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Flop (identifier: P19490-1)

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.
Isoform Flip (identifier: P19490-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 907889Glutamate receptor 1
PRO_0000011531

Regions

Topological domain19 – 536518Extracellular By similarity
Transmembrane537 – 55721Helical; By similarity
Topological domain558 – 58427Cytoplasmic By similarity
Intramembrane585 – 60016Helical; Pore-forming; By similarity
Intramembrane601 – 6033 By similarity
Topological domain604 – 6096Cytoplasmic By similarity
Transmembrane610 – 63021Helical; By similarity
Topological domain631 – 805175Extracellular By similarity
Transmembrane806 – 82621Helical; Name=M4; By similarity
Topological domain827 – 90781Cytoplasmic By similarity
Region492 – 4943Glutamate binding By similarity
Region668 – 6692Glutamate binding By similarity
Motif904 – 9074PDZ-binding

Sites

Binding site4641Glutamate By similarity
Binding site4991Glutamate By similarity
Binding site7191Glutamate By similarity

Amino acid modifications

Modified residue6451Phosphoserine Ref.7
Modified residue7101Phosphoserine; by PKC
Modified residue8491Phosphoserine; by PKC, PKA and CAMK2 Ref.9
Modified residue8631Phosphoserine; by PKC and PKA Ref.9
Lipidation6031S-palmitoyl cysteine By similarity
Lipidation8291S-palmitoyl cysteine By similarity
Glycosylation631N-linked (GlcNAc...)
Glycosylation2491N-linked (GlcNAc...) Ref.20
Glycosylation2571N-linked (GlcNAc...) Ref.20
Glycosylation3631N-linked (GlcNAc...) Ref.20
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 323 Ref.20
Disulfide bond732 ↔ 787 By similarity

Natural variations

Alternative sequence7581N → G in isoform Flip.
VSP_000097
Alternative sequence7681N → S in isoform Flip.
VSP_000098
Alternative sequence7721L → V in isoform Flip.
VSP_000099
Alternative sequence7781N → S in isoform Flip.
VSP_000100
Alternative sequence790 – 7934GGGD → KDSG in isoform Flip.
VSP_000101
Natural variant7101S → T. Ref.6 Ref.8

Experimental info

Mutagenesis6451S → A: No effect on phosphorylation by CaMK2. Ref.9
Mutagenesis8491S → A: Abolishes phosphorylation by CaMK2. Ref.9
Mutagenesis9051T → A: Loss of interaction with DLG1. Ref.11
Mutagenesis9071L → A: Loss of interaction with DLG1. Ref.11
Sequence conflict671S → T in AAA63479. Ref.6
Sequence conflict2481A → R in AAA63479. Ref.6
Sequence conflict6981R → L in AAA63479. Ref.6

Secondary structure

.............................................................. 907
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Flop [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 2D4CFA7CCD532838

FASTA907101,579
        10         20         30         40         50         60 
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 

        70         80         90        100        110        120 
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 

       130        140        150        160        170        180 
FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT 

       190        200        210        220        230        240 
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL 

       250        260        270        280        290        300 
NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 

       310        320        330        340        350        360 
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 

       370        380        390        400        410        420 
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 

       430        440        450        460        470        480 
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 

       490        500        510        520        530        540 
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 

       550        560        570        580        590        600 
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 

       610        620        630        640        650        660 
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 

       670        680        690        700        710        720 
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 

       730        740        750        760        770        780 
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW 

       790        800        810        820        830        840 
WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 

       850        860        870        880        890        900 
GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM 


PLGATGL 

« Hide

Isoform Flip [UniParc].

Checksum: 5FA3091114C0BA6B
Show »

FASTA907101,555

References

[1]"Cloning by functional expression of a member of the glutamate receptor family."
Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F.
Nature 342:643-648(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
Tissue: Forebrain.
[2]Hartley M.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"A family of AMPA-selective glutamate receptors."
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H.
Science 249:556-560(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
Tissue: Brain.
[4]Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893.
[5]"Molecular cloning and functional expression of glutamate receptor subunit genes."
Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F.
Science 249:1033-1037(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
[6]"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 FLIP), VARIANT THR-710.
Tissue: Brain.
[7]"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors."
Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A., Soderling T.R.
Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-645.
[8]"Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696."
Nakazawa K., Tadakuma T., Nokihara K., Ito M.
Neurosci. Res. 24:75-86(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-710, PHOSPHORYLATION.
[9]"Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II."
Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.
J. Biol. Chem. 272:32528-32533(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-849 AND SER-863, MUTAGENESIS OF SER-645 AND SER-849.
[10]"SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit."
Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.
J. Biol. Chem. 273:19518-19524(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1.
[11]"Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif."
Cai C., Coleman S.K., Niemi K., Keinaenen K.
J. Biol. Chem. 277:31484-31490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-905 AND LEU-907.
[12]"Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics."
Bedoukian M.A., Weeks A.M., Partin K.M.
J. Biol. Chem. 281:23908-23921(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
[13]"SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN1.
[14]"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.
[15]"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.
[16]Erratum
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
Nat. Neurosci. 12:808-808(2009)
[17]"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: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[18]"Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating."
Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W., Nicoll R.A.
Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNIH2 AND CACNG2.
[19]"Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide."
von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M., Goldman A., Keinanen K.
FEBS J. 273:5219-5229(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH DLG1, INTERACTION WITH DLG1.
[20]"Crystal structure of the glutamate receptor GluA1 N-terminal domain."
Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.
Biochem. J. 438:255-263(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT, GLYCOSYLATION AT ASN-249; ASN-257 AND ASN-363, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17184 mRNA. Translation: CAA35050.1.
M36418 mRNA. Translation: AAA41243.2.
M38060 mRNA. Translation: AAA63479.1.
PIRA40170.
ACRTK1. S07059.
RefSeqNP_113796.1. NM_031608.1.
UniGeneRn.29971.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AWWX-ray2.21C890-907[»]
3SAJX-ray2.50A/B/C/D22-392[»]
ProteinModelPortalP19490.
SMRP19490. Positions 406-520, 645-788.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248399. 5 interactions.
DIPDIP-30929N.
IntActP19490. 17 interactions.
MINTMINT-726538.

Chemistry

BindingDBP19490.
ChEMBLCHEMBL2093871.

Protein family/group databases

TCDB1.A.10.1.1. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSiteP19490.

Proteomic databases

PRIDEP19490.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID50592.
KEGGrno:50592.
UCSCRGD:621531. rat. [P19490-1]

Organism-specific databases

CTD2890.
RGD621531. Gria1.

Phylogenomic databases

HOVERGENHBG051839.
KOK05197.
PhylomeDBP19490.

Gene expression databases

GenevestigatorP19490.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP19490.
NextBio610434.

Entry information

Entry nameGRIA1_RAT
AccessionPrimary (citable) accession number: P19490
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references