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Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)

 ZC12A_MOUSE             Reviewed;         596 AA.
Q5D1E7; Q3U8J3; Q3UE76; Q8JZW9; Q922T4;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 2.
07-JUN-2017, entry version 78.
RecName: Full=Endoribonuclease ZC3H12A {ECO:0000305};
EC=3.1.-.- {ECO:0000269|PubMed:19322177};
AltName: Full=Monocyte chemotactic protein-induced protein 1 {ECO:0000303|PubMed:21115689};
Short=MCP-induced protein 1 {ECO:0000303|PubMed:16574901};
Short=MCPIP-1 {ECO:0000303|PubMed:16574901};
AltName: Full=Regnase-1 {ECO:0000303|PubMed:26000482};
Short=Reg1 {ECO:0000303|PubMed:23706741};
AltName: Full=Zinc finger CCCH domain-containing protein 12A {ECO:0000312|MGI:MGI:2385891};
Name=Zc3h12a {ECO:0000303|PubMed:19322177,
ECO:0000312|MGI:MGI:2385891};
Synonyms=Mcpip {ECO:0000303|PubMed:16574901},
Mcpip1 {ECO:0000303|PubMed:19666473};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAX14018.1}
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND POSSIBLE INVOLVEMENT IN ISCHEMIC HEART DISEASE.
STRAIN=FVB/NJ {ECO:0000312|EMBL:AAX14018.1};
PubMed=16574901; DOI=10.1161/01.RES.0000220106.64661.71;
Zhou L., Azfer A., Niu J., Graham S., Choudhury M., Adamski F.M.,
Younce C., Binkley P.F., Kolattukudy P.E.;
"Monocyte chemoattractant protein-1 induces a novel transcription
factor that causes cardiac myocyte apoptosis and ventricular
dysfunction.";
Circ. Res. 98:1177-1185(2006).
[2] {ECO:0000312|EMBL:BAE25089.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25089.1}, and
NOD {ECO:0000312|EMBL:BAE42965.1};
TISSUE=Bone marrow macrophage {ECO:0000312|EMBL:BAE31025.1},
Embryonic stomach {ECO:0000312|EMBL:BAE25089.1},
Skin {ECO:0000312|EMBL:BAE36216.1}, and
Spleen {ECO:0000312|EMBL:BAE42965.1};
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] {ECO:0000312|EMBL:AAH36563.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II {ECO:0000312|EMBL:AAH36563.1}, and
FVB/N {ECO:0000312|EMBL:AAH06817.1};
TISSUE=Lung {ECO:0000312|EMBL:AAH36563.1}, and
Mammary gland {ECO:0000312|EMBL:AAH06817.1};
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]
FUNCTION IN INFLAMMATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=18178554; DOI=10.1074/jbc.M707861200;
Liang J., Wang J., Azfer A., Song W., Tromp G., Kolattukudy P.E.,
Fu M.;
"A novel CCCH-zinc finger protein family regulates proinflammatory
activation of macrophages.";
J. Biol. Chem. 283:6337-6346(2008).
[6]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=18682727; DOI=10.1371/journal.pone.0002880;
Liang J., Song W., Tromp G., Kolattukudy P.E., Fu M.;
"Genome-wide survey and expression profiling of CCCH-zinc finger
family reveals a functional module in macrophage activation.";
PLoS ONE 3:E2880-E2880(2008).
[7]
FUNCTION AS A TRANSCRIPTION FACTOR IN ADIPOGENESIS, AND INDUCTION.
PubMed=19666473; DOI=10.1074/jbc.M109.025320;
Younce C.W., Azfer A., Kolattukudy P.E.;
"MCP-1 (monocyte chemotactic protein-1)-induced protein, a recently
identified zinc finger protein, induces adipogenesis in 3T3-L1 pre-
adipocytes without peroxisome proliferator-activated receptor gamma.";
J. Biol. Chem. 284:27620-27628(2009).
[8]
FUNCTION AS AN ENDORIBONUCLEASE, CATALYTIC ACTIVITY, COFACTOR,
RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-141 AND CYS-306,
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=19322177; DOI=10.1038/nature07924;
Matsushita K., Takeuchi O., Standley D.M., Kumagai Y., Kawagoe T.,
Miyake T., Satoh T., Kato H., Tsujimura T., Nakamura H., Akira S.;
"Zc3h12a is an RNase essential for controlling immune responses by
regulating mRNA decay.";
Nature 458:1185-1190(2009).
[9]
FUNCTION IN INFLAMMATION, CATALYTIC ACTIVITY, INTERACTION WITH
UBIQUITIN, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-141;
CYS-157; ASP-278; ASP-279 AND CYS-306.
PubMed=21115689; DOI=10.1084/jem.20092641;
Liang J., Saad Y., Lei T., Wang J., Qi D., Yang Q., Kolattukudy P.E.,
Fu M.;
"MCP-induced protein 1 deubiquitinates TRAF proteins and negatively
regulates JNK and NF-kappaB signaling.";
J. Exp. Med. 207:2959-2973(2010).
[10]
FUNCTION IN STRESS GRANULE FORMATION, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF ASP-141; CYS-157; ASP-225 AND ASP-226.
PubMed=21971051; DOI=10.1074/jbc.M111.276006;
Qi D., Huang S., Miao R., She Z.G., Quinn T., Chang Y., Liu J.,
Fan D., Chen Y.E., Fu M.;
"Monocyte chemotactic protein-induced protein 1 (MCPIP1) suppresses
stress granule formation and determines apoptosis under stress.";
J. Biol. Chem. 286:41692-41700(2011).
[11]
FUNCTION IN INFLAMMATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21616078; DOI=10.1016/j.yjmcc.2011.04.018;
Niu J., Wang K., Graham S., Azfer A., Kolattukudy P.E.;
"MCP-1-induced protein attenuates endotoxin-induced myocardial
dysfunction by suppressing cardiac NF-kappaB activation via inhibition
of IkappaB kinase activation.";
J. Mol. Cell. Cardiol. 51:177-186(2011).
[12]
FUNCTION AS AN ENDORIBONUCLEASE, INTERACTION WITH BTRC; IKBKB AND
IRAK1, PHOSPHORYLATION AT SER-435 AND SER-439, TISSUE SPECIFICITY, AND
MUTAGENESIS OF SER-435 AND SER-439.
PubMed=22037600; DOI=10.1038/ni.2137;
Iwasaki H., Takeuchi O., Teraguchi S., Matsushita K., Uehata T.,
Kuniyoshi K., Satoh T., Saitoh T., Matsushita M., Standley D.M.,
Akira S.;
"The IkappaB kinase complex regulates the stability of cytokine-
encoding mRNA induced by TLR-IL-1R by controlling degradation of
regnase-1.";
Nat. Immunol. 12:1167-1175(2011).
[13]
FUNCTION IN ADIPOGENESIS.
PubMed=22739135; DOI=10.1159/000339066;
Younce C., Kolattukudy P.;
"MCP-1 induced protein promotes adipogenesis via oxidative stress,
endoplasmic reticulum stress and autophagy.";
Cell. Physiol. Biochem. 30:307-320(2012).
[14]
FUNCTION AS AN ENDORIBONUCLEASE, AND INDUCTION.
PubMed=23185455; DOI=10.1371/journal.pone.0049841;
Li M., Cao W., Liu H., Zhang W., Liu X., Cai Z., Guo J., Wang X.,
Hui Z., Zhang H., Wang J., Wang L.;
"MCPIP1 down-regulates IL-2 expression through an ARE-independent
pathway.";
PLoS ONE 7:E49841-E49841(2012).
[15]
FUNCTION IN T-CELL ACTIVATION, PROTEOLYTIC CLEAVAGE, DISRUPTION
PHENOTYPE, CONDITIONAL KNOCKOUT, AND MUTAGENESIS OF ARG-111; ARG-130;
ARG-136; ASP-141; ARG-158 AND ARG-214.
PubMed=23706741; DOI=10.1016/j.cell.2013.04.034;
Uehata T., Iwasaki H., Vandenbon A., Matsushita K.,
Hernandez-Cuellar E., Kuniyoshi K., Satoh T., Mino T., Suzuki Y.,
Standley D.M., Tsujimura T., Rakugi H., Isaka Y., Takeuchi O.,
Akira S.;
"Malt1-induced cleavage of regnase-1 in CD4(+) helper T cells
regulates immune activation.";
Cell 153:1036-1049(2013).
[16]
FUNCTION AS AN ENDORIBONUCLEASE IN INFLAMMATION, INTERACTION WITH
UPF1, ASSOCIATION WITH RIBOSOMES, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, CONDITIONAL KNOCKOUT, AND MUTAGENESIS OF ASP-141.
PubMed=26000482; DOI=10.1016/j.cell.2015.04.029;
Mino T., Murakawa Y., Fukao A., Vandenbon A., Wessels H.H., Ori D.,
Uehata T., Tartey S., Akira S., Suzuki Y., Vinuesa C.G., Ohler U.,
Standley D.M., Landthaler M., Fujiwara T., Takeuchi O.;
"Regnase-1 and Roquin regulate a common element in inflammatory mRNAs
by spatiotemporally distinct mechanisms.";
Cell 161:1058-1073(2015).
[17]
DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=26320658; DOI=10.1016/j.immuni.2015.07.021;
Garg A.V., Amatya N., Chen K., Cruz J.A., Grover P., Whibley N.,
Conti H.R., Hernandez Mir G., Sirakova T., Childs E.C.,
Smithgall T.E., Biswas P.S., Kolls J.K., McGeachy M.J.,
Kolattukudy P.E., Gaffen S.L.;
"MCPIP1 endoribonuclease activity negatively regulates interleukin-17-
mediated signaling and inflammation.";
Immunity 43:475-487(2015).
[18]
FUNCTION AS AN ENDORIBONUCLEASE.
PubMed=26134560; DOI=10.1074/jbc.M114.635870;
Huang S., Liu S., Fu J.J., Tony Wang T., Yao X., Kumar A., Liu G.,
Fu M.;
"Monocyte chemotactic protein-induced protein 1 and 4 form a complex
but act independently in regulation of interleukin-6 mRNA
degradation.";
J. Biol. Chem. 290:20782-20792(2015).
[19]
FUNCTION AS A ENDORIBONUCLEASE IN MACROPHAGE POLARIZATION, DISRUPTION
PHENOTYPE, CONDITIONAL KNOCKOUT, INDUCTION, DOMAIN, AND MUTAGENESIS OF
ASP-141.
PubMed=25934862; DOI=10.4049/jimmunol.1402797;
Kapoor N., Niu J., Saad Y., Kumar S., Sirakova T., Becerra E., Li X.,
Kolattukudy P.E.;
"Transcription factors STAT6 and KLF4 implement macrophage
polarization via the dual catalytic powers of MCPIP.";
J. Immunol. 194:6011-6023(2015).
-!- FUNCTION: Endoribonuclease involved in various biological
functions such as cellular inflammatory response and immune
homeostasis, glial differentiation of neuroprogenitor cells, cell
death of cardiomyocytes, adipogenesis and angiogenesis. Functions
as an endoribonuclease involved in mRNA decay (PubMed:26000482).
Modulates the inflammatory response by promoting the degradation
of a set of translationally active cytokine-induced inflammation-
related mRNAs, such as IL6 and IL12B, during the early phase of
inflammation (PubMed:19322177, PubMed:21115689, PubMed:23185455,
PubMed:26000482). Prevents aberrant T-cell-mediated immune
reaction by degradation of multiple mRNAs controlling T-cell
activation, such as those encoding cytokines (IL6 and IL2), cell
surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription
factor (REL) (PubMed:23706741). Self regulates by destabilizing
its own mRNA (PubMed:22037600). Cleaves mRNA harboring a stem-loop
(SL), often located in their 3'-UTRs, during the early phase of
inflammation in a helicase UPF1-dependent manner (PubMed:19322177,
PubMed:23185455, PubMed:23706741, PubMed:26000482,
PubMed:26134560). Plays a role in the inhibition of microRNAs
(miRNAs) biogenesis (By similarity). Cleaves the terminal loop of
a set of precursor miRNAs (pre-miRNAs) important for the
regulation of the inflammatory response leading to their
degradation, and thus preventing the biosynthesis of mature miRNAs
(By similarity). Plays also a role in promoting angiogenesis in
response to inflammatory cytokines by inhibiting the production of
antiangiogenic microRNAs via its anti-dicer RNase activity (By
similarity). Affects the overall ubiquitination of cellular
proteins (PubMed:21115689). Positively regulates deubiquitinase
activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains on TNF receptor-associated factors (TRAFs),
preventing JNK and NF-kappa-B signaling pathway activation, and
hence negatively regulating macrophage-mediated inflammatory
response and immune homeostasis (PubMed:21115689). Induces also
deubiquitination of the transcription factor HIF1A, probably
leading to its stabilization and nuclear import, thereby
positively regulating the expression of proangiogenic HIF1A-
targeted genes. Involved in a TANK-dependent negative feedback
response to attenuate NF-kappaB activation through the
deubiquitination of IKBKG or TRAF6 in response to interleukin-1-
beta (IL1B) stimulation or upon DNA damage (By similarity).
Prevents stress granules (SGs) formation and promotes macrophage
apoptosis under stress conditions, including arsenite-induced
oxidative stress, heat shock, and energy deprivation
(PubMed:21971051). Plays a role in the regulation of macrophage
polarization; promotes IL4-induced polarization of macrophages M1
into anti-inflammatory M2 state (PubMed:25934862). May also act as
a transcription factor that regulates the expression of multiple
genes involved in inflammatory response, angiogenesis,
adipogenesis and apoptosis (PubMed:18178554, PubMed:19666473,
PubMed:22739135). Functions as a positive regulator of glial
differentiation of neuroprogenitor cells through an amyloid
precursor protein (APP)-dependent signaling pathway (By
similarity). Attenuates septic myocardial contractile dysfunction
in response to lipopolysaccharide (LPS) by reducing I-kappa-B-
kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial
proinflammatory cytokine production (PubMed:21616078).
{ECO:0000250|UniProtKB:Q5D1E8, ECO:0000269|PubMed:18178554,
ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:19666473,
ECO:0000269|PubMed:21115689, ECO:0000269|PubMed:21616078,
ECO:0000269|PubMed:21971051, ECO:0000269|PubMed:22037600,
ECO:0000269|PubMed:22739135, ECO:0000269|PubMed:23185455,
ECO:0000269|PubMed:23706741, ECO:0000269|PubMed:25934862,
ECO:0000269|PubMed:26000482, ECO:0000269|PubMed:26134560}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:19322177};
Note=Mg(2+) is required for RNase activity (PubMed:19322177).
{ECO:0000269|PubMed:19322177};
-!- SUBUNIT: Oligomer (By similarity). Found in a deubiquitination
complex with TANK, USP10 and ZC3H12A; this complex inhibits
genotoxic stress- or interleukin-1-beta-mediated NF-kappaB
activation by promoting IKBKG or TRAF6 deubiquitination. Interacts
with IKBKG; this interaction increases in response to DNA damage.
Interacts with TANK; this interaction increases in response to DNA
damage and serves as a bridge to anchor both TANK and USP10 into a
deubiquitinating complex. Interacts with TRAF6; this interaction
increases in response to DNA damage and is stimulated by TANK.
Interacts with USP10; this interaction increases in response to
DNA damage and serves as a bridge to anchor both TANK and USP10
into a deubiquitinating complex. Interacts with ZC3H12D. Interacts
with TNRC6A. Interacts with IKBKB/IKKB. Interacts with IKBKB/IKKB
(By similarity). Interacts with IKBKB/IKKB (PubMed:22037600).
Interacts with BTRC; the interaction occurs when ZC3H12A is
phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600).
Interacts with IRAK1; this interaction increases the interaction
between ZC3H12A and IKBKB/IKKB (PubMed:22037600). Interacts with
UPF1; this interaction occurs in a mRNA translationally
active- and termination-dependent manner and is essential for
ZC3H12A-mediated degradation of target mRNAs (PubMed:26000482).
Associates with ribosomes (PubMed:26000482). Interacts with
ubiquitin (PubMed:21115689). {ECO:0000250|UniProtKB:Q5D1E8,
ECO:0000269|PubMed:21115689, ECO:0000269|PubMed:22037600,
ECO:0000269|PubMed:26000482}.
-!- INTERACTION:
O14920:IKBKB (xeno); NbExp=4; IntAct=EBI-5326026, EBI-81266;
P51617:IRAK1 (xeno); NbExp=3; IntAct=EBI-5326026, EBI-358664;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574901,
ECO:0000269|PubMed:19322177}. Cytoplasm
{ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:21971051,
ECO:0000269|PubMed:26000482}. Rough endoplasmic reticulum membrane
{ECO:0000269|PubMed:26000482}; Peripheral membrane protein
{ECO:0000269|PubMed:26000482}; Cytoplasmic side
{ECO:0000269|PubMed:26000482}. Cytoplasmic granule
{ECO:0000269|PubMed:21971051}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:Q5D1E8}. Note=Predominantly localized in
the cytoplasm (PubMed:19322177). Colocalizes with GW182 on many
granule-like structures, probably corresponding to cytoplasmic GW
bodies (GWBs), also called processing bodies (P bodies)
(PubMed:21971051). Colocalizes with calnexin on the surface of the
rough endoplasmic reticulum (RER) membrane and with
translationally active polysomes (PubMed:26000482). Colocalizes
with ZC3H12D in cytoplasmic mRNA processing P-body, also known as
GW bodies (GWBs) (By similarity). {ECO:0000250|UniProtKB:Q5D1E8,
ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:21971051,
ECO:0000269|PubMed:26000482}.
-!- TISSUE SPECIFICITY: Highly expressed in macrophages
(PubMed:18178554). Expressed in lung, lymph nodes, spleen and
thymus (PubMed:22037600). Expressed weakly in heart
(PubMed:21616078). Expressed weakly in cardiomyocytes (at protein
level) (PubMed:16574901). Expressed in spleen, lung, intestine,
brown adipose tissue and thymus (PubMed:18682727). Weakly
expressed in the heart (PubMed:16574901). Weakly expressed in
cardiomyocytes (PubMed:16574901). {ECO:0000269|PubMed:16574901,
ECO:0000269|PubMed:18178554, ECO:0000269|PubMed:18682727,
ECO:0000269|PubMed:21616078, ECO:0000269|PubMed:22037600}.
-!- INDUCTION: Up-regulated by the transcription factor KLF4 in a
interleukin IL4-dependent manner in macrophage (PubMed:25934862).
Up-regulated by lipopolysaccharide (LPS) (at protein level)
(PubMed:21616078). Up-regulated by chemokine CCL2 during
adipocytes differentiation (PubMed:19666473). Up-regulated in
activated T lymphocytes (PubMed:23185455). Up-regulated in
response to lipopolysaccharide (LPS) in a MyD88-dependent manner
in macrophages (PubMed:18178554, PubMed:18682727,
PubMed:19322177). Up-regulated by phorbol 13-acetate 12-myristate
(PMA) in primary T lymphocytes (PubMed:23185455). Up-regulated by
interleukin IL17 in keratinocytes (PubMed:26320658).
{ECO:0000269|PubMed:18178554, ECO:0000269|PubMed:18682727,
ECO:0000269|PubMed:19322177, ECO:0000269|PubMed:19666473,
ECO:0000269|PubMed:21616078, ECO:0000269|PubMed:23185455,
ECO:0000269|PubMed:25934862, ECO:0000269|PubMed:26320658}.
-!- DOMAIN: The C3H1-type zinc finger domain and C-terminal region are
necessary for pre-miRNA binding (By similarity). The C-terminal
region and proline-rich domain are necessary for oligomerization
(By similarity). {ECO:0000250|UniProtKB:Q5D1E8}.
-!- PTM: Proteolytically cleaved between Arg-111 and Arg-214 by MALT1
in activated T-cells; cleavage at Arg-111 is critical for
promoting ZC3H12A degradation in response to T-cell receptor (TCR)
stimulation, and hence is necessary for prolonging the stability
of a set of mRNAs controlling T-cell activation (PubMed:23706741).
{ECO:0000269|PubMed:23706741}.
-!- PTM: Phosphorylated by IRAK1; phosphorylation is necessary for
subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex.
Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439
upon lipopolysaccharide (LPS) or IL1B stimulation in macrophages
through the MyD88-dependent signaling pathway; these
phosphorylations promote rapid ubiquitin proteasome-mediated
degradation of ZC3H12A in macrophages and hence allows its target
mRNAs, such as IL6, to escape from degradation and accumulate
during the inflammatory response (PubMed:22037600).
{ECO:0000269|PubMed:22037600}.
-!- PTM: Ubiquitinated; ubiquitination is induced in response to
interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-
dependent manner, leading to proteasome-mediated degradation
(PubMed:22037600). {ECO:0000269|PubMed:22037600}.
-!- DISEASE: Note=Increased expression of ZC3H12A is associated with
ischemic heart disease (PubMed:16574901).
{ECO:0000269|PubMed:16574901}.
-!- DISRUPTION PHENOTYPE: Most mice die within the first 12 weeks
(PubMed:21115689). Show severe inflammatory syndromes, including
growth retardation, splenomegaly and lymphoadenopathy
(PubMed:19322177, PubMed:21115689). show systemic inflammation
characterized by T-cell and B-cell activation (PubMed:23706741).
Exhibit greatly increased levels of plasma cells and infiltration
of plasma cells into the lungs (PubMed:19322177, PubMed:21115689).
Show elevated serum immunoglobulin levels and produce anti-nuclear
autoantibodies (PubMed:19322177, PubMed:23706741). Mice show
increased production of proinflammatory cytokine mRNAs and
secreted protein levels, such as IL6, TNF and PTGS2 expression
upon lipopolysaccharide (LPS) stimulation in bone marrow
macrophages (BBMs) or embryonic fibroblasts, particularly in the
early phase of the inflammatory response (PubMed:21115689,
PubMed:26000482). Show impaired degradation of IL6 mRNA
(PubMed:19322177, PubMed:21115689). Show an increased in both JNK
and NF-kappa-B signaling pathway activations upon LPS stimulation
(PubMed:21115689). Show an increase in global ubiquitinated
protein level in splenocytes (PubMed:21115689). Display a drastic
increase in both basal and LPS- or TNF-induced ubiquitination of
TRAF2, TRAF3 and TRAF6 in splenocytes (PubMed:21115689).
Splenocytes show spontaneously formed aggregation of stress
granules (SGs) and were resistant to stress-induced apoptosis
(PubMed:21971051). Heterozygous knockout mice display IL-17-
dependent enhanced resistance to disseminated Candida albicans
infection compared to wild-type mice (PubMed:26320658). Double
knockout of ZC3H12A and RC3H1 result in embryonic developmental
arrest and death; embryonic fibroblasts from these mice show a
higher increase in IL6, TNF and PTGS2 expression upon LPS
stimulation, both in early and late phases of the responses,
compared to single knockout of either ZC3H12A or RC3H1
(PubMed:26000482). T-cell specific conditional knockout mice die
within the first 8 to 17 weeks after birth with the development of
severe splenomegaly and the development of a severe autoimmune
inflammatory disease (PubMed:23706741). Show massive increase in
effector/memory T-cells with elevated production of interferon
IFNG, interleukins IL17A and IL4 in response to phorbol 13-acetate
12-myristate (PMA) (PubMed:23706741). Proteolytic cleavage is
inhibited in T-cells in response to antigen stimulation
(PubMed:23706741). Conditional knockout in myeloid cells show
impairment in IL4-induced macrophage M2 polarization
(PubMed:25934862). {ECO:0000269|PubMed:19322177,
ECO:0000269|PubMed:21115689, ECO:0000269|PubMed:21971051,
ECO:0000269|PubMed:23706741, ECO:0000269|PubMed:25934862,
ECO:0000269|PubMed:26000482, ECO:0000269|PubMed:26320658}.
-!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY920404; AAX14018.1; -; mRNA.
EMBL; AK142501; BAE25089.1; -; mRNA.
EMBL; AK149698; BAE29035.1; -; mRNA.
EMBL; AK152196; BAE31025.1; -; mRNA.
EMBL; AK161150; BAE36216.1; -; mRNA.
EMBL; AK172357; BAE42965.1; -; mRNA.
EMBL; AL626775; CAM20905.1; -; Genomic_DNA.
EMBL; BC006817; AAH06817.1; -; mRNA.
EMBL; BC036563; AAH36563.1; -; mRNA.
CCDS; CCDS18638.1; -.
RefSeq; NP_694799.1; NM_153159.2.
UniGene; Mm.402; -.
PDB; 2N5J; NMR; -; A=45-89.
PDB; 2N5K; NMR; -; A=299-327.
PDB; 2N5L; NMR; -; A=544-596.
PDB; 5H9V; X-ray; 2.75 A; A/B/C/D=134-339.
PDB; 5H9W; X-ray; 2.60 A; A/B=134-339.
PDBsum; 2N5J; -.
PDBsum; 2N5K; -.
PDBsum; 2N5L; -.
PDBsum; 5H9V; -.
PDBsum; 5H9W; -.
ProteinModelPortal; Q5D1E7; -.
SMR; Q5D1E7; -.
IntAct; Q5D1E7; 4.
STRING; 10090.ENSMUSP00000037172; -.
iPTMnet; Q5D1E7; -.
PhosphoSitePlus; Q5D1E7; -.
EPD; Q5D1E7; -.
MaxQB; Q5D1E7; -.
PaxDb; Q5D1E7; -.
PRIDE; Q5D1E7; -.
Ensembl; ENSMUST00000036188; ENSMUSP00000037172; ENSMUSG00000042677.
GeneID; 230738; -.
KEGG; mmu:230738; -.
UCSC; uc008urw.2; mouse.
CTD; 80149; -.
MGI; MGI:2385891; Zc3h12a.
eggNOG; KOG3777; Eukaryota.
eggNOG; ENOG410ZNK1; LUCA.
GeneTree; ENSGT00750000117218; -.
HOGENOM; HOG000060218; -.
HOVERGEN; HBG108758; -.
InParanoid; Q5D1E7; -.
KO; K18668; -.
OMA; FPPREYW; -.
OrthoDB; EOG091G03B2; -.
PhylomeDB; Q5D1E7; -.
TreeFam; TF315783; -.
PRO; PR:Q5D1E7; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000042677; -.
Genevisible; Q5D1E7; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISO:MGI.
GO; GO:0004540; F:ribonuclease activity; ISO:MGI.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:Ensembl.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:1990869; P:cellular response to chemokine; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:1904637; P:cellular response to ionomycin; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IDA:UniProtKB.
GO; GO:1903936; P:cellular response to sodium arsenite; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; ISO:MGI.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:MGI.
GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IDA:UniProtKB.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:BHF-UCL.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; IDA:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IDA:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IDA:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:BHF-UCL.
GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
GO; GO:0010884; P:positive regulation of lipid storage; IMP:BHF-UCL.
GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; IDA:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
GO; GO:1903003; P:positive regulation of protein deubiquitination; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
InterPro; IPR021869; RNase_Zc3h12_NYN.
Pfam; PF11977; RNase_Zc3h12a; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Apoptosis; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA damage; DNA-binding;
Endonuclease; Endoplasmic reticulum; Hydrolase; Immunity;
Inflammatory response; Magnesium; Membrane; Metal-binding;
Neurogenesis; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Stress response; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 596 Endoribonuclease ZC3H12A.
/FTId=PRO_0000341513.
ZN_FING 301 324 C3H1-type.
REGION 42 87 Ubiquitin association domain.
{ECO:0000305|PubMed:21115689}.
REGION 81 150 Necessary for interaction with TANK.
{ECO:0000250|UniProtKB:Q5D1E8}.
REGION 112 281 RNase. {ECO:0000250|UniProtKB:Q5D1E8}.
REGION 214 220 RNA binding.
{ECO:0000250|UniProtKB:Q5D1E8}.
REGION 301 454 Necessary for interaction with ZC3H12D.
{ECO:0000250|UniProtKB:Q5D1E8}.
COMPBIAS 476 533 Pro-rich. {ECO:0000255}.
METAL 226 226 Magnesium.
{ECO:0000250|UniProtKB:Q5D1E8}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E8}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000269|PubMed:22037600}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000269|PubMed:22037600}.
MUTAGEN 111 111 R->A: Loss of MALT1-dependent cleavage
and degradation in T-cells.
{ECO:0000269|PubMed:23706741}.
MUTAGEN 130 130 R->A: Reduces MALT1-dependent cleavage
and degradation in T-cells.
{ECO:0000269|PubMed:23706741}.
MUTAGEN 136 136 R->A: Reduces MALT1-dependent cleavage
and degradation in T-cells.
{ECO:0000269|PubMed:23706741}.
MUTAGEN 141 141 D->N: Loss of RNase activity. Loss of
mRNAs and miRNAs degradation. Loss of
protein deubiquitination and suppression
of inhibition on JNK and NF-kappa-B
signaling pathway activation. Inhibits
induction of angiogenesis and macrophage
M2 polarization. Mislocalized in stress
granule (SG). Loss of the ability to
inhibit SG formation under stress. Does
not inhibit binding to IL6 mRNA.
{ECO:0000269|PubMed:19322177,
ECO:0000269|PubMed:21115689,
ECO:0000269|PubMed:21971051,
ECO:0000269|PubMed:23706741,
ECO:0000269|PubMed:25934862,
ECO:0000269|PubMed:26000482}.
MUTAGEN 157 157 C->A: Loss of protein deubiquitination
and suppression of inhibition on JNK and
NF-kappa-B signaling pathway activation.
Loss of the ability to inhibit stress
granule (SG) formation. No loss of RNase
activity. {ECO:0000269|PubMed:21115689,
ECO:0000269|PubMed:21971051}.
MUTAGEN 158 158 R->A: Reduces MALT1-dependent cleavage
and degradation in T-cells.
{ECO:0000269|PubMed:23706741}.
MUTAGEN 214 214 R->A: Reduces MALT1-dependent cleavage
and degradation in T-cells.
{ECO:0000269|PubMed:23706741}.
MUTAGEN 225 225 D->A: Loss of RNase activity, no loss of
protein deubiquitination and ability to
inhibit stress granule (SG) formation
under stress; when associated with A-226.
{ECO:0000269|PubMed:21971051}.
MUTAGEN 226 226 D->A: Loss of RNase activity and no loss
of protein deubiquitination; when
associated with A-226.
{ECO:0000269|PubMed:21971051}.
MUTAGEN 278 278 D->A: Loss of inhibition on JNK and NF-
kappa-B signaling pathway activation;
when associated with A-279.
{ECO:0000269|PubMed:21115689}.
MUTAGEN 279 279 D->A: Loss of inhibition on JNK and NF-
kappa-B signaling pathway activation;
when associated with A-278.
{ECO:0000269|PubMed:21115689}.
MUTAGEN 306 306 C->R: Loss of protein deubiquitination
and suppression of inhibition on JNK and
NF-kappa-B signaling pathway activations.
No loss of RNase activity.
{ECO:0000269|PubMed:19322177,
ECO:0000269|PubMed:21115689}.
MUTAGEN 435 435 S->A: Reduces its phosphorylation status,
does not interact with IKBKB/IKKB and
BTRC, inhibits IL6 mRNA instability and
IKK-mediated degradation of ZC3H12A; when
associated with A-439.
{ECO:0000269|PubMed:22037600}.
MUTAGEN 439 439 S->A: Reduces its phosphorylation status,
does not interact with IKBKB/IKKB and
BTRC, inhibits IL6 mRNA instability and
IKK-mediated degradation of ZC3H12A; when
associated with A-435.
CONFLICT 280 280 P -> H (in Ref. 2; BAE29035).
{ECO:0000305}.
CONFLICT 315 315 G -> E (in Ref. 1; AAX14018).
{ECO:0000305}.
HELIX 47 58 {ECO:0000244|PDB:2N5J}.
HELIX 62 72 {ECO:0000244|PDB:2N5J}.
HELIX 78 88 {ECO:0000244|PDB:2N5J}.
STRAND 138 141 {ECO:0000244|PDB:5H9W}.
HELIX 142 148 {ECO:0000244|PDB:5H9W}.
STRAND 149 151 {ECO:0000244|PDB:5H9W}.
STRAND 154 156 {ECO:0000244|PDB:5H9W}.
HELIX 157 169 {ECO:0000244|PDB:5H9W}.
STRAND 175 180 {ECO:0000244|PDB:5H9W}.
HELIX 181 184 {ECO:0000244|PDB:5H9W}.
STRAND 193 195 {ECO:0000244|PDB:5H9W}.
HELIX 198 204 {ECO:0000244|PDB:5H9W}.
STRAND 208 211 {ECO:0000244|PDB:5H9W}.
STRAND 213 216 {ECO:0000244|PDB:5H9W}.
STRAND 219 222 {ECO:0000244|PDB:5H9W}.
HELIX 225 236 {ECO:0000244|PDB:5H9W}.
STRAND 239 241 {ECO:0000244|PDB:5H9W}.
HELIX 247 252 {ECO:0000244|PDB:5H9W}.
HELIX 254 263 {ECO:0000244|PDB:5H9W}.
STRAND 268 270 {ECO:0000244|PDB:5H9W}.
STRAND 273 275 {ECO:0000244|PDB:5H9W}.
STRAND 283 285 {ECO:0000244|PDB:5H9W}.
HELIX 288 291 {ECO:0000244|PDB:5H9W}.
STRAND 301 304 {ECO:0000244|PDB:2N5K}.
STRAND 323 325 {ECO:0000244|PDB:2N5K}.
HELIX 546 557 {ECO:0000244|PDB:2N5L}.
TURN 558 560 {ECO:0000244|PDB:2N5L}.
HELIX 563 572 {ECO:0000244|PDB:2N5L}.
HELIX 581 592 {ECO:0000244|PDB:2N5L}.
SEQUENCE 596 AA; 65598 MW; 420E116564B70212 CRC64;
MSDPCGTKPV QESNPTMSLW SLEDRHSSQG RPQPDQDPVA KEAPTSELQM KVDFFRKLGY
SSSEIHSVLQ KLGVQADTNT VLGELVKHGS ATERECQALT APSPQPPLVP RGGSTPKPST
LEPSLPEEDR EGSDLRPVVI DGSNVAMSHG NKEVFSCRGI LLAVNWFLER GHTDITVFVP
SWRKEQPRPD VPITDQHILR ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAFESDGVV
VSNDTYRDLQ GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLPSE
HRKQPCPYGK KCTYGIKCRF FHPERPSRPQ RSVADELRAN ALLSPPRTPV KDKSSQRPSP
ASQSSSVSLE AEPGSLDGKK LGARSSPGPH REGSPQTCAP AGRSLPVSGG SFGPTEWLAH
TQDSLPYTSQ ECLDSGIGSL ESQMSELWGV RGGSPGESGP TRGPYAGYHS YGSKVPAAPS
FSPFRPAMGA GHFSVPTDYV PPPPTYPSRE YWSEPYPLPP PTPVLQEPQR PSPGAGGGPW
GRVGDLAKER AGVYTKLCGV FPPHLVEAVM RRFPQLLDPQ QLAAEILSYK SQHLSE


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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