Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P23818 (GRIA1_MOUSE)

Entry version 193 (23 Feb 2022)
Sequence version 1 (01 Nov 1991)
Previous versions | rss
Add a publicationFeedback
Protein

Glutamate receptor 1

Gene

Gria1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei464GlutamateBy similarity1
Binding sitei499GlutamateBy similarity1
Binding sitei719GlutamateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-204005, COPII-mediated vesicle transport
R-MMU-399710, Activation of AMPA receptors
R-MMU-416993, Trafficking of GluR2-containing AMPA receptors
R-MMU-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-MMU-5694530, Cargo concentration in the ER
R-MMU-8849932, Synaptic adhesion-like molecules

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gria1
Synonyms:Glur1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:95808, Gria1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000020524

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 536ExtracellularBy similarityAdd BLAST518
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei537 – 557HelicalBy similarityAdd BLAST21
Topological domaini558 – 584CytoplasmicBy similarityAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>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

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi905 – 907TGL → AGA: Almost abolishes interaction with SHANK3. 1 Publication3

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3502

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001153019 – 907Glutamate receptor 1Add BLAST889

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi63N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi75 ↔ 323By similarity
Glycosylationi249N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi257N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi363N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi603S-palmitoyl cysteine1 Publication1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei645PhosphoserineBy similarity1
Modified residuei710PhosphoserineBy similarity1
Disulfide bondi732 ↔ 787By similarity
Lipidationi829S-palmitoyl cysteine1 Publication1
Modified residuei849PhosphoserineBy similarity1
Modified residuei863Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which 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.1 Publication
Phosphorylated at Ser-645. Phosphorylated at Ser-710 by PKC. Phosphorylated at Ser-849 by PKC, PKA and CAMK2. Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (By similarity). Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation (PubMed:23676497).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P23818

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P23818

PRoteomics IDEntifications database

More...PRIDEi		P23818

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		271017

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2341, 4 N-Linked glycans (3 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P23818, 6 sites, 4 N-linked glycans (3 sites)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P23818

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P23818

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P23818

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the outer plexiform layer of the retina of the eye (at protein level) (PubMed:28334377). Expressed in the forebrain and hippocampus (at protein level) (PubMed:31651360).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000020524, Expressed in dentate gyrus of hippocampal formation and 203 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P23818, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P23818, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits (By similarity). Tetramers may be formed by the dimerization of dimers (By similarity).

Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity).

Interacts with HIP1 and RASGRF2 (PubMed:12839988, PubMed:16407208).

Interacts with SYNDIG1 and GRIA2 (PubMed:20152115).

Interacts with DLG1 (via C-terminus).

Interacts with LRFN1.

Interacts with PRKG2.

Interacts with CNIH2 and CACNG2.

Interacts with CACNG5.

Interacts (via C-terminus) with PDLIM4 (via LIM domain); this interaction as well as the interaction of PDLIM4 with alpha-actinin is required for their colocalization in early endosomes.

Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity).

Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (PubMed:23524343).

Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain) (PubMed:16606358).

Interacts with CACNG3; associates GRIA1 with the adapter protein complex 4 (AP-4) to target GRIA1 to the somatodendritic compartment of neurons (PubMed:18341993).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		200058, 21 interactors

Database of interacting proteins

More...DIPi		DIP-31970N

Protein interaction database and analysis system

More...IntActi		P23818, 11 interactors

Molecular INTeraction database

More...MINTi		P23818

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000044494

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P23818

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P23818, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P23818

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni492 – 494Glutamate bindingBy similarity3
Regioni668 – 669Glutamate bindingBy similarity2
Regioni857 – 881DisorderedSequence analysisAdd BLAST25

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi904 – 907PDZ-binding4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1054, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157342

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P23818

Database for complete collections of gene phylogenies

More...PhylomeDBi		P23818

TreeFam database of animal gene trees

More...TreeFami		TF315232

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001828, ANF_lig-bd_rcpt
IPR019594, Glu/Gly-bd
IPR001508, Iono_rcpt_met
IPR001320, Iontro_rcpt
IPR028082, Peripla_BP_I

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01094, ANF_receptor, 1 hit
PF00060, Lig_chan, 1 hit
PF10613, Lig_chan-Glu_bd, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00177, NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00918, Lig_chan-Glu_bd, 1 hit
SM00079, PBPe, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53822, SSF53822, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P23818-1 [UniParc]FASTAAdd to basket
« 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 RTSDARDHTR 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
PKGSALRGPV NLAVLKLSEQ GVLDKLKSKW WYDKGECGSK DSGSKDKTSA 
       810        820        830        840        850
LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI 
       860        870        880        890        900
NEAIRTSTLP RNSGAGASGG SGSGENGRVV SQDFPKSMQS IPCMSHSSGM 

PLGATGL
Length:907
Mass (Da):101,569
Last modified:November 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF0FF7031DADD7CEB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q7TNB5Q7TNB5_MOUSE
Glutamate receptor
Gria1
907Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F6YNQ1F6YNQ1_MOUSE
Glutamate receptor
Gria1
838Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X57497 mRNA Translation: CAA40734.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS48800.1

Protein sequence database of the Protein Information Resource

More...PIRi		S12874

NCBI Reference Sequences

More...RefSeqi		NP_001106796.1, NM_001113325.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000036315; ENSMUSP00000044494; ENSMUSG00000020524

Database of genes from NCBI RefSeq genomes

More...GeneIDi		14799

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:14799

UCSC genome browser

More...UCSCi		uc007izs.3, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57497 mRNA Translation: CAA40734.1
CCDSiCCDS48800.1
PIRiS12874
RefSeqiNP_001106796.1, NM_001113325.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
7LDDelectron microscopy3.40A/C1-907[»]
7LDEelectron microscopy3.90A/C1-907[»]
SMRiP23818
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi200058, 21 interactors
DIPiDIP-31970N
IntActiP23818, 11 interactors
MINTiP23818
STRINGi10090.ENSMUSP00000044494

Chemistry databases

BindingDBiP23818
ChEMBLiCHEMBL3502

PTM databases

GlyConnecti2341, 4 N-Linked glycans (3 sites)
GlyGeniP23818, 6 sites, 4 N-linked glycans (3 sites)
iPTMnetiP23818
PhosphoSitePlusiP23818
SwissPalmiP23818

Proteomic databases

MaxQBiP23818
PaxDbiP23818
PRIDEiP23818
ProteomicsDBi271017

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P23818, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...Antibodypediai		28276, 1030 antibodies from 46 providers

The DNASU plasmid repository

More...DNASUi		14799

Genome annotation databases

EnsembliENSMUST00000036315; ENSMUSP00000044494; ENSMUSG00000020524
GeneIDi14799
KEGGimmu:14799
UCSCiuc007izs.3, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2890
MGIiMGI:95808, Gria1
VEuPathDBiHostDB:ENSMUSG00000020524

Phylogenomic databases

eggNOGiKOG1054, Eukaryota
GeneTreeiENSGT00940000157342
InParanoidiP23818
PhylomeDBiP23818
TreeFamiTF315232

Enzyme and pathway databases

ReactomeiR-MMU-204005, COPII-mediated vesicle transport
R-MMU-399710, Activation of AMPA receptors
R-MMU-416993, Trafficking of GluR2-containing AMPA receptors
R-MMU-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-MMU-5694530, Cargo concentration in the ER
R-MMU-8849932, Synaptic adhesion-like molecules

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		14799, 0 hits in 65 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Gria1, mouse

Protein Ontology

More...PROi		PR:P23818
RNActiP23818, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000020524, Expressed in dentate gyrus of hippocampal formation and 203 other tissues
ExpressionAtlasiP23818, baseline and differential
GenevisibleiP23818, MM

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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGRIA1_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23818
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 23, 2022
This is version 193 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again