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Cyclic GMP-AMP synthase (cGAMP synthase) (cGAS) (m-cGAS) (EC 2.7.7.86) (2'3'-cGAMP synthase) (Mab-21 domain-containing protein 1)

 CGAS_MOUSE              Reviewed;         507 AA.
Q8C6L5; Q3ULW3;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Cyclic GMP-AMP synthase {ECO:0000303|PubMed:23258413};
Short=cGAMP synthase {ECO:0000303|PubMed:23258413};
Short=cGAS {ECO:0000303|PubMed:23258413};
Short=m-cGAS {ECO:0000303|PubMed:23258413};
EC=2.7.7.86 {ECO:0000269|PubMed:23647843};
AltName: Full=2'3'-cGAMP synthase {ECO:0000303|PubMed:23258413};
AltName: Full=Mab-21 domain-containing protein 1;
Name=Mb21d1 {ECO:0000312|MGI:MGI:2442261};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF GLU-211 AND ASP-213.
PubMed=23258413; DOI=10.1126/science.1232458;
Sun L., Wu J., Du F., Chen X., Chen Z.J.;
"Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the
type I interferon pathway.";
Science 339:786-791(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland, and Ovary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=23722158; DOI=10.1038/nature12306;
Ablasser A., Goldeck M., Cavlar T., Deimling T., Witte G., Rohl I.,
Hopfner K.P., Ludwig J., Hornung V.;
"cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger
that activates STING.";
Nature 498:380-384(2013).
[7]
FUNCTION.
PubMed=24077100; DOI=10.1038/nature12640;
Ablasser A., Schmid-Burgk J.L., Hemmerling I., Horvath G.L.,
Schmidt T., Latz E., Hornung V.;
"Cell intrinsic immunity spreads to bystander cells via the
intercellular transfer of cGAMP.";
Nature 503:530-534(2013).
[8]
FUNCTION.
PubMed=23929945; DOI=10.1126/science.1240933;
Gao D., Wu J., Wu Y.T., Du F., Aroh C., Yan N., Sun L., Chen Z.J.;
"Cyclic GMP-AMP synthase is an innate immune sensor of HIV and other
retroviruses.";
Science 341:903-906(2013).
[9]
FUNCTION, AND MUTAGENESIS OF GLY-198 AND SER-199.
PubMed=26229117; DOI=10.1126/science.aab3632;
Bridgeman A., Maelfait J., Davenne T., Partridge T., Peng Y.,
Mayer A., Dong T., Kaever V., Borrow P., Rehwinkel J.;
"Viruses transfer the antiviral second messenger cGAMP between
cells.";
Science 349:1228-1232(2015).
[10]
GLUTAMYLATION AT GLU-272, GLUTAMYLATION AT GLU-302, AND MUTAGENESIS OF
GLU-272 AND GLU-302.
PubMed=26829768; DOI=10.1038/ni.3356;
Xia P., Ye B., Wang S., Zhu X., Du Y., Xiong Z., Tian Y., Fan Z.;
"Glutamylation of the DNA sensor cGAS regulates its binding and
synthase activity in antiviral immunity.";
Nat. Immunol. 17:369-378(2016).
[11]
FUNCTION, DOMAIN, MONOMER, AND DNA-BINDING.
PubMed=28214358; DOI=10.1002/1873-3468.12598;
Lee A., Park E.B., Lee J., Choi B.S., Kang S.J.;
"The N terminus of cGAS de-oligomerizes the cGAS:DNA complex and lifts
the DNA size restriction of core-cGAS activity.";
FEBS Lett. 591:954-961(2017).
[12]
FUNCTION, DOMAIN, CLEAVAGE, AND ENZYME REGULATION.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS
to regulate responses to DNA virus infection.";
Immunity 46:393-404(2017).
[13]
FUNCTION, DNA-BINDING, AND DOMAIN.
PubMed=28363908; DOI=10.4049/jimmunol.1601909;
Tao J., Zhang X.W., Jin J., Du X.X., Lian T., Yang J., Zhou X.,
Jiang Z., Su X.D.;
"Nonspecific DNA Binding of cGAS N Terminus Promotes cGAS
Activation.";
J. Immunol. 198:3627-3636(2017).
[14]
FUNCTION.
PubMed=28738408; DOI=10.1038/nature23449;
Mackenzie K.J., Carroll P., Martin C.A., Murina O., Fluteau A.,
Simpson D.J., Olova N., Sutcliffe H., Rainger J.K., Leitch A.,
Osborn R.T., Wheeler A.P., Nowotny M., Gilbert N., Chandra T.,
Reijns M.A.M., Jackson A.P.;
"cGAS surveillance of micronuclei links genome instability to innate
immunity.";
Nature 0:0-0(2017).
[15]
FUNCTION.
PubMed=28759028; DOI=10.1038/ncb3586;
Glueck S., Guey B., Gulen M.F., Wolter K., Kang T.W., Schmacke N.A.,
Bridgeman A., Rehwinkel J., Zender L., Ablasser A.;
"Innate immune sensing of cytosolic chromatin fragments through cGAS
promotes senescence.";
Nat. Cell Biol. 0:0-0(2017).
[16]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 147-507 IN COMPLEXES WITH
DNA; GMP; GTP; ATP; CYCLIC GMP-AMP; MAGNESIUM AND ZINC IONS, FUNCTION,
COFACTOR, CATALYTIC ACTIVITY, AND DNA-BINDING.
PubMed=23647843; DOI=10.1016/j.cell.2013.04.046;
Gao P., Ascano M., Wu Y., Barchet W., Gaffney B.L., Zillinger T.,
Serganov A.A., Liu Y., Jones R.A., Hartmann G., Tuschl T., Patel D.J.;
"Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced
by DNA-activated cyclic GMP-AMP synthase.";
Cell 153:1094-1107(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 142-507 IN COMPLEX WITH
ZINC.
PubMed=24332030; DOI=10.1016/j.immuni.2013.10.019;
Li X., Shu C., Yi G., Chaton C.T., Shelton C.L., Diao J., Zuo X.,
Kao C.C., Herr A.B., Li P.;
"Cyclic GMP-AMP synthase is activated by double-stranded DNA-induced
oligomerization.";
Immunity 39:1019-1031(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 147-507 IN COMPLEX WITH
ZINC, AND SUBUNIT.
PubMed=24462292; DOI=10.1016/j.celrep.2014.01.003;
Zhang X., Wu J., Du F., Xu H., Sun L., Chen Z., Brautigam C.A.,
Zhang X., Chen Z.J.;
"The cytosolic DNA sensor cGAS forms an oligomeric complex with DNA
and undergoes switch-like conformational changes in the activation
loop.";
Cell Rep. 6:421-430(2014).
-!- FUNCTION: Nucleotidyltransferase that catalyzes the formation of
cyclic GMP-AMP (cGAMP) from ATP and GTP (PubMed:23258413,
PubMed:23647843, PubMed:23722158, PubMed:26829768,
PubMed:28214358). 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:23258413, PubMed:23647843,
PubMed:23722158, PubMed:26829768, PubMed:28214358). 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 (PubMed:23722158, PubMed:28363908, PubMed:28314590).
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
(PubMed:23722158, PubMed:28363908, PubMed:28314590). Has antiviral
activity by sensing the presence of dsDNA from DNA viruses in the
cytoplasm (PubMed:23258413, PubMed:23647843, PubMed:23722158).
Also acts as an innate immune sensor of infection by retroviruses
by detecting the presence of reverse-transcribed DNA in the
cytosol (PubMed:23929945). 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 (By similarity). Also detects the presence of DNA
from bacteria (By similarity). 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 (PubMed:24077100). 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
(PubMed:26229117). In addition to antiviral activity, also
involved in the response to cellular stresses, such as senescence,
DNA damage or genome instability (PubMed:28738408,
PubMed:28759028). 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
(PubMed:28759028). Also involved in the inflammatory response to
genome instability and double-stranded DNA breaks: acts by
localizing to micronuclei arising from genome instability
(PubMed:28738408). 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, MB21D1/cGAS binds self-DNA
exposed to the cytosol, leading to cGAMP synthesis and subsequent
activation of TMEM173/STING and type-I interferon production
(PubMed:28738408). {ECO:0000250|UniProtKB:Q8N884,
ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:23722158, ECO:0000269|PubMed:23929945,
ECO:0000269|PubMed:24077100, ECO:0000269|PubMed:26229117,
ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:28214358,
ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:28363908,
ECO:0000269|PubMed:28738408, ECO:0000269|PubMed:28759028}.
-!- CATALYTIC ACTIVITY: ATP + GTP = 2 diphosphate + cyclic G-P(2'-
5')A-P(3'-5'). {ECO:0000269|PubMed:23647843}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:23647843};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:23647843};
Note=Binds 1 Mg(2+) per subunit. Is also active with Mn(2+).
{ECO:0000269|PubMed:23647843};
-!- ENZYME REGULATION: Nucleotidyltransferase activity is stimulated
by double-stranded DNA but not RNA (By similarity). The enzyme
activity is impaired by the cleavage by CASP1 (PubMed:28314590).
{ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:28314590}.
-!- SUBUNIT: Monomer in the absence of DNA and when bound to double-
stranded DNA (dsDNA) (PubMed:28214358). Interacts with PQBP1 (via
WW domain) (By similarity). {ECO:0000250|UniProtKB:Q8N884,
ECO:0000269|PubMed:28214358}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:23258413}.
-!- DOMAIN: The N-terminal part (1-146) binds unspecifically dsDNA and
expand the binding and moving range of MB21D1 on dsDNA. Enhances
the enzyme activity and activation of innate immune signaling upon
cytosolic recognition of dsDNA (PubMed:28363908, PubMed:28214358,
PubMed:28314590). When the N-terminal part (1-146) is missing the
protein bound to dsDNA homodimerizes (PubMed:28214358).
{ECO:0000269|PubMed:28214358, ECO:0000269|PubMed:28314590,
ECO:0000269|PubMed:28363908}.
-!- PTM: Polyglutamylated by TTLL6 at Glu-272, leading to impair DNA-
binding activity. Monoglutamylated at Glu-302 by TTLL4, leading to
impair the nucleotidyltransferase activity. Deglutamylated by
AGBL5/CCP5 and AGBL6/CCP6. {ECO:0000269|PubMed:26829768}.
-!- PTM: Cleaved by CASP1 upon DNA virus infection; the cleavage
impairs cGAMP production (PubMed:28314590). Also cleaved by the
pyroptotic CASP4 during non-canonical inflammasome activation;
does not cut at the same sites than CASP1 (PubMed:28314590).
{ECO:0000269|PubMed:28314590}.
-!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
-!- CAUTION: Was reported to homodimerize in presence of double-
stranded DNA (dsDNA) (PubMed:24332030). However, this result was
based on a structure lacking the N-terminal part (1-146), which
caused homodimerization in presence of dsDNA (PubMed:28214358).
{ECO:0000269|PubMed:24332030}.
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EMBL; KC294567; AGB51854.1; -; mRNA.
EMBL; AK054330; BAC35733.1; -; mRNA.
EMBL; AK145268; BAE26335.1; -; mRNA.
EMBL; AC158987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466522; EDL26396.1; -; Genomic_DNA.
EMBL; BC052196; AAH52196.1; -; mRNA.
EMBL; BC145651; AAI45652.1; -; mRNA.
EMBL; BC145653; AAI45654.1; -; mRNA.
CCDS; CCDS40702.1; -.
RefSeq; NP_775562.2; NM_173386.5.
UniGene; Mm.101559; -.
PDB; 4K8V; X-ray; 2.00 A; A/B/C/D=147-507.
PDB; 4K96; X-ray; 2.08 A; A/B=147-507.
PDB; 4K97; X-ray; 2.41 A; A=147-507.
PDB; 4K98; X-ray; 1.94 A; A=147-507.
PDB; 4K99; X-ray; 1.95 A; A=147-507.
PDB; 4K9A; X-ray; 2.26 A; A=147-507.
PDB; 4K9B; X-ray; 2.26 A; A=147-507.
PDB; 4LEY; X-ray; 2.50 A; A/B/C/D=142-507.
PDB; 4LEZ; X-ray; 2.36 A; A/C=142-507.
PDB; 4O6A; X-ray; 1.86 A; A/B=147-507.
PDB; 5N6I; X-ray; 3.60 A; A/B/C/D/E/F=139-507.
PDB; 5XZB; X-ray; 2.13 A; A=149-505.
PDBsum; 4K8V; -.
PDBsum; 4K96; -.
PDBsum; 4K97; -.
PDBsum; 4K98; -.
PDBsum; 4K99; -.
PDBsum; 4K9A; -.
PDBsum; 4K9B; -.
PDBsum; 4LEY; -.
PDBsum; 4LEZ; -.
PDBsum; 4O6A; -.
PDBsum; 5N6I; -.
PDBsum; 5XZB; -.
ProteinModelPortal; Q8C6L5; -.
SMR; Q8C6L5; -.
STRING; 10090.ENSMUSP00000063331; -.
iPTMnet; Q8C6L5; -.
PhosphoSitePlus; Q8C6L5; -.
EPD; Q8C6L5; -.
MaxQB; Q8C6L5; -.
PaxDb; Q8C6L5; -.
PRIDE; Q8C6L5; -.
Ensembl; ENSMUST00000070742; ENSMUSP00000063331; ENSMUSG00000032344.
GeneID; 214763; -.
KEGG; mmu:214763; -.
UCSC; uc009quj.2; mouse.
CTD; 115004; -.
MGI; MGI:2442261; Mb21d1.
eggNOG; ENOG410IE27; Eukaryota.
eggNOG; ENOG410XTKD; LUCA.
GeneTree; ENSGT00710000106842; -.
HOGENOM; HOG000293423; -.
HOVERGEN; HBG068840; -.
InParanoid; Q8C6L5; -.
KO; K17834; -.
OMA; PQDSQWD; -.
OrthoDB; EOG091G0MHW; -.
TreeFam; TF331255; -.
BRENDA; 2.7.7.86; 3474.
PRO; PR:Q8C6L5; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032344; -.
ExpressionAtlas; Q8C6L5; baseline and differential.
Genevisible; Q8C6L5; MM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0061501; F:cyclic-GMP-AMP synthase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:UniProtKB.
GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038001; P:paracrine signaling; IDA:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB.
InterPro; IPR024810; Mab-21_dom.
Pfam; PF03281; Mab-21; 1.
SMART; SM01265; Mab-21; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antiviral defense; ATP-binding;
Complete proteome; Cytoplasm; DNA-binding; GTP-binding; Immunity;
Innate immunity; Isopeptide bond; Magnesium; Metal-binding;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Transferase; Zinc.
CHAIN 1 507 Cyclic GMP-AMP synthase.
/FTId=PRO_0000421764.
NP_BIND 364 371 GTP. {ECO:0000269|PubMed:23647843}.
NP_BIND 420 424 ATP. {ECO:0000269|PubMed:23647843}.
REGION 1 146 DNA-binding.
{ECO:0000269|PubMed:28363908}.
REGION 119 132 Required for activation upon DNA viral
infection. {ECO:0000269|PubMed:28314590}.
REGION 158 201 DNA-binding.
{ECO:0000269|PubMed:23647843}.
REGION 372 395 DNA-binding.
{ECO:0000269|PubMed:23647843}.
METAL 211 211 Magnesium; catalytic.
{ECO:0000269|PubMed:23647843}.
METAL 213 213 Magnesium; catalytic.
{ECO:0000269|PubMed:23647843}.
METAL 307 307 Magnesium; catalytic.
{ECO:0000269|PubMed:23647843}.
METAL 378 378 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 384 384 Zinc. {ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 385 385 Zinc. {ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 392 392 Zinc. {ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
BINDING 197 197 GTP. {ECO:0000269|PubMed:23647843}.
BINDING 199 199 ATP. {ECO:0000269|PubMed:23647843}.
BINDING 307 307 GTP. {ECO:0000269|PubMed:23647843}.
BINDING 371 371 ATP. {ECO:0000269|PubMed:23647843}.
BINDING 402 402 ATP. {ECO:0000269|PubMed:23647843}.
MOD_RES 272 272 5-glutamyl polyglutamate.
{ECO:0000269|PubMed:26829768}.
MOD_RES 302 302 5-glutamyl glutamate.
{ECO:0000269|PubMed:26829768}.
MOD_RES 402 402 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8N884}.
MUTAGEN 198 198 G->A: Abolishes stimulation of interferon
production; when associated with A-199.
{ECO:0000269|PubMed:26229117}.
MUTAGEN 199 199 S->A: Abolishes stimulation of interferon
production; when associated with A-199.
{ECO:0000269|PubMed:26229117}.
MUTAGEN 211 211 E->A: Abolishes ability to promote type-I
interferon production.
{ECO:0000269|PubMed:23258413}.
MUTAGEN 213 213 D->A: Abolishes ability to promote type-I
interferon production.
{ECO:0000269|PubMed:23258413}.
MUTAGEN 272 272 E->A: Increased DNA-binding activity.
{ECO:0000269|PubMed:26829768}.
MUTAGEN 302 302 E->A: Increased nucleotidyltransferase
activity. {ECO:0000269|PubMed:26829768}.
CONFLICT 6 6 R -> I (in Ref. 2; BAE26335).
{ECO:0000305}.
CONFLICT 471 471 P -> R (in Ref. 2; BAE26335).
{ECO:0000305}.
HELIX 147 157 {ECO:0000244|PDB:4O6A}.
HELIX 161 184 {ECO:0000244|PDB:4O6A}.
STRAND 185 187 {ECO:0000244|PDB:4O6A}.
TURN 188 191 {ECO:0000244|PDB:4O6A}.
STRAND 193 198 {ECO:0000244|PDB:4O6A}.
TURN 199 203 {ECO:0000244|PDB:4O6A}.
STRAND 207 209 {ECO:0000244|PDB:4O6A}.
STRAND 211 219 {ECO:0000244|PDB:4O6A}.
STRAND 222 228 {ECO:0000244|PDB:4O6A}.
STRAND 232 239 {ECO:0000244|PDB:4O6A}.
HELIX 249 251 {ECO:0000244|PDB:4O6A}.
STRAND 252 257 {ECO:0000244|PDB:4O6A}.
HELIX 259 274 {ECO:0000244|PDB:4O6A}.
STRAND 279 284 {ECO:0000244|PDB:4O6A}.
STRAND 293 314 {ECO:0000244|PDB:4O6A}.
HELIX 320 322 {ECO:0000244|PDB:4O6A}.
TURN 329 332 {ECO:0000244|PDB:4O6A}.
HELIX 334 340 {ECO:0000244|PDB:4O6A}.
STRAND 345 349 {ECO:0000244|PDB:4O6A}.
STRAND 352 354 {ECO:0000244|PDB:4K98}.
HELIX 359 361 {ECO:0000244|PDB:4O6A}.
STRAND 363 366 {ECO:0000244|PDB:4O6A}.
HELIX 368 376 {ECO:0000244|PDB:4O6A}.
TURN 382 385 {ECO:0000244|PDB:4O6A}.
HELIX 394 411 {ECO:0000244|PDB:4O6A}.
HELIX 413 415 {ECO:0000244|PDB:4O6A}.
HELIX 420 433 {ECO:0000244|PDB:4O6A}.
HELIX 437 440 {ECO:0000244|PDB:4O6A}.
HELIX 442 444 {ECO:0000244|PDB:4O6A}.
HELIX 445 462 {ECO:0000244|PDB:4O6A}.
STRAND 468 470 {ECO:0000244|PDB:4O6A}.
TURN 478 480 {ECO:0000244|PDB:4O6A}.
HELIX 483 498 {ECO:0000244|PDB:4O6A}.
HELIX 502 505 {ECO:0000244|PDB:4O6A}.
SEQUENCE 507 AA; 58194 MW; 9FDA84DF5E4859CA CRC64;
MEDPRRRTTA PRAKKPSAKR APTQPSRTRA HAESCGPQRG ARSRRAERDG DTTEKPRAPG
PRVHPARATE LTKDAQPSAM DAAGATARPA VRVPQQQAIL DPELPAVREP QPPADPEARK
VVRGPSHRRG ARSTGQPRAP RGSRKEPDKL KKVLDKLRLK RKDISEAAET VNKVVERLLR
RMQKRESEFK GVEQLNTGSY YEHVKISAPN EFDVMFKLEV PRIELQEYYE TGAFYLVKFK
RIPRGNPLSH FLEGEVLSAT KMLSKFRKII KEEVKEIKDI DVSVEKEKPG SPAVTLLIRN
PEEISVDIIL ALESKGSWPI STKEGLPIQG WLGTKVRTNL RREPFYLVPK NAKDGNSFQG
ETWRLSFSHT EKYILNNHGI EKTCCESSGA KCCRKECLKL MKYLLEQLKK EFQELDAFCS
YHVKTAIFHM WTQDPQDSQW DPRNLSSCFD KLLAFFLECL RTEKLDHYFI PKFNLFSQEL
IDRKSKEFLS KKIEYERNNG FPIFDKL


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