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

Peptidyl-prolyl cis-trans isomerase ESS1 (PPIase ESS1) (EC 5.2.1.8) (Parvulin ESS1) (Processing/termination factor 1)

 ESS1_YEAST              Reviewed;         170 AA.
P22696; D6VWJ3;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 3.
25-OCT-2017, entry version 167.
RecName: Full=Peptidyl-prolyl cis-trans isomerase ESS1;
Short=PPIase ESS1;
EC=5.2.1.8;
AltName: Full=Parvulin ESS1;
AltName: Full=Processing/termination factor 1;
Name=ESS1; Synonyms=PIN1, PTF1; OrderedLocusNames=YJR017C;
ORFNames=J1452;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBY864;
PubMed=2648698; DOI=10.1002/yea.320050108;
Hanes S.D., Shank P.R., Bostian K.A.;
"Sequence and mutational analysis of ESS1, a gene essential for growth
in Saccharomyces cerevisiae.";
Yeast 5:55-72(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DH484;
PubMed=7781779; DOI=10.1016/0014-5793(95)00471-K;
Hani J., Stumpf G., Domdey H.;
"PTF1 encodes an essential protein in Saccharomyces cerevisiae, which
shows strong homology with a new putative family of PPIases.";
FEBS Lett. 365:198-202(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
ENZYME REGULATION.
PubMed=9558330; DOI=10.1021/bi973162p;
Hennig L., Christner C., Kipping M., Schelbert B., Ruecknagel K.P.,
Grabley S., Kuellertz G., Fischer G.;
"Selective inactivation of parvulin-like peptidyl-prolyl cis/trans
isomerases by juglone.";
Biochemistry 37:5953-5960(1998).
[6]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-127 AND GLY-162.
PubMed=9867817; DOI=10.1074/jbc.274.1.108;
Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G.,
Wiebauer K., Rahfeld J.-U.;
"Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a
defect in 3'-end formation of a pre-mRNA in Saccharomyces
cerevisiae.";
J. Biol. Chem. 274:108-116(1999).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RPB1.
PubMed=10531363; DOI=10.1074/jbc.274.44.31583;
Morris D.P., Phatnani H.P., Greenleaf A.L.;
"Phospho-carboxyl-terminal domain binding and the role of a prolyl
isomerase in pre-mRNA 3'-End formation.";
J. Biol. Chem. 274:31583-31587(1999).
[8]
INTERACTION WITH SIN3.
PubMed=10899127; DOI=10.1093/emboj/19.14.3739;
Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
"Cyclophilin A and Ess1 interact with and regulate silencing by the
Sin3-Rpd3 histone deacetylase.";
EMBO J. 19:3739-3749(2000).
[9]
IDENTIFICATION OF PROBABLE INITIATION SITE.
PubMed=12748633; DOI=10.1038/nature01644;
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and
regulatory elements.";
Nature 423:241-254(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
MUTAGENESIS OF CYS-120; SER-122 AND HIS-164.
PubMed=15728580; DOI=10.1074/jbc.M412172200;
Gemmill T.R., Wu X., Hanes S.D.;
"Vanishingly low levels of Ess1 prolyl-isomerase activity are
sufficient for growth in Saccharomyces cerevisiae.";
J. Biol. Chem. 280:15510-15517(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Essential PPIase specific for phosphoserine and
phosphothreonine N-terminal to the proline residue. Required for
efficient pre-mRNA 3'-end processing and transcription
termination, probably by inducing conformational changes by
proline-directed isomerization in the C-terminal domain (CTD) of
RPB1, thereby altering cofactor binding with the RNA polymerase II
transcription complex. Also targets the SIN3-RPD3 histone
deacetylase complex (HDAC).
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000269|PubMed:9867817}.
-!- ENZYME REGULATION: Inhibited by 5-hydroxy-1,4-naphthoquinone
(juglone), but not by FK506 or cyclosporin A.
{ECO:0000269|PubMed:9558330}.
-!- SUBUNIT: Interacts with the RNA polymerase II largest subunit
(RPB1) and with the SIN1-RDP3 HDAC subunit SIN3.
{ECO:0000269|PubMed:10531363, ECO:0000269|PubMed:10899127}.
-!- INTERACTION:
P07278:BCY1; NbExp=2; IntAct=EBI-6679, EBI-9475;
P10592:SSA2; NbExp=2; IntAct=EBI-6679, EBI-8603;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The WW domain binds to the phosphorylated tandem 7
residues repeats of RPB1.
-!- MISCELLANEOUS: Present with 4401 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA60941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA89541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=Ref.1; Type=Frameshift; Positions=127; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X85972; CAA59961.1; -; Genomic_DNA.
EMBL; X87611; CAA60941.1; ALT_INIT; Genomic_DNA.
EMBL; Z49517; CAA89541.1; ALT_INIT; Genomic_DNA.
EMBL; BK006943; DAA08809.1; -; Genomic_DNA.
PIR; S52764; S52764.
RefSeq; NP_012551.2; NM_001181675.1.
ProteinModelPortal; P22696; -.
SMR; P22696; -.
BioGrid; 33773; 979.
DIP; DIP-3856N; -.
ELM; P22696; -.
IntAct; P22696; 115.
MINT; MINT-569771; -.
STRING; 4932.YJR017C; -.
BindingDB; P22696; -.
iPTMnet; P22696; -.
MaxQB; P22696; -.
PRIDE; P22696; -.
TopDownProteomics; P22696; -.
EnsemblFungi; YJR017C; YJR017C; YJR017C.
GeneID; 853475; -.
KEGG; sce:YJR017C; -.
EuPathDB; FungiDB:YJR017C; -.
SGD; S000003778; ESS1.
GeneTree; ENSGT00640000091578; -.
HOGENOM; HOG000275331; -.
InParanoid; P22696; -.
KO; K09578; -.
OMA; DEVQCLH; -.
OrthoDB; EOG092C4TRA; -.
BioCyc; YEAST:YJR017C-MONOMER; -.
Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation.
PRO; PR:P22696; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblPlants.
GO; GO:0005634; C:nucleus; IC:SGD.
GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
GO; GO:0000993; F:RNA polymerase II core binding; IPI:SGD.
GO; GO:0009630; P:gravitropism; IEA:EnsemblPlants.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:SGD.
GO; GO:0031064; P:negative regulation of histone deacetylation; IMP:SGD.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:2000749; P:positive regulation of chromatin silencing at rDNA; IMP:SGD.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:SGD.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IGI:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:SGD.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:SGD.
GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
GO; GO:0032880; P:regulation of protein localization; IEA:EnsemblPlants.
GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
CDD; cd00201; WW; 1.
InterPro; IPR000297; PPIase_PpiC.
InterPro; IPR023058; PPIase_PpiC_CS.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00639; Rotamase; 1.
Pfam; PF00397; WW; 1.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS01096; PPIC_PPIASE_1; 1.
PROSITE; PS50198; PPIC_PPIASE_2; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
Reference proteome; Rotamase.
CHAIN 1 170 Peptidyl-prolyl cis-trans isomerase ESS1.
/FTId=PRO_0000193433.
DOMAIN 9 43 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 57 170 PpiC. {ECO:0000255|PROSITE-
ProRule:PRU00278}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 120 120 C->R: Abolishes PPIase activity.
{ECO:0000269|PubMed:15728580}.
MUTAGEN 122 122 S->P: Abolishes PPIase activity.
{ECO:0000269|PubMed:15728580}.
MUTAGEN 127 127 G->D: In PTF1-2; decreases the catalytic
efficiency 20-fold.
{ECO:0000269|PubMed:9867817}.
MUTAGEN 162 162 G->S: In PTF1-5; decreases the catalytic
efficiency 12-fold.
{ECO:0000269|PubMed:9867817}.
MUTAGEN 164 164 H->R: Abolishes PPIase activity.
{ECO:0000269|PubMed:15728580}.
CONFLICT 8 8 R -> S (in Ref. 1). {ECO:0000305}.
CONFLICT 17 17 V -> A (in Ref. 1). {ECO:0000305}.
CONFLICT 128 128 D -> G (in Ref. 1). {ECO:0000305}.
SEQUENCE 170 AA; 19405 MW; 18D3EC02E8395175 CRC64;
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH KHLRDHPVRV
RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR LDDDSKTNSF EALAKERSDC
SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV GEVSDIVESG SGVHVIKRVG


Related products :

Catalog number Product name Quantity
EIAAB31142 hEPVH,Homo sapiens,hPar14,hPar17,Human,Par14,Par17,Parvulin-14,Parvulin-17,Peptidyl-prolyl cis_trans isomerase EPVH,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4,Peptidyl-prolyl cis-trans iso
EIAAB31143 Bos taurus,Bovine,Par14,Parvulin-14,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4,Peptidyl-prolyl cis-trans isomerase Pin4,PIN4,PPIase Pin4,Rotamase Pin4
EIAAB31141 Mouse,Mus musculus,Par14,Parvulin-14,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4,Peptidyl-prolyl cis-trans isomerase Pin4,Pin4,PPIase Pin4,Rotamase Pin4
EIAAB32020 40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,CYP-40,Peptidyl-prolyl cis-trans isomerase D,PPIase D,Ppid,Rat,Rattus norvegicus,Rotamase D
EIAAB32022 40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,CYP-40,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase D,PPIase D,Ppid,Rotamase D
EIAAB32021 40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,Cyclophilin-related protein,CYP40,CYP-40,CYPD,Homo sapiens,Human,Peptidyl-prolyl cis-trans isomerase D,PPIase D,PPID,Rotamase D
EIAAB32030 Cyclophilin G,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase G,Peptidyl-prolyl isomerase G,PPIase G,Ppig,Rotamase G
EIAAB32019 40 kDa peptidyl-prolyl cis-trans isomerase,Bos taurus,Bovine,Cyclophilin-40,Cyclophilin-related protein,CYP-40,CYPD,Estrogen receptor-binding cyclophilin,Peptidyl-prolyl cis-trans isomerase D,PPIase D
EIAAB31140 Homo sapiens,Human,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Peptidyl-prolyl cis-trans isomerase Pin1,PIN1,PPIase Pin1,Rotamase Pin1
EIAAB31138 Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Peptidyl-prolyl cis-trans isomerase Pin1,Pin1,PPIase Pin1
EIAAB31139 Bos taurus,Bovine,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Peptidyl-prolyl cis-trans isomerase Pin1,PIN1,PPIase Pin1,Rotamase Pin1
EIAAB32032 Cyclophilin G,Matrin cyclophilin,Matrin-cyp,Peptidyl-prolyl cis-trans isomerase G,Peptidyl-prolyl isomerase G,PPIase G,Ppig,Rat,Rattus norvegicus,Rotamase G
EIAAB32031 CARS-cyclophilin,CARS-Cyp,CASP10,Clk-associating RS-cyclophilin,Cyclophilin G,Homo sapiens,Human,Peptidyl-prolyl cis-trans isomerase G,Peptidyl-prolyl isomerase G,PPIase G,PPIG,Rotamase G,SR-cyclophil
C291 Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 PPIase lmg
C291 Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 PPIase 500
CE73 Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 PPIase l0
CE06 Human Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 PPIase 50
18-271-81040 Peptidylprolyl Isomerase - Chicken Anti Peptidylprolyl Isomerase; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; FKBP-21; NcFKBP22 Polyclonal 0.1 mg
10-288-22243F Peptidyl-prolyl cis-trans isomerase. mitochondrial - EC 5.2.1.8; PPIase; Rotamase; Cyclophilin F 0.1 mg
10-288-22243F Peptidyl-prolyl cis-trans isomerase. mitochondrial - EC 5.2.1.8; PPIase; Rotamase; Cyclophilin F 0.05 mg
29-363 PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of 0.1 mg
29-364 PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of 0.1 mg
30-165 PPIF is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of 0.1 mg
30-723 PPIA is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of 0.1 mg
15-288-22243F Peptidyl-prolyl cis-trans isomerase. mitochondrial - EC 5.2.1.8; PPIase; Rotamase; Cyclophilin F Polyclonal 0.05 mg


 

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