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

 CGAS_PIG                Reviewed;         495 AA.
I3LM39;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
11-JUL-2012, sequence version 1.
25-OCT-2017, entry version 37.
RecName: Full=Cyclic GMP-AMP synthase {ECO:0000250|UniProtKB:Q8N884};
Short=cGAMP synthase {ECO:0000250|UniProtKB:Q8N884};
Short=cGAS {ECO:0000250|UniProtKB:Q8N884};
EC=2.7.7.86 {ECO:0000269|PubMed:23722159};
AltName: Full=2'3'-cGAMP synthase {ECO:0000250|UniProtKB:Q8N884};
AltName: Full=Mab-21 domain-containing protein 1 {ECO:0000250|UniProtKB:Q8N884};
Name=MB21D1 {ECO:0000250|UniProtKB:Q8N884};
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Porcine genome sequencing project;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 135-495 IN COMPLEXES WITH
MAGNESIUM IONS, ZINC IONS; ATP; GTP; UTP AND DNA, COFACTOR, FUNCTION,
CATALYTIC ACTIVITY, ENZYME REGULATION, DNA-BINDING, AND MUTAGENESIS OF
GLU-200 AND ASP-202.
PubMed=23722159; DOI=10.1038/nature12305;
Civril F., Deimling T., de Oliveira Mann C.C., Ablasser A., Moldt M.,
Witte G., Hornung V., Hopfner K.P.;
"Structural mechanism of cytosolic DNA sensing by cGAS.";
Nature 498:332-337(2013).
-!- FUNCTION: Nucleotidyltransferase that catalyzes the formation of
cyclic GMP-AMP (cGAMP) from ATP and GTP (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
(By similarity). 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 (By similarity). Has antiviral activity by
sensing the presence of dsDNA from DNA viruses in the cytoplasm
(By similarity). Also acts as an innate immune sensor of infection
by retroviruses by detecting the presence of reverse-transcribed
DNA in the cytosol (By similarity). 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, such as M.tuberculosis. 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 (By similarity). 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 (By similarity). In addition to antiviral activity, also
involved in the response to cellular stresses, such as senescence,
DNA damage or genome instability (By similarity). 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 (By similarity). Also involved in the
inflammatory response to genome instability and double-stranded
DNA breaks: acts by localizing to micronuclei arising from genome
instability (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q8C6L5,
ECO:0000269|PubMed:23722159}.
-!- CATALYTIC ACTIVITY: ATP + GTP = 2 diphosphate + cyclic G-P(2'-
5')A-P(3'-5'). {ECO:0000269|PubMed:23722159}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:23722159};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:23722159};
-!- ENZYME REGULATION: The enzyme activity is strongly increased by
double-stranded DNA, but not by single-stranded DNA or RNA
(PubMed:23722159). The enzyme activity is impaired by the cleavage
by CASP1 (By similarity). {ECO:0000250|UniProtKB:Q8N884,
ECO:0000269|PubMed:23722159}.
-!- SUBUNIT: Monomer in the absence of DNA and when bound to dsDNA.
Interacts with PQBP1 (via WW domain).
{ECO:0000250|UniProtKB:Q8N884}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q8C6L5}.
-!- DOMAIN: The N-terminal part (1-160) 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 (By similarity). When the N-
terminal part (1-160) is missing the protein bound to dsDNA
homodimerizes (By similarity). {ECO:0000250|UniProtKB:Q8C6L5,
ECO:0000250|UniProtKB:Q8N884}.
-!- PTM: Polyglutamylated by TTLL6 at Glu-261, leading to impair DNA-
binding activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6.
{ECO:0000250|UniProtKB:Q8C6L5}.
-!- PTM: 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. {ECO:0000250|UniProtKB:Q8N884}.
-!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; FP102323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_013840602.1; XM_013985148.1.
PDB; 4JLX; X-ray; 2.00 A; A=135-495.
PDB; 4JLZ; X-ray; 2.27 A; A/B=135-495.
PDB; 4KB6; X-ray; 3.08 A; A=135-495.
PDBsum; 4JLX; -.
PDBsum; 4JLZ; -.
PDBsum; 4KB6; -.
SMR; I3LM39; -.
STRING; 9823.ENSSSCP00000025159; -.
PaxDb; I3LM39; -.
PeptideAtlas; I3LM39; -.
PRIDE; I3LM39; -.
Ensembl; ENSSSCT00000030573; ENSSSCP00000025159; ENSSSCG00000021383.
GeneID; 100516408; -.
KEGG; ssc:100516408; -.
CTD; 115004; -.
eggNOG; ENOG410IE27; Eukaryota.
eggNOG; ENOG410XTKD; LUCA.
GeneTree; ENSGT00710000106842; -.
InParanoid; I3LM39; -.
KO; K17834; -.
OMA; PQDSQWD; -.
OrthoDB; EOG091G0MHW; -.
TreeFam; TF331255; -.
Proteomes; UP000008227; Chromosome 1.
Bgee; ENSSSCG00000021383; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0061501; F:cyclic-GMP-AMP synthase activity; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; ISS: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; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0009190; P:cyclic nucleotide biosynthetic process; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038001; P:paracrine signaling; ISS:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; ISS:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; ISS: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 1 495 Cyclic GMP-AMP synthase.
/FTId=PRO_0000423063.
NP_BIND 351 358 GTP. {ECO:0000269|PubMed:23722159}.
NP_BIND 410 414 ATP. {ECO:0000269|PubMed:23722159}.
REGION 1 134 DNA-binding.
{ECO:0000250|UniProtKB:Q8N884}.
REGION 103 134 Required for activation upon DNA viral
infection.
{ECO:0000250|UniProtKB:Q8N884}.
REGION 147 190 DNA-binding.
{ECO:0000269|PubMed:23722159}.
REGION 359 382 DNA-binding.
{ECO:0000269|PubMed:23722159}.
METAL 200 200 Magnesium; catalytic.
{ECO:0000269|PubMed:23722159}.
METAL 202 202 Magnesium; catalytic.
{ECO:0000269|PubMed:23722159}.
METAL 294 294 Magnesium; catalytic.
{ECO:0000269|PubMed:23722159}.
METAL 365 365 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:23722159}.
METAL 371 371 Zinc. {ECO:0000269|PubMed:23722159}.
METAL 372 372 Zinc. {ECO:0000269|PubMed:23722159}.
METAL 379 379 Zinc. {ECO:0000269|PubMed:23722159}.
BINDING 186 186 GTP. {ECO:0000269|PubMed:23722159}.
BINDING 188 188 ATP. {ECO:0000269|PubMed:23722159}.
BINDING 294 294 GTP. {ECO:0000269|PubMed:23722159}.
BINDING 358 358 ATP. {ECO:0000269|PubMed:23722159}.
BINDING 389 389 ATP. {ECO:0000269|PubMed:23722159}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8N884}.
MOD_RES 261 261 5-glutamyl polyglutamate.
{ECO:0000250|UniProtKB:Q8C6L5}.
MOD_RES 389 389 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8N884}.
MUTAGEN 200 200 E->Q: Abolishes enzyme activity and
stimulation of interferon production;
when associated with N-202.
{ECO:0000269|PubMed:23722159}.
MUTAGEN 202 202 D->N: Abolishes enzyme activity and
stimulation of interferon production;
when associated with Q-200.
{ECO:0000269|PubMed:23722159}.
HELIX 139 147 {ECO:0000244|PDB:4JLX}.
HELIX 150 173 {ECO:0000244|PDB:4JLX}.
TURN 177 180 {ECO:0000244|PDB:4JLX}.
STRAND 182 184 {ECO:0000244|PDB:4JLX}.
TURN 188 192 {ECO:0000244|PDB:4JLZ}.
STRAND 200 208 {ECO:0000244|PDB:4JLX}.
STRAND 213 217 {ECO:0000244|PDB:4JLX}.
STRAND 221 227 {ECO:0000244|PDB:4JLX}.
HELIX 238 240 {ECO:0000244|PDB:4JLX}.
HELIX 248 262 {ECO:0000244|PDB:4JLX}.
STRAND 269 271 {ECO:0000244|PDB:4JLX}.
STRAND 281 285 {ECO:0000244|PDB:4JLX}.
STRAND 287 289 {ECO:0000244|PDB:4JLX}.
STRAND 291 301 {ECO:0000244|PDB:4JLX}.
HELIX 307 309 {ECO:0000244|PDB:4JLX}.
TURN 316 319 {ECO:0000244|PDB:4JLX}.
HELIX 321 328 {ECO:0000244|PDB:4JLX}.
STRAND 332 335 {ECO:0000244|PDB:4JLX}.
STRAND 339 344 {ECO:0000244|PDB:4JLZ}.
HELIX 346 348 {ECO:0000244|PDB:4JLX}.
STRAND 350 353 {ECO:0000244|PDB:4JLX}.
HELIX 355 363 {ECO:0000244|PDB:4JLX}.
STRAND 366 368 {ECO:0000244|PDB:4JLZ}.
TURN 369 372 {ECO:0000244|PDB:4JLX}.
HELIX 381 398 {ECO:0000244|PDB:4JLX}.
TURN 399 401 {ECO:0000244|PDB:4JLX}.
TURN 404 407 {ECO:0000244|PDB:4JLX}.
HELIX 410 423 {ECO:0000244|PDB:4JLX}.
HELIX 427 429 {ECO:0000244|PDB:4JLX}.
HELIX 432 434 {ECO:0000244|PDB:4JLX}.
HELIX 435 452 {ECO:0000244|PDB:4JLX}.
TURN 468 470 {ECO:0000244|PDB:4JLX}.
HELIX 473 488 {ECO:0000244|PDB:4JLX}.
HELIX 492 494 {ECO:0000244|PDB:4JLX}.
SEQUENCE 495 AA; 55809 MW; 13E76296D97E176B CRC64;
MAARRGKSTR TASEVGAAGP RASARSVNGA PTVPEAARPG ARRNGPSRAS GCRREKSGPD
PREKPQVRTR TARAEDQAEG PSAPSERVEP PSAQGASLLR AGSCRAREAR SARELRPQAG
ATELAAPARM EAPPGAWKLQ TVLEKVRLSR HEISEAAEVV NWVVEHLLRR LQGGESEFKG
VALLRTGSYY ERVKISAPNE FDVMFKLEVP RIQLEEYCNS GAHYFVKFKR NPGGNPLEQF
LEKEILSASK MLSKFRKIIK EEIKNIEGVT VERKRRGSPA VTLLISKPKE ISVDIILALE
SKSSWPASTQ KGLPISQWLG AKVKNNLKRQ PFYLVPKHAK EGSGFQEETW RLSFSHIEKD
ILKNHGQSKT CCEIDGVKCC RKECLKLMKY LLEQLKKKFG NRRELAKFCS YHVKTAFFHV
CTQDPHDNQW HLKNLECCFD NCVAYFLQCL KTEQLANYFI PGVNLFSRDL IDKPSKEFLS
KQIEYERNNG FPVFW


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