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Cell death activator CIDE-3 (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27)

 CIDEC_MOUSE             Reviewed;         239 AA.
P56198; Q499X5; Q8BNV7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
12-SEP-2018, entry version 115.
RecName: Full=Cell death activator CIDE-3;
AltName: Full=Cell death-inducing DFFA-like effector protein C;
AltName: Full=Fat-specific protein FSP27;
Name=Cidec; Synonyms=Fsp27;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=1339452;
Danesch U., Hoeck W., Ringold G.M.;
"Cloning and transcriptional regulation of a novel adipocyte-specific
gene, FSP27. CAAT-enhancer-binding protein (C/EBP) and C/EBP-like
proteins interact with sequences required for differentiation-
dependent expression.";
J. Biol. Chem. 267:7185-7193(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
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 MRNA].
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).
[5]
TISSUE SPECIFICITY.
PubMed=12910269; DOI=10.1038/ng1225;
Zhou Z., Yon Toh S., Chen Z., Guo K., Ng C.P., Ponniah S., Lin S.C.,
Hong W., Li P.;
"Cidea-deficient mice have lean phenotype and are resistant to
obesity.";
Nat. Genet. 35:49-56(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=18334488; DOI=10.1074/jbc.M708323200;
Keller P., Petrie J.T., De Rose P., Gerin I., Wright W.S.,
Chiang S.H., Nielsen A.R., Fischer C.P., Pedersen B.K.,
MacDougald O.A.;
"Fat-specific protein 27 regulates storage of triacylglycerol.";
J. Biol. Chem. 283:14355-14365(2008).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
PubMed=18654663; DOI=10.1172/JCI34090;
Nishino N., Tamori Y., Tateya S., Kawaguchi T., Shibakusa T.,
Mizunoya W., Inoue K., Kitazawa R., Kitazawa S., Matsuki Y.,
Hiramatsu R., Masubuchi S., Omachi A., Kimura K., Saito M., Amo T.,
Ohta S., Yamaguchi T., Osumi T., Cheng J., Fujimoto T., Nakao H.,
Nakao K., Aiba A., Okamura H., Fushiki T., Kasuga M.;
"FSP27 contributes to efficient energy storage in murine white
adipocytes by promoting the formation of unilocular lipid droplets.";
J. Clin. Invest. 118:2808-2821(2008).
[8]
INDUCTION.
PubMed=18509062; DOI=10.1073/pnas.0802063105;
Puri V., Ranjit S., Konda S., Nicoloro S.M., Straubhaar J., Chawla A.,
Chouinard M., Lin C., Burkart A., Corvera S., Perugini R.A.,
Czech M.P.;
"Cidea is associated with lipid droplets and insulin sensitivity in
humans.";
Proc. Natl. Acad. Sci. U.S.A. 105:7833-7838(2008).
[9]
SUBCELLULAR LOCATION, UBIQUITINATION, INDUCTION, AND MUTAGENESIS OF
LYS-224; LYS-226 AND LYS-236.
PubMed=20089860; DOI=10.1074/jbc.M109.043786;
Nian Z., Sun Z., Yu L., Toh S.Y., Sang J., Li P.;
"Fat-specific protein 27 undergoes ubiquitin-dependent degradation
regulated by triacylglycerol synthesis and lipid droplet formation.";
J. Biol. Chem. 285:9604-9615(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-182; LYS-186
AND ARG-190.
PubMed=22144693; DOI=10.1083/jcb.201104142;
Gong J., Sun Z., Wu L., Xu W., Schieber N., Xu D., Shui G., Yang H.,
Parton R.G., Li P.;
"Fsp27 promotes lipid droplet growth by lipid exchange and transfer at
lipid droplet contact sites.";
J. Cell Biol. 195:953-963(2011).
[11]
FUNCTION AS A CEBPB COACTIVATOR, INTERACTION WITH CEBPB, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=22245780; DOI=10.1038/nm.2614;
Wang W., Lv N., Zhang S., Shui G., Qian H., Zhang J., Chen Y., Ye J.,
Xie Y., Shen Y., Wenk M.R., Li P.;
"Cidea is an essential transcriptional coactivator regulating mammary
gland secretion of milk lipids.";
Nat. Med. 18:235-243(2012).
[12]
FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION, SUBUNIT, INTERACTION
WITH PLIN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-46; LYS-53;
ARG-55; LYS-75; LYS-77; 86-GLU--ASP-88; 87-GLU-ASP-88; LYS-112;
LYS-115 AND LYS-117.
PubMed=23481402; DOI=10.1038/ncomms2581;
Sun Z., Gong J., Wu H., Xu W., Wu L., Xu D., Gao J., Wu J.W., Yang H.,
Yang M., Li P.;
"Perilipin1 promotes unilocular lipid droplet formation through the
activation of Fsp27 in adipocytes.";
Nat. Commun. 4:1594-1594(2013).
[13]
TISSUE SPECIFICITY, AND INDUCTION BY OSMOTIC STRESS.
PubMed=23233732; DOI=10.1194/jlr.M033365;
Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
"Fat-specific protein 27 modulates nuclear factor of activated T cells
5 and the cellular response to stress.";
J. Lipid Res. 54:734-743(2013).
-!- FUNCTION: Binds to lipid droplets and regulates their enlargement,
thereby restricting lipolysis and favoring storage. At focal
contact sites between lipid droplets, promotes directional net
neutral lipid transfer from the smaller to larger lipid droplets.
The transfer direction may be driven by the internal pressure
difference between the contacting lipid droplet pair. Its role in
neutral lipid transfer and lipid droplet enlargement is activated
by the interaction with PLIN1. May act as a CEBPB coactivator in
the white adipose tissue to control the expression of a subset of
CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1,
TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces
apoptosis or increases cell susceptibility to apoptosis induced by
serum deprivation or TGFB treatment. As mature adipocytes, that
express high CIDEC levels, are quite resistant to apoptotic
stimuli, the physiological significance of its role in apoptosis
is unclear. May play a role in the modulation of the response to
osmotic stress by preventing NFAT5 to translocate into the nucleus
and activate its target genes expression.
{ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:22144693,
ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23481402}.
-!- SUBUNIT: Homodimer. Interacts with CIDEA. Interacts with NFAT5;
this interaction is direct and retains NFAT5 in the cytoplasm (By
similarity). Interacts with CEBPB. Interacts with PLIN1.
{ECO:0000250, ECO:0000269|PubMed:22245780,
ECO:0000269|PubMed:23481402}.
-!- SUBCELLULAR LOCATION: Lipid droplet. Endoplasmic reticulum.
Nucleus. Note=Diffuses quickly on lipid droplet surface, but
becomes trapped and clustered at lipid droplet contact sites,
thereby enabling its rapid enrichment at lipid droplet contact
sites.
-!- TISSUE SPECIFICITY: Expressed almost exclusively in adipose
tissue, including subcutaneous and epididymal white adipose tissue
(at protein level). Although abundantly present in brown adipose
tissue at the mRNA level, the protein is almost undetectable in
this tissue (PubMed:18654663), or at moderate levels
(PubMed:22245780, PubMed:12910269). Expressed in the mammary
gland, in stromal adipose tissue, but becomes undetectable at the
end of pregnancy and during lactation (at protein level).
Expressed at low levels in skeletal muscle and heart.
{ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:1339452,
ECO:0000269|PubMed:18654663, ECO:0000269|PubMed:22245780,
ECO:0000269|PubMed:23233732}.
-!- DEVELOPMENTAL STAGE: Up-regulated during differentiation into
adipocytes in various cell lines, including TA1 and 3T3-L1.
Decreases in the mammary gland during pregnancy from day 14.5
until 18.5, when it becomes hardly detectable, and during
lactation. {ECO:0000269|PubMed:1339452,
ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18654663,
ECO:0000269|PubMed:22245780}.
-!- INDUCTION: Up-regulated under conditions that enhance
triacylglycerol deposition, including rosiglitazone treatment and
high-fat diet. This up-regulation is mediated by PPARG. Up-
regulated by isoproterenol, a beta-agonist, and oleic acid
treatment. This induction is due to protein stabilization. Down-
regulated upon hypertonic conditions.
{ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:20089860,
ECO:0000269|PubMed:23233732}.
-!- DOMAIN: The CIDE-N domain is involved in homodimerization which is
crucial for its function in promoting lipid exchange and transfer.
{ECO:0000269|PubMed:23481402}.
-!- PTM: Ubiquitinated and targeted to proteasomal degradation,
resulting in a short half-life (about 15 minutes in 3T3-L1 cells).
Protein stability depends on triaclyglycerol synthesis, fatty acid
availability and lipid droplet formation.
{ECO:0000269|PubMed:20089860}.
-!- DISRUPTION PHENOTYPE: Mutant animals are born in a Mendelian ratio
and appear physically normal at birth. The body weights of wild-
type and mutant mice fed a standard diet do not differ up to 14
weeks of age, nor does food intake. From 16 weeks of age, the body
weight of mutant mice significantly decreases compared with that
of wild-type mice. When animals are fed a high-fat diet, the gain
in body weight is significantly smaller for mutant mice than for
wild-type. Under these feeding conditions, mutant mice are also
protected from insulin resistance and from accumulation of fat in
the liver. The body temperature do not differ significantly
between mutant and wild-type mice maintained at room temperature,
but the basal rate of oxygen consumption is significantly
increased in mutants. {ECO:0000269|PubMed:18654663}.
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EMBL; M61737; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK080133; BAC37830.1; -; mRNA.
EMBL; AC153910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC099676; AAH99676.1; -; mRNA.
CCDS; CCDS20418.1; -.
PIR; A42445; A42445.
RefSeq; NP_001288224.1; NM_001301295.1.
RefSeq; NP_848460.1; NM_178373.3.
UniGene; Mm.10026; -.
PDB; 4IKG; X-ray; 1.93 A; A=39-118.
PDB; 4MAC; X-ray; 2.00 A; A/B=32-120.
PDBsum; 4IKG; -.
PDBsum; 4MAC; -.
ProteinModelPortal; P56198; -.
SMR; P56198; -.
BioGrid; 199749; 1.
IntAct; P56198; 1.
MINT; P56198; -.
STRING; 10090.ENSMUSP00000032416; -.
SwissLipids; SLP:000000723; -.
iPTMnet; P56198; -.
PhosphoSitePlus; P56198; -.
PaxDb; P56198; -.
PRIDE; P56198; -.
Ensembl; ENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278.
Ensembl; ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278.
GeneID; 14311; -.
KEGG; mmu:14311; -.
UCSC; uc009dgb.2; mouse.
CTD; 63924; -.
MGI; MGI:95585; Cidec.
eggNOG; ENOG410IWQS; Eukaryota.
eggNOG; ENOG4111HCT; LUCA.
GeneTree; ENSGT00390000018596; -.
HOGENOM; HOG000029211; -.
HOVERGEN; HBG050961; -.
InParanoid; P56198; -.
TreeFam; TF334321; -.
Reactome; R-MMU-8964572; Lipid particle organization.
PRO; PR:P56198; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030278; Expressed in 98 organ(s), highest expression level in epididymal fat pad.
CleanEx; MM_CIDEC; -.
ExpressionAtlas; P56198; baseline and differential.
Genevisible; P56198; MM.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0034389; P:lipid particle organization; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003508; CIDE-N_dom.
Pfam; PF02017; CIDE-N; 1.
SMART; SM00266; CAD; 1.
PROSITE; PS51135; CIDE_N; 1.
1: Evidence at protein level;
3D-structure; Activator; Apoptosis; Complete proteome;
Endoplasmic reticulum; Lipid droplet; Nucleus; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 239 Cell death activator CIDE-3.
/FTId=PRO_0000144723.
DOMAIN 41 118 CIDE-N. {ECO:0000255|PROSITE-
ProRule:PRU00447}.
MUTAGEN 46 46 R->E: Abolishes CIDE-N/CIDE-N interaction
between the 2 homodimer subunits.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 53 53 K->A: Slightly inhibits interaction with
PLIN1. {ECO:0000269|PubMed:23481402}.
MUTAGEN 55 55 R->E: Abolishes CIDE-N/CIDE-N interaction
between the 2 homodimer subunits.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 75 75 K->A: Inhibits interaction with PLIN1;
when associated with A-77.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 77 77 K->A: Inhibits interaction with PLIN1;
when associated with A-75.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 86 88 EED->QQN: Abolishes CIDE-N/CIDE-N
interaction between the 2 homodimer
subunits and inhibits lipid droplet
enlargement. No effect on
homodimerization.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 87 88 ED->QN: Reduces CIDE-N/CIDE-N interaction
between the 2 homodimer subunits and
inhibits lipid droplet enlargement.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 112 112 K->A: Slightly inhibits interaction with
PLIN1; when associated with A-115.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 115 115 K->A: Slightly inhibits interaction with
PLIN1; when associated with A-112 or A-
117. {ECO:0000269|PubMed:23481402}.
MUTAGEN 117 117 K->A: Slightly inhibits interaction with
PLIN1; when associated with A-115.
{ECO:0000269|PubMed:23481402}.
MUTAGEN 182 182 K->A: Abolishes lipid droplet enlargement
activity, but not localization to lipid
droplets, nor enrichement at contact
sites; when associated with A-186 and A-
190. {ECO:0000269|PubMed:22144693}.
MUTAGEN 186 186 K->A: Abolishes lipid droplet enlargement
activity, but not localization to lipid
droplets, nor enrichement at contact
sites; when associated with A-182 and A-
190. {ECO:0000269|PubMed:22144693}.
MUTAGEN 190 190 R->A: Abolishes lipid droplet enlargement
activity, but not localization to lipid
droplets, nor enrichement at contact
sites; when associated with A-182 and A-
186. {ECO:0000269|PubMed:22144693}.
MUTAGEN 224 224 K->A: No effect on protein stability;
when associated with A-226. Drastically
increased protein stability and decreased
ubiquitination; when associated with A-
226 and A-236.
{ECO:0000269|PubMed:20089860}.
MUTAGEN 226 226 K->A: No effect on protein stability;
when associated with A-226. Drastically
increased protein stability and decreased
ubiquitination; when associated with A-
224 and A-236.
{ECO:0000269|PubMed:20089860}.
MUTAGEN 236 236 K->A: No effect on protein stability.
Drastically increased protein stability
and decreased ubiquitination; when
associated with A-224 and A-226.
{ECO:0000269|PubMed:20089860}.
CONFLICT 188 189 ML -> IV (in Ref. 1; M61737).
{ECO:0000305}.
STRAND 44 48 {ECO:0000244|PDB:4IKG}.
STRAND 55 59 {ECO:0000244|PDB:4IKG}.
HELIX 63 73 {ECO:0000244|PDB:4IKG}.
STRAND 82 85 {ECO:0000244|PDB:4IKG}.
TURN 86 88 {ECO:0000244|PDB:4IKG}.
HELIX 95 100 {ECO:0000244|PDB:4IKG}.
STRAND 106 110 {ECO:0000244|PDB:4IKG}.
SEQUENCE 239 AA; 27324 MW; 7F4E6C5D2E24A161 CRC64;
MDYAMKSLSL LYPRSLSRHV AVSTAVVTQQ LVSKPSRETP RARPCRVSTA DRKVRKGIMA
HSLEDLLNKV QDILKLKDKP FSLVLEEDGT IVETEEYFQA LAKDTMFMVL LKGQKWKPPS
EQRKKRAQLA LSQKPTKKID VARVTFDLYK LNPQDFIGCL NVKATLYDTY SLSYDLHCYK
AKRIVKEMLR WTLFSMQATG HMLLGTSSYM QQFLDATEEE QPAKAKPSSL LPACLKMLQ


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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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