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Entry version 52 (17 Jun 2020)
Sequence version 1 (11 Jul 2012)
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Protein

Cyclic GMP-AMP synthase

Gene

CGAS

Organism
Sus scrofa (Pig)
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

Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:23722159). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:23722159). Acts as a key cytosolic DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Binds cytosolic DNA directly, leading to activation and synthesis of cGAMP, a second messenger that binds to and activates TMEM173/STING, thereby triggering type-I interferon production. Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes. Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm. Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol. Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA. Also detects the presence of DNA from bacteria. cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote TMEM173/STING activation and convey immune response to connecting cells. cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but TMEM173/STING-dependent manner. In addition to antiviral activity, also involved in the response to cellular stresses, such as senescence, DNA damage or genome instability. Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via TMEM173/STING and promote cellular senescence. Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability. Micronuclei, which as frequently found in cancer cells, consist of chromatin surrounded by its own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to cGAMP synthesis and subsequent activation of TMEM173/STING and type-I interferon production. Acts as a suppressor of DNA repair in response to DNA damage: translocates to the nucleus following dephosphorylation at Tyr-190 and inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The enzyme activity is strongly increased by double-stranded DNA, but not by single-stranded DNA or RNA (PubMed:23722159). Acetylation at Lys-359, Lys-369 and Lys-389 inhibits the cyclic GMP-AMP synthase activity (By similarity). The enzyme activity is impaired by the cleavage by CASP1 (By similarity).By similarity1 Publication

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 sitei186GTP1 Publication1
Binding sitei188ATP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi200Magnesium; catalytic1 Publication1
Metal bindingi202Magnesium; catalytic1 Publication1
Metal bindingi294Magnesium; catalytic1 Publication1
Binding sitei294GTP1 Publication1
Binding sitei358ATP1 Publication1
Metal bindingi365Zinc; via tele nitrogen1 Publication1
Metal bindingi371Zinc1 Publication1
Metal bindingi372Zinc1 Publication1
Metal bindingi379Zinc1 Publication1
Binding sitei389ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi351 – 358GTP1 Publication8
Nucleotide bindingi410 – 414ATP1 Publication5

<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

GO - Biological processi

<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 functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processAntiviral defense, DNA damage, DNA repair, Immunity, Innate immunity
LigandATP-binding, GTP-binding, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

<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:
Cyclic GMP-AMP synthaseBy similarity (EC:2.7.7.861 Publication)
Short name:
cGAMP synthaseBy similarity
Short name:
cGASBy similarity
Alternative name(s):
2'3'-cGAMP synthaseBy similarity
Mab-21 domain-containing protein 1By similarity
<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:CGASBy similarity
Synonyms:MB21D1By similarity
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<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
  • UP000008227 <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 1

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:86614 CGAS

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<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>Mutagenesisi200E → Q: Abolishes enzyme activity and stimulation of interferon production; when associated with N-202. 1 Publication1
Mutagenesisi202D → N: Abolishes enzyme activity and stimulation of interferon production; when associated with Q-200. 1 Publication1

<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 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_00004230631 – 495Cyclic GMP-AMP synthaseAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei7N6-acetyllysineBy similarity1
Modified residuei190PhosphotyrosineBy similarity1
Modified residuei2615-glutamyl polyglutamateBy similarity1
Modified residuei359N6-acetyllysineBy similarity1
Modified residuei369N6-acetyllysineBy similarity1
Modified residuei389N6-acetyllysineBy similarity1

<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

Polyglutamylated by TTLL6 at Glu-261, leading to impair DNA-binding activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6.By similarity
Cleaved by CASP1 upon DNA virus infection; the cleavage impairs cGAMP production. Also cleaved by the pyroptotic CASP4 and CASP5 during non-canonical inflammasome activation; they don't cut at the same sites than CASP1.By similarity
Phosphorylation at Tyr-190 by BLK promotes cytosolic retention. Translocates into the nucleus following dephosphorylation at Tyr-190.By similarity
Acetylation at Lys-359, Lys-369 and Lys-389 inhibits the cyclic GMP-AMP synthase activity. Deacetylated upon cytosolic DNA challenge such as viral infections.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
I3LM39

PeptideAtlas

More...
PeptideAtlasi
I3LM39

PRoteomics IDEntifications database

More...
PRIDEi
I3LM39

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSSSCG00000021383 Expressed in lung and 5 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
I3LM39 baseline and differential

<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

Monomer in the absence of DNA. Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes binding to two DNA molecules (By similarity).

Interacts with PQBP1 (via WW domain).

Interacts with TRIM14; this interaction stabilizes CGAS and promotes type I interferon production.

Interacts with ZCCHC3; promoting sensing of dsDNA by CGAS.

Interacts with PARP1; interaction takes place in the nucleus and prevents the formation of the PARP1-TIMELESS complex (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000025159

<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

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
I3LM39

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>Regioni1 – 134DNA-bindingBy similarityAdd BLAST134
Regioni57 – 68Required for association with the cell membraneBy similarityAdd BLAST12
Regioni103 – 134Required for activation upon DNA viral infectionBy similarityAdd BLAST32
Regioni147 – 190DNA-binding1 PublicationAdd BLAST44
Regioni359 – 382DNA-binding1 PublicationAdd BLAST24

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>Motifi268 – 278Nuclear localization signalBy similarityAdd BLAST11

<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 N-terminal part (1-160) binds unspecifically dsDNA and expand the binding and moving range of CGAS on dsDNA. Enhances the enzyme activity and activation of innate immune signaling upon cytosolic recognition of dsDNA. When the N-terminal part (1-160) is missing the protein bound to dsDNA homodimerizes.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 mab-21 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IE27 Eukaryota
ENOG410XTKD LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00980000198551

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_040428_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
I3LM39

KEGG Orthology (KO)

More...
KOi
K17834

Identification of Orthologs from Complete Genome Data

More...
OMAi
VKCCRKE

Database of Orthologous Groups

More...
OrthoDBi
759341at2759

TreeFam database of animal gene trees

More...
TreeFami
TF331255

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024810 Mab-21_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03281 Mab-21, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01265 Mab-21, 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>Sequencei

<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.

I3LM39-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAARRGKSTR TASEVGAAGP RASARSVNGA PTVPEAARPG ARRNGPSRAS
60 70 80 90 100
GCRREKSGPD PREKPQVRTR TARAEDQAEG PSAPSERVEP PSAQGASLLR
110 120 130 140 150
AGSCRAREAR SARELRPQAG ATELAAPARM EAPPGAWKLQ TVLEKVRLSR
160 170 180 190 200
HEISEAAEVV NWVVEHLLRR LQGGESEFKG VALLRTGSYY ERVKISAPNE
210 220 230 240 250
FDVMFKLEVP RIQLEEYCNS GAHYFVKFKR NPGGNPLEQF LEKEILSASK
260 270 280 290 300
MLSKFRKIIK EEIKNIEGVT VERKRRGSPA VTLLISKPKE ISVDIILALE
310 320 330 340 350
SKSSWPASTQ KGLPISQWLG AKVKNNLKRQ PFYLVPKHAK EGSGFQEETW
360 370 380 390 400
RLSFSHIEKD ILKNHGQSKT CCEIDGVKCC RKECLKLMKY LLEQLKKKFG
410 420 430 440 450
NRRELAKFCS YHVKTAFFHV CTQDPHDNQW HLKNLECCFD NCVAYFLQCL
460 470 480 490
KTEQLANYFI PGVNLFSRDL IDKPSKEFLS KQIEYERNNG FPVFW
Length:495
Mass (Da):55,809
Last modified:July 11, 2012 - 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:i13E76296D97E176B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
FP102323 Genomic DNA No translation available.

NCBI Reference Sequences

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RefSeqi
XP_013840602.1, XM_013985148.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00000030573; ENSSSCP00000025159; ENSSSCG00000021383
ENSSSCT00015028332; ENSSSCP00015011100; ENSSSCG00015021453
ENSSSCT00025037600; ENSSSCP00025015781; ENSSSCG00025027757
ENSSSCT00030086223; ENSSSCP00030039757; ENSSSCG00030061695
ENSSSCT00035063373; ENSSSCP00035025648; ENSSSCG00035047597
ENSSSCT00040088529; ENSSSCP00040038910; ENSSSCG00040064832
ENSSSCT00045053754; ENSSSCP00045037382; ENSSSCG00045031514
ENSSSCT00050013192; ENSSSCP00050005463; ENSSSCG00050009802
ENSSSCT00055053600; ENSSSCP00055042758; ENSSSCG00055027117
ENSSSCT00060037939; ENSSSCP00060016133; ENSSSCG00060028039
ENSSSCT00065057000; ENSSSCP00065024791; ENSSSCG00065041662

Database of genes from NCBI RefSeq genomes

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GeneIDi
100516408

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:100516408

<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
FP102323 Genomic DNA No translation available.
RefSeqiXP_013840602.1, XM_013985148.1

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
4JLXX-ray2.00A135-495[»]
4JLZX-ray2.27A/B135-495[»]
4KB6X-ray3.08A135-495[»]
SMRiI3LM39
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000025159

Proteomic databases

PaxDbiI3LM39
PeptideAtlasiI3LM39
PRIDEiI3LM39

Genome annotation databases

EnsembliENSSSCT00000030573; ENSSSCP00000025159; ENSSSCG00000021383
ENSSSCT00015028332; ENSSSCP00015011100; ENSSSCG00015021453
ENSSSCT00025037600; ENSSSCP00025015781; ENSSSCG00025027757
ENSSSCT00030086223; ENSSSCP00030039757; ENSSSCG00030061695
ENSSSCT00035063373; ENSSSCP00035025648; ENSSSCG00035047597
ENSSSCT00040088529; ENSSSCP00040038910; ENSSSCG00040064832
ENSSSCT00045053754; ENSSSCP00045037382; ENSSSCG00045031514
ENSSSCT00050013192; ENSSSCP00050005463; ENSSSCG00050009802
ENSSSCT00055053600; ENSSSCP00055042758; ENSSSCG00055027117
ENSSSCT00060037939; ENSSSCP00060016133; ENSSSCG00060028039
ENSSSCT00065057000; ENSSSCP00065024791; ENSSSCG00065041662
GeneIDi100516408
KEGGissc:100516408

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
115004
VGNCiVGNC:86614 CGAS

Phylogenomic databases

eggNOGiENOG410IE27 Eukaryota
ENOG410XTKD LUCA
GeneTreeiENSGT00980000198551
HOGENOMiCLU_040428_2_0_1
InParanoidiI3LM39
KOiK17834
OMAiVKCCRKE
OrthoDBi759341at2759
TreeFamiTF331255

Gene expression databases

BgeeiENSSSCG00000021383 Expressed in lung and 5 other tissues
ExpressionAtlasiI3LM39 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR024810 Mab-21_dom
PfamiView protein in Pfam
PF03281 Mab-21, 1 hit
SMARTiView protein in SMART
SM01265 Mab-21, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiCGAS_PIG
<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: I3LM39
<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: July 24, 2013
Last sequence update: July 11, 2012
Last modified: June 17, 2020
This is version 52 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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