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

 CGAS_HUMAN              Reviewed;         522 AA.
Q8N884; L0L2J9; Q14CV6; Q32NC9; Q5SWL0; Q5SWL1; Q96E45;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
30-AUG-2017, entry version 123.
RecName: Full=Cyclic GMP-AMP synthase;
Short=cGAMP synthase;
Short=cGAS;
Short=h-cGAS;
EC=2.7.7.86 {ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:23722159, ECO:0000269|PubMed:25131990};
AltName: Full=2'3'-cGAMP synthase;
AltName: Full=Mab-21 domain-containing protein 1;
Name=MB21D1; Synonyms=C6orf150;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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] (ISOFORM 1), AND VARIANT
ASN-35.
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ASN-35 AND HIS-261.
TISSUE=Brain, Prostate, and Testis;
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).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-414, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
FUNCTION, AND INDUCTION.
PubMed=21478870; DOI=10.1038/nature09907;
Schoggins J.W., Wilson S.J., Panis M., Murphy M.Y., Jones C.T.,
Bieniasz P., Rice C.M.;
"A diverse range of gene products are effectors of the type I
interferon antiviral response.";
Nature 472:481-485(2011).
[8]
FUNCTION.
PubMed=23707065; DOI=10.1016/j.celrep.2013.05.009;
Diner E.J., Burdette D.L., Wilson S.C., Monroe K.M.,
Kellenberger C.A., Hyodo M., Hayakawa Y., Hammond M.C., Vance R.E.;
"The innate immune DNA sensor cGAS produces a noncanonical cyclic
dinucleotide that activates human STING.";
Cell Rep. 3:1355-1361(2013).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-173; LEU-174;
ARG-176; 212-GLY-SER-213; GLU-225; ASP-227; 396-CYS-CYS-397; LYS-407
AND LYS-411.
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).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-211; ARG-376 AND
TYR-436.
PubMed=25131990; DOI=10.1016/j.cell.2014.07.028;
Kranzusch P.J., Lee A.S., Wilson S.C., Solovykh M.S., Vance R.E.,
Berger J.M., Doudna J.A.;
"Structure-guided reprogramming of human cGAS dinucleotide linkage
specificity.";
Cell 158:1011-1021(2014).
[11]
FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
PubMed=26048138; DOI=10.1016/j.chom.2015.05.003;
Wassermann R., Gulen M.F., Sala C., Perin S.G., Lou Y., Rybniker J.,
Schmid-Burgk J.L., Schmidt T., Hornung V., Cole S.T., Ablasser A.;
"Mycobacterium tuberculosis differentially activates cGAS- and
inflammasome-dependent intracellular immune responses through ESX-1.";
Cell Host Microbe 17:799-810(2015).
[12]
FUNCTION, AND ENZYME REGULATION.
PubMed=26300263; DOI=10.1016/j.molcel.2015.07.022;
Kranzusch P.J., Wilson S.C., Lee A.S., Berger J.M., Doudna J.A.,
Vance R.E.;
"Ancient origin of cGAS-STING reveals mechanism of universal 2',3'
cGAMP signaling.";
Mol. Cell 59:891-903(2015).
[13]
FUNCTION, AND MUTAGENESIS OF GLU-225 AND ASP-227.
PubMed=26229115; DOI=10.1126/science.aab3628;
Gentili M., Kowal J., Tkach M., Satoh T., Lahaye X., Conrad C.,
Boyron M., Lombard B., Durand S., Kroemer G., Loew D., Dalod M.,
Thery C., Manel N.;
"Transmission of innate immune signaling by packaging of cGAMP in
viral particles.";
Science 349:1232-1236(2015).
[14]
FUNCTION, AND DOMAIN.
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).
[15]
FUNCTION, CLEAVAGE, ENZYME REGULATION, DOMAIN, AND MUTAGENESIS OF
ASP-33; ASP-67; ASP-90; ASP-95; ASP-140 AND ASP-157.
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).
[16]
FUNCTION, DNA-BINDING, DOMAIN, AND MONOMER.
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).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 157-222 IN COMPLEX WITH ZINC
IONS, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, ENZYME REGULATION,
DNA-BINDING, AND MUTAGENESIS OF LYS-171; LYS-173; GLU-225; ASP-227;
LYS-384; HIS-390; LYS-394; CYS-396; CYS-397; CYS-404; LYS-407 AND
LYS-414.
PubMed=23707061; DOI=10.1016/j.celrep.2013.05.008;
Kranzusch P.J., Lee A.S., Berger J.M., Doudna J.A.;
"Structure of human cGAS reveals a conserved family of second-
messenger enzymes in innate immunity.";
Cell Rep. 3:1362-1368(2013).
[18]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 157-522 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).
[19]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 161-522 IN COMPLEX WITH
ZINC, FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-384; LYS-400;
LYS-403; LYS-407 AND LYS-411.
PubMed=24116191; DOI=10.1371/journal.pone.0076983;
Kato K., Ishii R., Goto E., Ishitani R., Tokunaga F., Nureki O.;
"Structural and functional analyses of DNA-sensing and immune
activation by human cGAS.";
PLoS ONE 8:E76983-E76983(2013).
[20]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 161-522 IN COMPLEX WITH ZINC
AND CYCLIC GMP-AMP, FUNCTION, AND MUTAGENESIS OF ARG-236; LYS-254;
LYS-327; LYS-347; ARG-353 AND LYS-394.
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:28314590).
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:28363908, PubMed:28214358). Has
antiviral activity by acting 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:28363908). 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:28363908, PubMed:28314590). cGAMP
can 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:26229115). {ECO:0000269|PubMed:21478870,
ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23707065, ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:24116191, ECO:0000269|PubMed:24462292,
ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:26229115,
ECO:0000269|PubMed:26300263, ECO:0000269|PubMed:28214358,
ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:28363908}.
-!- FUNCTION: (Microbial infection) Upon M.tuberculosis infection THP-
1 cells knocked-out for this gene have impaired type-I interferon
production (IF-1 beta), nor do they produce type-I IFN upon
transfection with dsDNA (PubMed:26048138).
{ECO:0000269|PubMed:26048138}.
-!- CATALYTIC ACTIVITY: ATP + GTP = 2 diphosphate + cyclic G-P(2'-
5')A-P(3'-5'). {ECO:0000269|PubMed:23258413,
ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:25131990}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q8C6L5};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q8C6L5};
-!- ENZYME REGULATION: The enzyme activity is strongly increased by
double-stranded DNA, but not by single-stranded DNA or RNA
(PubMed:23258413, PubMed:23707061, PubMed:26300263). The enzyme
activity is impaired by the cleavage at Asp-140 and Asp-157
produced by CASP1 (PubMed:28314590). {ECO:0000269|PubMed:23258413,
ECO:0000269|PubMed:23707061, ECO:0000269|PubMed:26300263,
ECO:0000269|PubMed:28314590}.
-!- SUBUNIT: Monomer in the absence of DNA and when bound to dsDNA.
{ECO:0000269|PubMed:28363908}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:23258413, ECO:0000269|PubMed:26048138}.
Note=Upon transfection with dsDNA forms punctate structures that
co-localize with DNA and Beclin-1 (BECN1) (PubMed:26048138).
{ECO:0000269|PubMed:26048138}.
-!- SUBCELLULAR LOCATION: Note=(Microbial infection) Upon infection
with virulent M.tuberculosis forms aggregates with dsDNA, non-
virulent bacteria (without the ESX-1 locus) do not form these
aggregates (PubMed:26048138). {ECO:0000269|PubMed:26048138}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N884-1; Sequence=Displayed;
Name=2;
IsoId=Q8N884-2; Sequence=VSP_014388, VSP_014389;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the monocytic cell line THP1.
{ECO:0000269|PubMed:23258413}.
-!- INDUCTION: By type I interferons. {ECO:0000269|PubMed:21478870}.
-!- 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 (PubMed:28363908, PubMed:28214358).
When the N-terminal part (1-160) is missing the protein bound to
dsDNA homodimerizes (By similarity).
{ECO:0000250|UniProtKB:Q8C6L5, ECO:0000269|PubMed:28214358,
ECO:0000269|PubMed:28363908}.
-!- PTM: Polyglutamylated by TTLL6 at Glu-286, leading to impair DNA-
binding activity. Monoglutamylated at Glu-314 by TTLL4, leading to
impair the nucleotidyltransferase activity. Deglutamylated by
AGBL5/CCP5 and AGBL6/CCP6. {ECO:0000250|UniProtKB:Q8C6L5}.
-!- PTM: Cleaved by CASP1 at Asp-140 and Asp-157 upon DNA virus
infection; the cleavage impairs cGAMP production
(PubMed:28314590). Also cleaved by the pyroptotic CASP4 and CASP5
during non-canonical inflammasome activation; they don't cut at
the same sites than CASP1 (PubMed:28314590).
{ECO:0000269|PubMed:28314590}.
-!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH12928.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; KC294566; AGB51853.1; -; mRNA.
EMBL; AK097148; BAC04965.1; -; mRNA.
EMBL; AL603910; CAI14878.1; -; Genomic_DNA.
EMBL; AC019205; CAI14878.1; JOINED; Genomic_DNA.
EMBL; AL603910; CAI14879.1; -; Genomic_DNA.
EMBL; AC019205; CAI14879.1; JOINED; Genomic_DNA.
EMBL; BC012928; AAH12928.1; ALT_INIT; mRNA.
EMBL; BC108714; AAI08715.1; -; mRNA.
EMBL; BC113606; AAI13607.1; -; mRNA.
EMBL; BC113608; AAI13609.1; -; mRNA.
EMBL; BC143694; AAI43695.1; -; mRNA.
CCDS; CCDS4978.1; -. [Q8N884-1]
RefSeq; NP_612450.2; NM_138441.2. [Q8N884-1]
UniGene; Hs.658405; -.
PDB; 4KM5; X-ray; 2.50 A; A=157-522.
PDB; 4LEV; X-ray; 1.95 A; A/B=157-522.
PDB; 4LEW; X-ray; 2.04 A; A/B=157-522.
PDB; 4MKP; X-ray; 1.95 A; A=161-522.
PDB; 4O67; X-ray; 2.44 A; A/B=161-522.
PDB; 4O68; X-ray; 2.44 A; A=147-522.
PDB; 4O69; X-ray; 2.25 A; A=161-522.
PDBsum; 4KM5; -.
PDBsum; 4LEV; -.
PDBsum; 4LEW; -.
PDBsum; 4MKP; -.
PDBsum; 4O67; -.
PDBsum; 4O68; -.
PDBsum; 4O69; -.
ProteinModelPortal; Q8N884; -.
SMR; Q8N884; -.
BioGrid; 125408; 7.
IntAct; Q8N884; 5.
STRING; 9606.ENSP00000359339; -.
iPTMnet; Q8N884; -.
PhosphoSitePlus; Q8N884; -.
BioMuta; MB21D1; -.
DMDM; 68565218; -.
EPD; Q8N884; -.
MaxQB; Q8N884; -.
PaxDb; Q8N884; -.
PeptideAtlas; Q8N884; -.
PRIDE; Q8N884; -.
DNASU; 115004; -.
Ensembl; ENST00000370315; ENSP00000359339; ENSG00000164430. [Q8N884-1]
Ensembl; ENST00000370318; ENSP00000359342; ENSG00000164430. [Q8N884-2]
GeneID; 115004; -.
KEGG; hsa:115004; -.
UCSC; uc003pgx.2; human. [Q8N884-1]
CTD; 115004; -.
DisGeNET; 115004; -.
GeneCards; MB21D1; -.
H-InvDB; HIX0022366; -.
HGNC; HGNC:21367; MB21D1.
HPA; HPA031700; -.
HPA; HPA031702; -.
MIM; 613973; gene.
neXtProt; NX_Q8N884; -.
OpenTargets; ENSG00000164430; -.
PharmGKB; PA134956015; -.
eggNOG; ENOG410IE27; Eukaryota.
eggNOG; ENOG410XTKD; LUCA.
GeneTree; ENSGT00710000106842; -.
HOGENOM; HOG000293423; -.
HOVERGEN; HBG068840; -.
InParanoid; Q8N884; -.
KO; K17834; -.
OMA; PQDSQWD; -.
OrthoDB; EOG091G0MHW; -.
PhylomeDB; Q8N884; -.
TreeFam; TF331255; -.
BRENDA; 2.7.7.86; 2681.
Reactome; R-HSA-1834941; STING mediated induction of host immune responses.
ChiTaRS; MB21D1; human.
GenomeRNAi; 115004; -.
PRO; PR:Q8N884; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000164430; -.
CleanEx; HS_C6orf150; -.
Genevisible; Q8N884; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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:0002230; P:positive regulation of defense response to virus by host; IMP: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; Alternative splicing; Antiviral defense;
ATP-binding; Complete proteome; Cytoplasm; DNA-binding; GTP-binding;
Immunity; Innate immunity; Isopeptide bond; Magnesium; Metal-binding;
Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Polymorphism; Reference proteome; Transferase; Zinc.
CHAIN 1 522 Cyclic GMP-AMP synthase.
/FTId=PRO_0000089543.
NP_BIND 376 383 GTP. {ECO:0000305|PubMed:24462292}.
NP_BIND 435 439 ATP. {ECO:0000305|PubMed:24462292}.
REGION 1 160 DNA-binding.
{ECO:0000269|PubMed:28363908}.
REGION 120 160 Required for activation upon DNA viral
infection. {ECO:0000269|PubMed:28314590}.
REGION 173 215 DNA-binding.
{ECO:0000305|PubMed:23707061}.
REGION 384 407 DNA-binding.
{ECO:0000305|PubMed:23707061}.
METAL 225 225 Magnesium; catalytic. {ECO:0000305}.
METAL 227 227 Magnesium; catalytic. {ECO:0000305}.
METAL 319 319 Magnesium; catalytic.
{ECO:0000250|UniProtKB:Q8C6L5}.
METAL 390 390 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 396 396 Zinc. {ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 397 397 Zinc. {ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
METAL 404 404 Zinc. {ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292}.
BINDING 211 211 GTP. {ECO:0000250|UniProtKB:Q8C6L5}.
BINDING 213 213 ATP. {ECO:0000250|UniProtKB:Q8C6L5}.
BINDING 319 319 GTP. {ECO:0000305|PubMed:24462292}.
BINDING 383 383 ATP. {ECO:0000250|UniProtKB:Q8C6L5}.
BINDING 414 414 ATP. {ECO:0000250|UniProtKB:Q8C6L5}.
SITE 140 141 Cleavage; by CASP1.
{ECO:0000269|PubMed:28314590}.
SITE 157 158 Cleavage; by CASP1.
{ECO:0000269|PubMed:28314590}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 286 286 5-glutamyl polyglutamate.
{ECO:0000250|UniProtKB:Q8C6L5}.
MOD_RES 314 314 5-glutamyl glutamate.
{ECO:0000250|UniProtKB:Q8C6L5}.
MOD_RES 414 414 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 445 447 VCT -> RLY (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014388.
VAR_SEQ 448 522 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014389.
VARIANT 35 35 T -> N (in dbSNP:rs9352000).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_050811.
VARIANT 261 261 P -> H (in dbSNP:rs610913).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_033677.
MUTAGEN 33 33 D->A: No effect on type I IFN and RSAD2
induction. No effect on cleavage by
CASP1. No effect on cleavage by CASP1;
when associated with A-67; A-90 and A-95.
Highly decreases cleavage by CASP1 and
enhances RSAD2 induction upon DNA virus
infection; when associated with A-67; A-
90; A-95 and A-140. Abolishes cleavage by
CASP1 and enhances RSAD2 induction upon
DNA virus infection; when associated with
A-67; A-90; A-95; A-140 and A-157.
{ECO:0000269|PubMed:28314590}.
MUTAGEN 67 67 D->A: No effect on type I IFN and RSAD2
induction. No effect on cleavage by
CASP1; when associated with A-33; A-90
and A-95. Highly decreases cleavage by
CASP1 and enhances RSAD2 induction upon
DNA virus infection; when assocaited with
A-33; A-90; A-95 and A-140. Abolishes
cleavage by CASP1 and enhances RSAD2
induction upon DNA virus infection; when
associated with A-33; A-90; A-95; A-140
and A-157. {ECO:0000269|PubMed:28314590}.
MUTAGEN 90 90 D->A: No effect on type I IFN and RSAD2
induction. No effect on cleavage by
CASP1; when associated with A-33; A-67
and A-95. Highly decreases cleavage by
CASP1 and enhances RSAD2 induction upon
DNA virus infection; when associated with
A-33; A-67; A-95 and A-140. Abolishes
cleavage by CASP1 and enhances RSAD2
induction upon DNA virus infection; when
associated with A-33; A-67; A-95; A-140
and A-157. {ECO:0000269|PubMed:28314590}.
MUTAGEN 95 95 D->A: No effect on type I IFN and RSAD2
induction. No effect on cleavage by
CASP1; when associated with A-33; A-67
and A-90. Highly decreases cleavage by
CASP1 and enhances RSAD2 induction upon
DNA virus infection; when associated with
A-33; A-67; A-90 and A-140. Abolishes
cleavage by CASP1 and enhances RSAD2
induction upon DNA virus infection; when
associated with A-33; A-67; A-90; A-140
and A-157. {ECO:0000269|PubMed:28314590}.
MUTAGEN 140 140 D->A: Highly decreases cleavage by CASP1
and enhances type I IFN and RSAD2
induction upon DNA virus infection.
Abolishes cleavage by CASP1, enhances
RSAD2 induction upon DNA virus infection
but no effect on cleavage by CASP5; when
associated with A-157. Highly decreases
cleavage by CASP1 and enhances RSAD2
induction upon DNA virus infection; when
associated with A-33; A-67; A-90 and A-
95. Abolishes cleavage by CASP1 and
enhances RSAD2 induction upon DNA virus
infection; when associated with A-33; A-
67; A-90; A-95 and A-157.
{ECO:0000269|PubMed:28314590}.
MUTAGEN 140 140 D->H: Highly decreases cleavage by CASP1
and enhances type I IFN and RSAD2
induction upon DNA virus infection.
{ECO:0000269|PubMed:28314590}.
MUTAGEN 157 157 D->A: No effect on type I IFN and RSAD2
induction. Highly decreases cleavage by
CASP1 and enhances type I IFN and
enhances RSAD2 induction upon DNA virus
infection. Abolishes cleavage by CASP1,
enhances RSAD2 induction upon DNA virus
infection but no effect on cleavage by
CASP5; when associated with A-140.
Abolishes cleavage by CASP1; when
associated with A-33; A-67; A-90; A-95
and A-140. {ECO:0000269|PubMed:28314590}.
MUTAGEN 157 157 D->H: Highly decreases cleavage by CASP1
and enhances type I IFN and enhances
RSAD2 induction upon DNA virus infection.
{ECO:0000269|PubMed:28314590}.
MUTAGEN 171 171 K->A: No effect on stimulation of
interferon production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 173 173 K->A: Strongly reduces enzyme activity
and stimulation of interferon production;
when associated with A-176. No effect on
stimulation of interferon production.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:24116191}.
MUTAGEN 173 173 K->E: Strongly reduces stimulation of
interferon production.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23722159}.
MUTAGEN 174 174 L->N: Strongly reduces enzyme activity
and stimulation of interferon production.
{ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:24116191}.
MUTAGEN 176 176 R->A: Strongly reduces enzyme activity
and stimulation of interferon production;
when associated with A-173.
{ECO:0000269|PubMed:23722159}.
MUTAGEN 211 211 T->Q: Abolishes enzyme activity; when
associated with I-376 and I-436.
{ECO:0000269|PubMed:25131990}.
MUTAGEN 212 213 GS->AA: Abolishes enzyme activity.
Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:23722159}.
MUTAGEN 225 225 E->A: Abolishes enzyme activity and
stimulation of interferon production;
when associated with A-227.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:26229115}.
MUTAGEN 227 227 D->A: Abolishes enzyme activity and
stimulation of interferon production;
when associated with A-225.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23722159,
ECO:0000269|PubMed:26229115}.
MUTAGEN 236 236 R->E: Abolishes stimulation of interferon
production; when associated with E-254
and E-327. {ECO:0000269|PubMed:24462292}.
MUTAGEN 254 254 K->E: Abolishes stimulation of interferon
production; when associated with E-236
and E-327. {ECO:0000269|PubMed:24462292}.
MUTAGEN 327 327 K->E: Abolishes stimulation of interferon
production; when associated with E-236
and E-254. {ECO:0000269|PubMed:24462292}.
MUTAGEN 347 347 K->E: Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:24462292}.
MUTAGEN 353 353 R->E: Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:24462292}.
MUTAGEN 376 376 R->I: Alters enzyme activity, leading to
the appearance of 3'-5' linked cGAMP.
Abolishes enzyme activity; when
associated with Q-211 and I-436.
{ECO:0000269|PubMed:25131990}.
MUTAGEN 384 384 K->A,E: Abolishes stimulation of
interferon production.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24116191}.
MUTAGEN 390 390 H->A: Strongly reduces stimulation of
interferon production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 394 394 K->A: Abolishes enzyme activity. No
effect on stimulation of interferon
production. {ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:24462292}.
MUTAGEN 394 394 K->E: Abolishes enzyme activity.
Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 396 397 CC->AA: Abolishes DNA binding and enzyme
activity. Abolishes stimulation of
interferon production.
{ECO:0000269|PubMed:23722159}.
MUTAGEN 396 396 C->A: Abolishes DNA binding and enzyme
activity. {ECO:0000269|PubMed:23707061}.
MUTAGEN 397 397 C->A: Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 400 400 K->E: Abolishes stimulation of interferon
production; when associated with E-403.
{ECO:0000269|PubMed:24116191}.
MUTAGEN 403 403 K->E: Abolishes stimulation of interferon
production; when associated with E-400.
{ECO:0000269|PubMed:24116191}.
MUTAGEN 404 404 C->A: Abolishes stimulation of interferon
production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 407 407 K->A,E: Abolishes enzyme activity and
stimulation of interferon production;
when associated with A-411. Abolishes
enzyme activity. Abolishes stimulation of
interferon production.
{ECO:0000269|PubMed:23707061,
ECO:0000269|PubMed:23722159}.
MUTAGEN 411 411 K->A: Abolishes enzyme activity and
stimulation of interferon production;
when associated with A-407.
{ECO:0000269|PubMed:23722159}.
MUTAGEN 414 414 K->A,E: Abolishes stimulation of
interferon production.
{ECO:0000269|PubMed:23707061}.
MUTAGEN 436 436 Y->I: Abolishes enzyme activity; when
associated with Q-211 and I-376.
{ECO:0000269|PubMed:25131990}.
STRAND 157 159 {ECO:0000244|PDB:4LEV}.
HELIX 162 174 {ECO:0000244|PDB:4LEV}.
TURN 175 178 {ECO:0000244|PDB:4LEV}.
HELIX 180 197 {ECO:0000244|PDB:4LEV}.
HELIX 201 203 {ECO:0000244|PDB:4LEV}.
STRAND 207 210 {ECO:0000244|PDB:4LEV}.
HELIX 212 216 {ECO:0000244|PDB:4MKP}.
STRAND 220 222 {ECO:0000244|PDB:4O67}.
STRAND 225 233 {ECO:0000244|PDB:4LEV}.
STRAND 237 242 {ECO:0000244|PDB:4LEV}.
STRAND 246 254 {ECO:0000244|PDB:4LEV}.
HELIX 263 265 {ECO:0000244|PDB:4LEV}.
HELIX 273 288 {ECO:0000244|PDB:4LEV}.
STRAND 292 294 {ECO:0000244|PDB:4LEW}.
STRAND 296 298 {ECO:0000244|PDB:4LEV}.
STRAND 304 306 {ECO:0000244|PDB:4LEV}.
STRAND 308 312 {ECO:0000244|PDB:4LEV}.
TURN 313 315 {ECO:0000244|PDB:4LEV}.
STRAND 316 326 {ECO:0000244|PDB:4LEV}.
HELIX 332 334 {ECO:0000244|PDB:4LEV}.
TURN 341 344 {ECO:0000244|PDB:4LEV}.
HELIX 346 353 {ECO:0000244|PDB:4LEV}.
STRAND 357 361 {ECO:0000244|PDB:4LEV}.
STRAND 375 378 {ECO:0000244|PDB:4LEV}.
HELIX 380 388 {ECO:0000244|PDB:4LEV}.
STRAND 391 393 {ECO:0000244|PDB:4LEW}.
TURN 394 397 {ECO:0000244|PDB:4LEV}.
STRAND 398 400 {ECO:0000244|PDB:4LEV}.
HELIX 406 423 {ECO:0000244|PDB:4LEV}.
HELIX 425 427 {ECO:0000244|PDB:4LEV}.
TURN 429 432 {ECO:0000244|PDB:4LEV}.
HELIX 435 448 {ECO:0000244|PDB:4LEV}.
HELIX 452 455 {ECO:0000244|PDB:4LEV}.
HELIX 457 459 {ECO:0000244|PDB:4LEV}.
HELIX 460 477 {ECO:0000244|PDB:4LEV}.
TURN 493 495 {ECO:0000244|PDB:4LEV}.
HELIX 498 513 {ECO:0000244|PDB:4LEV}.
HELIX 518 521 {ECO:0000244|PDB:4LEV}.
SEQUENCE 522 AA; 58814 MW; 808FF6F9F3BF8C50 CRC64;
MQPWHGKAMQ RASEAGATAP KASARNARGA PMDPTESPAA PEAALPKAGK FGPARKSGSR
QKKSAPDTQE RPPVRATGAR AKKAPQRAQD TQPSDATSAP GAEGLEPPAA REPALSRAGS
CRQRGARCST KPRPPPGPWD VPSPGLPVSA PILVRRDAAP GASKLRAVLE KLKLSRDDIS
TAAGMVKGVV DHLLLRLKCD SAFRGVGLLN TGSYYEHVKI SAPNEFDVMF KLEVPRIQLE
EYSNTRAYYF VKFKRNPKEN PLSQFLEGEI LSASKMLSKF RKIIKEEIND IKDTDVIMKR
KRGGSPAVTL LISEKISVDI TLALESKSSW PASTQEGLRI QNWLSAKVRK QLRLKPFYLV
PKHAKEGNGF QEETWRLSFS HIEKEILNNH GKSKTCCENK EEKCCRKDCL KLMKYLLEQL
KERFKDKKHL DKFSSYHVKT AFFHVCTQNP QDSQWDRKDL GLCFDNCVTY FLQCLRTEKL
ENYFIPEFNL FSSNLIDKRS KEFLTKQIEY ERNNEFPVFD EF


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