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Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]

 CASP8_MOUSE             Reviewed;         480 AA.
O89110; O35669;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 167.
RecName: Full=Caspase-8;
Short=CASP-8;
EC=3.4.22.61;
Contains:
RecName: Full=Caspase-8 subunit p18;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=Casp8;
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 [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
STRAIN=129/SvJ;
PubMed=9654089; DOI=10.1046/j.1432-1327.1998.2530399.x;
Sakamaki K., Tsukumo S., Yonehara S.;
"Molecular cloning and characterization of mouse caspase-8.";
Eur. J. Biochem. 253:399-405(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND ENZYME REGULATION.
PubMed=9837723; DOI=10.1006/jmbi.1998.2226;
Van de Craen M., Van Loo G., Declercq W., Schotte P.,
van den Brande I., Mandruzzato S., van der Bruggen P., Fiers W.,
Vandenabeele P.;
"Molecular cloning and identification of murine caspase-8.";
J. Mol. Biol. 284:1017-1026(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 57-476.
Kioschis P., Kischkel F., Poustka A., Krammer P.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH NOL3.
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
[6]
INTERACTION WITH CASP8AP2.
PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
"FLASH links the CD95 signaling pathway to the cell nucleus and
nuclear bodies.";
EMBO J. 26:391-401(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
INTERACTION WITH TNFAIP8L2.
PubMed=18455983; DOI=10.1016/j.cell.2008.03.026;
Sun H., Gong S., Carmody R.J., Hilliard A., Li L., Sun J., Kong L.,
Xu L., Hilliard B., Hu S., Shen H., Yang X., Chen Y.H.;
"TIPE2, a negative regulator of innate and adaptive immunity that
maintains immune homeostasis.";
Cell 133:415-426(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-226, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Most upstream protease of the activation cascade of
caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A
induced cell death. Binding to the adapter molecule FADD recruits
it to either receptor. The resulting aggregate called death-
inducing signaling complex (DISC) performs CASP8 proteolytic
activation. The active dimeric enzyme is then liberated from the
DISC and free to activate downstream apoptotic proteases.
Proteolytic fragments of the N-terminal propeptide (termed CAP3,
CAP5 and CAP6) are likely retained in the DISC. Cleaves and
activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May
participate in the GZMB apoptotic pathways. Cleaves ADPRT.
Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC.
Likely target for the cowpox virus CRMA death inhibitory protein.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at position P1 and
has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
(Gly/Ser/Ala).
-!- ENZYME REGULATION: Inhibited by CRMA and P35.
{ECO:0000269|PubMed:9837723}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 18 kDa (p18) and a 10
kDa (p10) subunit. Interacts with FADD, CFLAR and PEA15. Interacts
with RFFL and RNF34; negatively regulate CASP8 through proteasomal
degradation (By similarity). Interacts with TNFAIP8L2. Interacts
with CASP8AP2. Interacts with NOL3; decreases CASP8 activity in a
mitochondria localization- and phosphorylation-dependent manner
and this interaction is dissociated by calcium.
{ECO:0000250|UniProtKB:Q14790, ECO:0000250|UniProtKB:Q9JHX4,
ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:17245429,
ECO:0000269|PubMed:18455983}.
-!- INTERACTION:
P19091:Ar; NbExp=2; IntAct=EBI-851690, EBI-1776062;
Q61160:Fadd; NbExp=6; IntAct=EBI-851690, EBI-524415;
P25446:Fas; NbExp=3; IntAct=EBI-851690, EBI-296206;
P01375:TNF (xeno); NbExp=2; IntAct=EBI-851690, EBI-359977;
Q9D8Y7:Tnfaip8l2; NbExp=2; IntAct=EBI-851690, EBI-1781612;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
Highest expression in spleen, thymus, lung, liver and kidney.
Lower expression in heart, brain, testis and skeletal muscle.
-!- DEVELOPMENTAL STAGE: In the embryo, highest expression occurs at
day 7.
-!- PTM: Generation of the subunits requires association with the
death-inducing signaling complex (DISC), whereas additional
processing is likely due to the autocatalytic activity of the
activated protease. GZMB and CASP10 can be involved in these
processing events (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation on Ser-389 during mitosis by CDK1 inhibits
activation by proteolysis and prevents apoptosis. This
phosphorylation occurs in cancer cell lines, as well as in primary
breast tissues and lymphocytes (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; AF067841; AAC40132.1; -; Genomic_DNA.
EMBL; AF067835; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067836; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067837; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067838; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067839; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067840; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067834; AAC40131.1; -; mRNA.
EMBL; AJ007749; CAA07677.1; -; mRNA.
EMBL; BC006737; AAH06737.1; -; mRNA.
EMBL; BC049955; AAH49955.1; -; mRNA.
EMBL; AJ000641; CAA04196.1; -; mRNA.
CCDS; CCDS14979.1; -.
RefSeq; NP_001073595.1; NM_001080126.1.
RefSeq; NP_033942.1; NM_009812.2.
UniGene; Mm.336851; -.
ProteinModelPortal; O89110; -.
SMR; O89110; -.
BioGrid; 198500; 7.
DIP; DIP-37435N; -.
IntAct; O89110; 8.
MINT; MINT-91569; -.
STRING; 10090.ENSMUSP00000027189; -.
MEROPS; C14.009; -.
iPTMnet; O89110; -.
PhosphoSitePlus; O89110; -.
EPD; O89110; -.
PaxDb; O89110; -.
PeptideAtlas; O89110; -.
PRIDE; O89110; -.
Ensembl; ENSMUST00000027189; ENSMUSP00000027189; ENSMUSG00000026029.
Ensembl; ENSMUST00000165549; ENSMUSP00000127375; ENSMUSG00000026029.
GeneID; 12370; -.
KEGG; mmu:12370; -.
UCSC; uc007bcs.1; mouse.
CTD; 841; -.
MGI; MGI:1261423; Casp8.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000276884; -.
HOVERGEN; HBG050803; -.
InParanoid; O89110; -.
KO; K04398; -.
PhylomeDB; O89110; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.61; 3474.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-140534; Ligand-dependent caspase activation.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-2562578; TRIF-mediated programmed cell death.
Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-MMU-3371378; Regulation by c-FLIP.
Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-MMU-5218900; CASP8 activity is inhibited.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5660668; CLEC7A/inflammasome pathway.
Reactome; R-MMU-69416; Dimerization of procaspase-8.
Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
Reactome; R-MMU-75153; Apoptotic execution phase.
Reactome; R-MMU-75157; FasL/ CD95L signaling.
Reactome; R-MMU-75158; TRAIL signaling.
PRO; PR:O89110; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026029; -.
CleanEx; MM_CASP8; -.
ExpressionAtlas; O89110; baseline and differential.
Genevisible; O89110; MM.
GO; GO:0031265; C:CD95 death-inducing signaling complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0030690; C:Noc1p-Noc2p complex; IMP:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:MGI.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0035877; F:death effector domain binding; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0048738; P:cardiac muscle tissue development; TAS:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
GO; GO:0001841; P:neural tube formation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:2001233; P:regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0070243; P:regulation of thymocyte apoptotic process; IGI:MGI.
GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:MGI.
CDD; cd00032; CASc; 1.
InterPro; IPR033170; Caspase-8.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF162; PTHR10454:SF162; 1.
Pfam; PF01335; DED; 2.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
Zymogen.
PROPEP 1 218 {ECO:0000250}.
/FTId=PRO_0000004632.
CHAIN 219 376 Caspase-8 subunit p18.
/FTId=PRO_0000004633.
PROPEP 377 387 {ECO:0000250}.
/FTId=PRO_0000004634.
CHAIN 388 480 Caspase-8 subunit p10.
/FTId=PRO_0000004635.
DOMAIN 3 80 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 101 177 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 319 319 {ECO:0000250}.
ACT_SITE 362 362 {ECO:0000250}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 226 226 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 336 336 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14790}.
MOD_RES 389 389 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q14790}.
CONFLICT 68 71 HISR -> PHPVG (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 94 99 DNAQIS -> RQCPRFL (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 96 96 A -> V (in Ref. 2; CAA07677).
{ECO:0000305}.
CONFLICT 103 107 VMLFK -> SCSFR (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 475 475 K -> N (in Ref. 4; CAA04196).
{ECO:0000305}.
SEQUENCE 480 AA; 55357 MW; 045268AE3DE5ED4F CRC64;
MDFQSCLYAI AEELGSEDLA ALKFLCLDYI PHKKQETIED AQKLFLRLRE KGMLEEGNLS
FLKELLFHIS RWDLLVNFLD CNREEMVREL RDPDNAQISP YRVMLFKLSE EVSELELRSF
KFLLNNEIPK CKLEDDLSLL EIFVEMEKRT MLAENNLETL KSICDQVNKS LLGKIEDYER
SSTERRMSLE GREELPPSVL DEMSLKMAEL CDSPREQDSE SRTSDKVYQM KNKPRGYCLI
INNHDFSKAR EDITQLRKMK DRKGTDCDKE ALSKTFKELH FEIVSYDDCT ANEIHEILEG
YQSADHKNKD CFICCILSHG DKGVVYGTDG KEASIYDLTS YFTGSKCPSL SGKPKIFFIQ
ACQGSNFQKG VPDEAGFEQQ NHTLEVDSSS HKNYIPDEAD FLLGMATVKN CVSYRDPVNG
TWYIQSLCQS LRERCPQGDD ILSILTGVNY DVSNKDDRRN KGKQMPQPTF TLRKKLFFPP


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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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
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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