Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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.
16-JAN-2019, entry version 113.
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, ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:29976794, ECO:0000269|PubMed:30007416};
AltName: Full=2'3'-cGAMP synthase {ECO:0000303|PubMed:23258413};
AltName: Full=Mab-21 domain-containing protein 1;
Name=Cgas {ECO:0000303|PubMed:23258413, ECO:0000312|MGI:MGI:2442261};
Synonyms=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 ACTIVITY 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 548:461-465(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. 19:1061-1070(2017).
[16]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ASN-172;
ARG-180; CYS-419 AND HIS-467.
PubMed=30007416; DOI=10.1016/j.cell.2018.06.026;
Zhou W., Whiteley A.T., de Oliveira Mann C.C., Morehouse B.R.,
Nowak R.P., Fischer E.S., Gray N.S., Mekalanos J.J., Kranzusch P.J.;
"Structure of the human cGAS-DNA complex reveals enhanced control of
immune surveillance.";
Cell 174:300-311(2018).
[17]
FUNCTION.
PubMed=30356214; DOI=10.1038/s41586-018-0629-6;
Liu H., Zhang H., Wu X., Ma D., Wu J., Wang L., Jiang Y., Fei Y.,
Zhu C., Tan R., Jungblut P., Pei G., Dorhoi A., Yan Q., Zhang F.,
Zheng R., Liu S., Liang H., Liu Z., Yang H., Chen J., Wang P.,
Tang T., Peng W., Hu Z., Xu Z., Huang X., Wang J., Li H., Zhou Y.,
Liu F., Yan D., Kaufmann S.H.E., Chen C., Mao Z., Ge B.;
"Nuclear cGAS suppresses DNA repair and promotes tumorigenesis.";
Nature 0:0-0(2018).
[18]
CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=29976794; DOI=10.1126/science.aat1022;
Du M., Chen Z.J.;
"DNA-induced liquid phase condensation of cGAS activates innate immune
signaling.";
Science 361:704-709(2018).
[19]
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).
[20]
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).
[21]
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).
[22] {ECO:0000244|PDB:5N6I}
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 139-507 IN COMPLEX WITH ZINC
AND DNA, FUNCTION, AND SUBUNIT.
PubMed=28902841; DOI=10.1038/nature23890;
Andreeva L., Hiller B., Kostrewa D., Lassig C., de Oliveira Mann C.C.,
Jan Drexler D., Maiser A., Gaidt M., Leonhardt H., Hornung V.,
Hopfner K.P.;
"cGAS senses long and HMGB/TFAM-bound U-turn DNA by forming protein-
DNA ladders.";
Nature 549:394-398(2017).
[23] {ECO:0000244|PDB:5XZB, ECO:0000244|PDB:5XZE, ECO:0000244|PDB:5XZG}
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 147-507 IN COMPLEX WITH ZINC
AND INHIBITOR RU.521, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
PubMed=28963528; DOI=10.1038/s41467-017-00833-9;
Vincent J., Adura C., Gao P., Luz A., Lama L., Asano Y., Okamoto R.,
Imaeda T., Aida J., Rothamel K., Gogakos T., Steinberg J.,
Reasoner S., Aso K., Tuschl T., Patel D.J., Glickman J.F., Ascano M.;
"Small molecule inhibition of cGAS reduces interferon expression in
primary macrophages from autoimmune mice.";
Nat. Commun. 8:750-750(2017).
-!- FUNCTION: Nucleotidyltransferase that catalyzes the formation of
cyclic GMP-AMP (cGAMP) from ATP and GTP and plays a key role in
innate immunity (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). Preferentially binds long dsDNA (around 45 bp)
and forms ladder-like networks that function cooperatively to
stabilize individual cGAS-dsDNA complexes (PubMed:28902841). 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, 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). Acts as a suppressor of DNA repair in response
to DNA damage: translocates to the nucleus following
dephosphorylation at Tyr-201 and inhibits homologous recombination
repair by interacting with PARP1, the CGAS-PARP1 interaction
leading to impede the formation of the PARP1-TIMELESS complex
(PubMed:30356214). {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,
ECO:0000269|PubMed:28902841, ECO:0000269|PubMed:30356214}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + GTP = cyclic G(2'-5')pA(3'-5')p + 2 diphosphate;
Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
ChEBI:CHEBI:37565, ChEBI:CHEBI:78624; EC=2.7.7.86;
Evidence={ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:29976794,
ECO:0000269|PubMed:30007416};
-!- 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};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:29976794};
Note=Undergoes a liquid-like phase transition after binding to
DNA, which is dependent on zinc. {ECO:0000250|UniProtKB:Q8N884};
-!- ACTIVITY 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).
Strongly inhibited by compound RU.521, which is specific for mouse
protein (PubMed:28963528, PubMed:30007416).
{ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:28314590,
ECO:0000269|PubMed:28963528, ECO:0000269|PubMed:30007416}.
-!- SUBUNIT: Monomer in the absence of DNA (PubMed:28214358).
Homodimer in presence of dsDNA: forms a 2:2 dimer with two enzymes
binding to two DNA molecules (PubMed:28902841). Interacts with
PQBP1 (via WW domain) (By similarity). Interacts with TRIM14; this
interaction stabilizes CGAS and promotes type I interferon
production (By similarity). Interacts with ZCCHC3; promoting
sensing of dsDNA by CGAS (By similarity). Interacts with PARP1;
interaction takes place in the nucleus and prevents the formation
of the PARP1-TIMELESS complex (By similarity).
{ECO:0000250|UniProtKB:Q8N884, ECO:0000269|PubMed:28214358,
ECO:0000269|PubMed:28902841}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:23258413}. Nucleus
{ECO:0000250|UniProtKB:Q8N884}. Note=Mainly localizes in the
cytosol. Upon transfection with dsDNA forms punctate structures
that co-localize with DNA and Beclin-1 (BECN1) (By similarity).
Phosphorylation at Tyr-201 promotes cytosolic retention;
translocates into the nucleus following dephosphorylation (By
similarity). {ECO:0000250|UniProtKB:Q8N884}.
-!- DOMAIN: The N-terminal part (1-146) 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 (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}.
-!- PTM: Phosphorylation at Tyr-201 by BLK promotes cytosolic
retention. Translocates into the nucleus following
dephosphorylation at Tyr-201. {ECO:0000250|UniProtKB:Q8N884}.
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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.
PDB; 5XZE; X-ray; 2.18 A; A=147-507.
PDB; 5XZG; X-ray; 1.83 A; A=147-507.
PDBsum; 4K8V; -.
PDBsum; 4K96; -.
PDBsum; 4K97; -.
PDBsum; 4K98; -.
PDBsum; 4K99; -.
PDBsum; 4K9A; -.
PDBsum; 4K9B; -.
PDBsum; 4LEY; -.
PDBsum; 4LEZ; -.
PDBsum; 4O6A; -.
PDBsum; 5N6I; -.
PDBsum; 5XZB; -.
PDBsum; 5XZE; -.
PDBsum; 5XZG; -.
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; Cgas.
eggNOG; ENOG410IE27; Eukaryota.
eggNOG; ENOG410XTKD; LUCA.
GeneTree; ENSGT00940000154062; -.
HOGENOM; HOG000293423; -.
HOVERGEN; HBG068840; -.
InParanoid; Q8C6L5; -.
KO; K17834; -.
OMA; PQDSQWD; -.
OrthoDB; 759341at2759; -.
TreeFam; TF331255; -.
BRENDA; 2.7.7.86; 3474.
PRO; PR:Q8C6L5; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032344; Expressed in 120 organ(s), highest expression level in embryo.
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:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IGI:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038001; P:paracrine signaling; IDA:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IDA:UniProtKB.
GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; 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.
GO; GO:0050776; P:regulation of immune response; IGI:MGI.
GO; GO:0002637; P:regulation of immunoglobulin production; IGI:MGI.
GO; GO:0050863; P:regulation of T cell activation; IGI:MGI.
GO; GO:0032479; P:regulation of type I interferon production; IGI:MGI.
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 damage; DNA repair; DNA-binding;
GTP-binding; Immunity; Innate immunity; Isopeptide bond; Magnesium;
Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
Phosphoprotein; 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:0000244|PDB:5N6I,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
REGION 372 395 DNA-binding. {ECO:0000244|PDB:5N6I,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
MOTIF 281 291 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q8N884}.
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:0000244|PDB:5N6I,
ECO:0000244|PDB:5XZB,
ECO:0000244|PDB:5XZE,
ECO:0000244|PDB:5XZG,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
METAL 384 384 Zinc. {ECO:0000244|PDB:5N6I,
ECO:0000244|PDB:5XZB,
ECO:0000244|PDB:5XZE,
ECO:0000244|PDB:5XZG,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
METAL 385 385 Zinc. {ECO:0000244|PDB:5N6I,
ECO:0000244|PDB:5XZB,
ECO:0000244|PDB:5XZE,
ECO:0000244|PDB:5XZG,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
METAL 392 392 Zinc. {ECO:0000244|PDB:5N6I,
ECO:0000244|PDB:5XZB,
ECO:0000244|PDB:5XZE,
ECO:0000244|PDB:5XZG,
ECO:0000269|PubMed:23647843,
ECO:0000269|PubMed:24332030,
ECO:0000269|PubMed:24462292,
ECO:0000269|PubMed:28902841,
ECO:0000269|PubMed:28963528}.
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 201 201 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8N884}.
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 172 172 N->K: Induces alteration of the DNA-
binding surface and leads to decreased
synthesis of cyclic GMP-AMP (cGAMP); when
associated with L-180.
{ECO:0000269|PubMed:30007416}.
MUTAGEN 180 180 R->L: Induces alteration of the DNA-
binding surface and leads to decreased
synthesis of cyclic GMP-AMP (cGAMP); when
associated with K-182.
{ECO:0000269|PubMed:30007416}.
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}.
MUTAGEN 419 419 C->S: Gains susceptibility to mouse-
specific RU.521; when associated with N-
467. {ECO:0000269|PubMed:30007416}.
MUTAGEN 467 467 H->N: Gains susceptibility to mouse-
specific RU.521; when associated with S-
419. {ECO:0000269|PubMed:30007416}.
CONFLICT 6 6 R -> I (in Ref. 2; BAE26335).
{ECO:0000305}.
CONFLICT 471 471 P -> R (in Ref. 2; BAE26335).
{ECO:0000305}.
HELIX 150 157 {ECO:0000244|PDB:5XZG}.
HELIX 161 183 {ECO:0000244|PDB:5XZG}.
STRAND 184 186 {ECO:0000244|PDB:5XZG}.
TURN 188 191 {ECO:0000244|PDB:5XZG}.
STRAND 193 198 {ECO:0000244|PDB:5XZG}.
TURN 199 203 {ECO:0000244|PDB:5XZG}.
STRAND 207 209 {ECO:0000244|PDB:5XZG}.
STRAND 211 219 {ECO:0000244|PDB:5XZG}.
STRAND 222 227 {ECO:0000244|PDB:5XZG}.
STRAND 232 241 {ECO:0000244|PDB:5XZG}.
HELIX 247 251 {ECO:0000244|PDB:5XZG}.
STRAND 252 257 {ECO:0000244|PDB:4O6A}.
HELIX 259 275 {ECO:0000244|PDB:5XZG}.
STRAND 279 284 {ECO:0000244|PDB:5XZG}.
STRAND 293 314 {ECO:0000244|PDB:5XZG}.
HELIX 320 322 {ECO:0000244|PDB:5XZG}.
TURN 329 332 {ECO:0000244|PDB:5XZG}.
HELIX 334 341 {ECO:0000244|PDB:5XZG}.
STRAND 345 348 {ECO:0000244|PDB:5XZG}.
STRAND 352 354 {ECO:0000244|PDB:4K98}.
STRAND 355 358 {ECO:0000244|PDB:5XZG}.
HELIX 359 361 {ECO:0000244|PDB:4O6A}.
STRAND 363 366 {ECO:0000244|PDB:5XZG}.
HELIX 368 376 {ECO:0000244|PDB:5XZG}.
TURN 382 385 {ECO:0000244|PDB:5XZG}.
HELIX 394 411 {ECO:0000244|PDB:5XZG}.
HELIX 413 415 {ECO:0000244|PDB:5XZG}.
HELIX 420 433 {ECO:0000244|PDB:5XZG}.
HELIX 437 440 {ECO:0000244|PDB:5XZG}.
HELIX 442 444 {ECO:0000244|PDB:5XZG}.
HELIX 445 462 {ECO:0000244|PDB:5XZG}.
STRAND 468 470 {ECO:0000244|PDB:4O6A}.
TURN 478 480 {ECO:0000244|PDB:5XZG}.
HELIX 483 498 {ECO:0000244|PDB:5XZG}.
HELIX 502 504 {ECO:0000244|PDB:5XZG}.
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


Related products :

Catalog number Product name Quantity
cGAS-101AP Cyclic-GMP-AMP Synthase antibodies (m) WB control: PC-cGAS Host: Rabbit Affinity purifed 100-150ul
cGAS-112AP Cyclic-GMP-AMP Synthase antibodies (h) WB control: PC-cGAS Host: Rabbit Affinity purifed 100-150ul
cGAS-112AP Cyclic-GMP-AMP Synthase antibodies (h) Polyclonal anbtibody Host: Rabbit Affinity purifed 200ul
cGAS-101AP Cyclic-GMP-AMP Synthase antibodies (m) Polyclonal anbtibody Host: Rabbit Affinity purifed 200ul
cGAS-112AP Cyclic-GMP-AMP Synthase antibodies (h) Antigenic peptide: P-cGAS2 Host: Rabbit Affinity purifed 100ul
cGAS-101AP Cyclic-GMP-AMP Synthase antibodies (m) Antigenic peptide: P-cGAS1 Host: Rabbit Affinity purifed 100ul
cGAS-112AP Cyclic-GMP-AMP Synthase antibodies (h) FITC-conjugates: cGAS2-FITC Host: Rabbit Affinity purifed 200ul
cGAS-112AP Cyclic-GMP-AMP Synthase antibodies (h) Biotin Conjugates: cGAS2-Biotin Host: Rabbit Affinity purifed 200ul
cGAS-101AP Cyclic-GMP-AMP Synthase antibodies (m) Biotin Conjugates: cGAS1-Biotin Host: Rabbit Affinity purifed 200ul
cGAS-101AP Cyclic-GMP-AMP Synthase antibodies (m) FITC-conjugates: cGAS1-FITC Host: Rabbit Affinity purifed 200ul
EIAAB33197 CCDC139,Coiled-coil domain-containing protein 139,DOBI,Homo sapiens,Human,Psi55 synthase,PUS10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,t
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
EIAAB28570 (2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2
EIAAB33196 Ccdc139,Coiled-coil domain-containing protein 139,Mouse,Mus musculus,Psi55 synthase,Pus10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,tRNA-u
U0167h CLIA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin 96T
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167m CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167m ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T


https://antibody-antibodies.com/ | https://gentaur.com/ | https://gen-script.com/ | https://diagenox.com/ | https://clonagen.com/ | http://gentaursearch.com/ | http://gentaurpub.com/ | https://gentaur-online.com/ | http://anti-anti-pdf.com/ | http://gentaur-worldwide.com/

 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur