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

Protein arginine N-methyltransferase 3 (EC 2.1.1.-) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3)

 ANM3_MOUSE              Reviewed;         532 AA.
Q922H1; Q80VU9; Q8BFV5;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
25-OCT-2017, entry version 134.
RecName: Full=Protein arginine N-methyltransferase 3;
EC=2.1.1.-;
AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
Name=Prmt3; Synonyms=Hrmt1l3;
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 (ISOFORM 2).
STRAIN=129/SvJ;
Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W.,
Johnson D.K.;
"Genomic organization, chromosomal mapping, and expression analysis of
the murine Prmt3 and Htatip2 genes.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 114-532 (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Brain, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-24, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
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).
[5]
STRUCTURE BY NMR OF 38-145.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C2H2 zinc finger domain of the protein
arginine N-methyltransferase 3 from Mus musculus.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
guanidino nitrogens of arginyl residues in some proteins.
{ECO:0000250}.
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide and high
concentrations of zinc chloride. {ECO:0000250}.
-!- SUBUNIT: Monomer or homodimer (By similarity). Interacts with
EPB41L3; this inhibits methylation of target proteins. Interacts
with the 40S ribosomal protein RPS2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q922H1-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q922H1-2; Sequence=VSP_010498;
-!- DOMAIN: The zinc-finger is responsible for substrate specificity.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY151050; AAN84530.1; -; Genomic_DNA.
EMBL; AK031738; BAC27531.1; -; mRNA.
EMBL; AK086646; BAC39708.1; -; mRNA.
EMBL; BC008128; AAH08128.1; -; mRNA.
EMBL; BC050775; AAH50775.1; -; mRNA.
CCDS; CCDS21307.1; -. [Q922H1-2]
RefSeq; NP_598501.1; NM_133740.2. [Q922H1-2]
UniGene; Mm.33202; -.
UniGene; Mm.349442; -.
PDB; 1WIR; NMR; -; A=38-145.
PDBsum; 1WIR; -.
ProteinModelPortal; Q922H1; -.
SMR; Q922H1; -.
IntAct; Q922H1; 1.
STRING; 10090.ENSMUSP00000032715; -.
iPTMnet; Q922H1; -.
PhosphoSitePlus; Q922H1; -.
PaxDb; Q922H1; -.
PRIDE; Q922H1; -.
Ensembl; ENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505. [Q922H1-2]
GeneID; 71974; -.
KEGG; mmu:71974; -.
UCSC; uc009hbt.1; mouse. [Q922H1-2]
CTD; 10196; -.
MGI; MGI:1919224; Prmt3.
eggNOG; KOG1499; Eukaryota.
eggNOG; ENOG410XQYH; LUCA.
GeneTree; ENSGT00550000074406; -.
HOGENOM; HOG000198521; -.
HOVERGEN; HBG001793; -.
InParanoid; Q922H1; -.
KO; K11436; -.
OMA; ITKTSMC; -.
OrthoDB; EOG091G0ADC; -.
PhylomeDB; Q922H1; -.
TreeFam; TF323587; -.
EvolutionaryTrace; Q922H1; -.
PRO; PR:Q922H1; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030505; -.
CleanEx; MM_PRMT3; -.
ExpressionAtlas; Q922H1; baseline and differential.
Genevisible; Q922H1; MM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:MGI.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
GO; GO:0006479; P:protein methylation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036236; Znf_C2H2_sf.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Metal-binding; Methyltransferase; Phosphoprotein;
Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O60678}.
CHAIN 2 532 Protein arginine N-methyltransferase 3.
/FTId=PRO_0000212327.
DOMAIN 214 532 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
ZN_FING 46 69 C2H2-type.
ACT_SITE 326 326 {ECO:0000250}.
ACT_SITE 335 335 {ECO:0000250}.
BINDING 227 227 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 236 236 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 260 260 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 282 282 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 311 311 S-adenosyl-L-methionine. {ECO:0000250}.
MOD_RES 2 2 N-acetylcysteine.
{ECO:0000250|UniProtKB:O60678}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000250|UniProtKB:O60678}.
VAR_SEQ 417 420 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_010498.
STRAND 49 51 {ECO:0000244|PDB:1WIR}.
STRAND 54 57 {ECO:0000244|PDB:1WIR}.
HELIX 58 67 {ECO:0000244|PDB:1WIR}.
HELIX 73 79 {ECO:0000244|PDB:1WIR}.
HELIX 84 96 {ECO:0000244|PDB:1WIR}.
HELIX 101 105 {ECO:0000244|PDB:1WIR}.
HELIX 116 119 {ECO:0000244|PDB:1WIR}.
STRAND 122 125 {ECO:0000244|PDB:1WIR}.
HELIX 127 130 {ECO:0000244|PDB:1WIR}.
HELIX 133 136 {ECO:0000244|PDB:1WIR}.
SEQUENCE 532 AA; 59902 MW; 878ADDCCF4054F17 CRC64;
MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF CDRLFASAEE
TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWEKDEYLK
PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL SESASVVEKL KHMEARALSA EAALARARED
LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY
RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE
DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC
TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKMDG
KHIDCHTTSI SDLEFSSDFT LRTTKTAMCT AVAGYFDIYF EKNCHNRVVF STGPQSTKTH
WKQTVFLLEK PFPVKAGEAL KGKITVHKNK KDPRSLIVTL TLNSSTQTYS LQ


Related products :

Catalog number Product name Quantity
18-003-42152 Protein arginine N-methyltransferase 3 - EC 2.1.1.-; Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3 Polyclonal 0.05 mg Aff Pur
EIAAB05333 CARM1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Homo sapiens,Human,PRMT4,Protein arginine N-methyltransferase 4
EIAAB05331 Carm1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Prmt4,Protein arginine N-methyltransferase 4,Rat,Rattus norvegicus
EIAAB05332 Carm1,Coactivator-associated arginine methyltransferase 1,Histone-arginine methyltransferase CARM1,Mouse,Mus musculus,Prmt4,Protein arginine N-methyltransferase 4
29-207 PRMT1 is a protein arginine methyltransferase that functions as a histone methyltransferase specific for H4.The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone me 0.1 mg
EIAAB31135 L-isoaspartyl protein carboxyl methyltransferase,Mouse,Mus musculus,Pcmt1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspa
EIAAB31136 Bos taurus,Bovine,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspar
EIAAB31133 Homo sapiens,Human,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspa
EIAAB31132 Chicken,Gallus gallus,L-isoaspartyl protein carboxyl methyltransferase,PCMT1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-a
EIAAB31137 L-isoaspartyl protein carboxyl methyltransferase,PCMT1,Pig,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspartate) O-methyl
EIAAB31134 L-isoaspartyl protein carboxyl methyltransferase,Pcmt1,PIMT,Protein L-isoaspartyl_D-aspartyl methyltransferase,Protein-beta-aspartate methyltransferase,Protein-L-isoaspartate(D-aspartate) O-methyltran
E2223m ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Te 96T
E2223Rb ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus 96T
U2223Rb CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus, 96T
E2223Rb Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbit
E2223h Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT
E2223m Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt
U2223m CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Tem 96T
U2223m CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
E2223h ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E2223h ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
U2223h CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E2223m ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
U2223Rb CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbi 96T
U2223h CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T


 

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

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





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

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

SIRET 48423788800017

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
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

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

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




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






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






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

GENTAUR Poland Sp. z o.o.


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

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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