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NADPH oxidase 4 (EC 1.6.3.-) (Kidney oxidase-1) (KOX-1) (Kidney superoxide-producing NADPH oxidase) (Renal NAD(P)H-oxidase) (Superoxide-generating NADPH oxidase 4)

 NOX4_MOUSE              Reviewed;         578 AA.
Q9JHI8; Q3TF39; Q8C3M1; Q8VCA3;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-OCT-2018, entry version 119.
RecName: Full=NADPH oxidase 4;
EC=1.6.3.-;
AltName: Full=Kidney oxidase-1;
Short=KOX-1;
AltName: Full=Kidney superoxide-producing NADPH oxidase;
AltName: Full=Renal NAD(P)H-oxidase;
AltName: Full=Superoxide-generating NADPH oxidase 4;
Name=Nox4; Synonyms=Renox;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND ACTIVITY REGULATION.
TISSUE=Kidney;
PubMed=10869423; DOI=10.1073/pnas.130135897;
Geiszt M., Kopp J.B., Varnai P., Leto T.L.;
"Identification of renox, an NAD(P)H oxidase in kidney.";
Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11032835; DOI=10.1074/jbc.M007597200;
Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S.,
Hattori M., Sakaki Y., Sumimoto H.;
"A novel superoxide-producing NAD(P)H oxidase in kidney.";
J. Biol. Chem. 276:1417-1423(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=11098048; DOI=10.1074/jbc.M001004200;
Yang S., Madyastha P., Bingel S., Ries W., Key L.;
"A new superoxide-generating oxidase in murine osteoclasts.";
J. Biol. Chem. 276:5452-5458(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Banfi B., Maturana A., Demaurex N., Krause K.-H.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Heart, and Liver;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=FVB/N; TISSUE=Kidney;
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).
[7]
INDUCTION.
PubMed=15016652; DOI=10.1182/blood-2003-07-2240;
Suliman H.B., Ali M., Piantadosi C.A.;
"Superoxide dismutase-3 promotes full expression of the EPO response
to hypoxia.";
Blood 104:43-50(2004).
[8]
ACTIVITY REGULATION.
PubMed=15638999; DOI=10.1211/0022357055119;
Ding Y., Chen Z.-J., Liu S., Che D., Vetter M., Chang C.-H.;
"Inhibition of Nox-4 activity by plumbagin, a plant-derived bioactive
naphthoquinone.";
J. Pharm. Pharmacol. 57:111-116(2005).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15802177; DOI=10.1016/j.neuroscience.2004.12.038;
Vallet P., Charnay Y., Steger K., Ogier-Denis E., Kovari E.,
Herrmann F., Michel J.-P., Szanto I.;
"Neuronal expression of the NADPH oxidase NOX4, and its regulation in
mouse experimental brain ischemia.";
Neuroscience 132:233-238(2005).
-!- FUNCTION: Constitutive NADPH oxidase which generates superoxide
intracellularly upon formation of a complex with CYBA/p22phox.
Regulates signaling cascades probably through phosphatases
inhibition. May function as an oxygen sensor regulating the
KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate
insulin signaling cascade. May play a role in apoptosis, bone
resorption and lipolysaccharide-mediated activation of NFKB.
{ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:11098048}.
-!- ACTIVITY REGULATION: Activated by insulin. Inhibited by
diphenylene iodonium (By similarity). Inhibited by plumbagin.
Activated by phorbol 12-myristate 13-acetate (PMA). {ECO:0000250,
ECO:0000269|PubMed:10869423, ECO:0000269|PubMed:15638999}.
-!- SUBUNIT: Interacts with, relocalizes and stabilizes CYBA/p22phox.
Interacts with TLR4. Interacts with protein disulfide isomerase
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
junction, focal adhesion {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=May localize to plasma membrane and focal
adhesions. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9JHI8-1; Sequence=Displayed;
Name=2;
IsoId=Q9JHI8-2; Sequence=VSP_019060, VSP_019061;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9JHI8-3; Sequence=VSP_019063, VSP_019064;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9JHI8-4; Sequence=VSP_019062;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: EXpressed in brain, in all layers of the
cerebellum, in pyramidal cells of the Ammon horn and in Purkinje
cells (at protein level). Expressed in osteoclasts, leukocytes,
kidney, liver and lung. {ECO:0000269|PubMed:10869423,
ECO:0000269|PubMed:11098048, ECO:0000269|PubMed:15802177}.
-!- INDUCTION: Upon brain ischemia it is up-regulated in ischemic
tissues and more specially in neocapillaries (at protein level).
Up-regulated upon hypoxia. {ECO:0000269|PubMed:15016652,
ECO:0000269|PubMed:15802177}.
-!- PTM: N-glycosylation is required for the function. {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BC021378; Type=Frameshift; Positions=52; Evidence={ECO:0000305};
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EMBL; AF261944; AAF87573.1; -; mRNA.
EMBL; AB041034; BAA95682.1; -; mRNA.
EMBL; AB042745; BAB18134.1; -; mRNA.
EMBL; AF218723; AAF43142.1; -; mRNA.
EMBL; AF276957; AAK69443.1; -; mRNA.
EMBL; AK050371; BAC34215.1; -; mRNA.
EMBL; AK085509; BAC39460.1; -; mRNA.
EMBL; AK169304; BAE41059.1; -; mRNA.
EMBL; BC021378; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS21437.1; -. [Q9JHI8-1]
RefSeq; NP_056575.1; NM_015760.5. [Q9JHI8-1]
RefSeq; XP_006508075.1; XM_006508012.1. [Q9JHI8-4]
UniGene; Mm.31748; -.
ProteinModelPortal; Q9JHI8; -.
SMR; Q9JHI8; -.
STRING; 10090.ENSMUSP00000032781; -.
PeroxiBase; 5966; MmNOx04.
iPTMnet; Q9JHI8; -.
PhosphoSitePlus; Q9JHI8; -.
PaxDb; Q9JHI8; -.
PRIDE; Q9JHI8; -.
DNASU; 50490; -.
Ensembl; ENSMUST00000032781; ENSMUSP00000032781; ENSMUSG00000030562. [Q9JHI8-1]
Ensembl; ENSMUST00000068829; ENSMUSP00000070039; ENSMUSG00000030562. [Q9JHI8-3]
GeneID; 50490; -.
KEGG; mmu:50490; -.
UCSC; uc009ifj.2; mouse. [Q9JHI8-2]
UCSC; uc009ifl.2; mouse. [Q9JHI8-1]
UCSC; uc009ifm.2; mouse. [Q9JHI8-4]
CTD; 50507; -.
MGI; MGI:1354184; Nox4.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
GeneTree; ENSGT00550000074350; -.
HOGENOM; HOG000216669; -.
HOVERGEN; HBG003760; -.
InParanoid; Q9JHI8; -.
KO; K21423; -.
OMA; FCCGPNS; -.
OrthoDB; EOG091G09RV; -.
PhylomeDB; Q9JHI8; -.
TreeFam; TF105354; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:Q9JHI8; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030562; Expressed in 163 organ(s), highest expression level in adult mammalian kidney.
CleanEx; MM_NOX4; -.
ExpressionAtlas; Q9JHI8; baseline and differential.
Genevisible; Q9JHI8; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043020; C:NADPH oxidase complex; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0072341; F:modified amino acid binding; ISO:MGI.
GO; GO:0016174; F:NAD(P)H oxidase activity; ISO:MGI.
GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IMP:UniProtKB.
GO; GO:0045453; P:bone resorption; IMP:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
GO; GO:0007569; P:cell aging; IMP:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0010467; P:gene expression; ISO:MGI.
GO; GO:0003015; P:heart process; IGI:ARUK-UCL.
GO; GO:0050667; P:homocysteine metabolic process; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:ARUK-UCL.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; ISO:MGI.
Gene3D; 3.40.50.80; -; 1.
InterPro; IPR000778; Cyt_b245_heavy_chain.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00466; GP91PHOX.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane; NADP;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 578 NADPH oxidase 4.
/FTId=PRO_0000238981.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 62 Extracellular. {ECO:0000255}.
TRANSMEM 63 83 Helical. {ECO:0000255}.
TOPO_DOM 84 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 154 Extracellular. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 188 Cytoplasmic. {ECO:0000255}.
TRANSMEM 189 209 Helical. {ECO:0000255}.
TOPO_DOM 210 424 Extracellular. {ECO:0000255}.
TRANSMEM 425 445 Helical. {ECO:0000255}.
TOPO_DOM 446 578 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 303 Ferric oxidoreductase.
DOMAIN 304 419 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
REGION 248 575 Mediates interaction with TLR4.
{ECO:0000250}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 150 164 DPRKLLFTTIPGLTG -> VGGVCFSIFCSLVIR (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019060.
VAR_SEQ 165 578 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019061.
VAR_SEQ 358 358 M -> MLCQKRWQPWHSRVWIYSFFVCSDAACHEDTSKMNH
AFLL (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019062.
VAR_SEQ 540 540 K -> FEDQGQDFVPARKQHLHRGAPKALSFFSNGKGYLHF
TIMTLKKCCFHGSPLIF (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019063.
VAR_SEQ 541 578 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_019064.
CONFLICT 298 298 R -> G (in Ref. 5; BAC39460).
{ECO:0000305}.
SEQUENCE 578 AA; 66519 MW; 7887ADD40599A3D1 CRC64;
MAVSWRSWLA NEGVKHLCLL IWLSLNVLLF WKTFLLYNQG PEYYYIHQML GLGLCLSRAS
ASVLNLNCSL ILLPMCRTVL AYLRGSQKVP SRRTRRLLDK SKTLHITCGV TICIFSGVHV
AAHLVNALNF SVNYSEDFLE LNAARYQNED PRKLLFTTIP GLTGVCMVVV LFLMVTASTY
AIRVSNYDIF WYTHNLFFVF YMLLLLHVSG GLLKYQTNVD THPPGCISLN QTSSQNMSIP
DYVSEHFHGS LPRGFSKLED RYQKTLVKIC LEEPKFQAHF PQTWIWISGP LCLYCAERLY
RCIRSNKPVT IISVINHPSD VMELRMIKEN FKARPGQYII LHCPSVSALE NHPFTLTMCP
TETKATFGVH FKVVGDWTER FRDLLLPPSS QDSEILPFIH SRNYPKLYID GPFGSPFEES
LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFQ WFADLLCVLH
NKFWQENRPD FVNIQLYLSQ TDGIQKIIGE KYHTLNSRLF IGRPRWKLLF DEIAKCNRGK
TVGVFCCGPS SISKTLHSLS NRNNSYGTKF EYNKESFS


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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

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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
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IBAN lautet DE8839050000107569353
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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
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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