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

1,3-beta-glucanosyltransferase GAS1 (EC 2.4.1.-) (Glycolipid-anchored surface protein 1) (Glycoprotein GP115)

 GAS1_YEAST              Reviewed;         559 AA.
P22146; D6W0D4; P23151;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
12-SEP-2018, entry version 167.
RecName: Full=1,3-beta-glucanosyltransferase GAS1;
EC=2.4.1.-;
AltName: Full=Glycolipid-anchored surface protein 1;
AltName: Full=Glycoprotein GP115;
Flags: Precursor;
Name=GAS1; Synonyms=GGP1; OrderedLocusNames=YMR307W;
ORFNames=YM9952.09;
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], PROTEIN SEQUENCE OF 23-39; 237-240;
435-437 AND 527-528, SUBCELLULAR LOCATION, AND GPI-ANCHOR AT ASN-528.
PubMed=1824714; DOI=10.1128/MCB.11.1.27;
Nuoffer C., Jenoe P., Conzelmann A., Riezman H.;
"Determinants for glycophospholipid anchoring of the Saccharomyces
cerevisiae GAS1 protein to the plasma membrane.";
Mol. Cell. Biol. 11:27-37(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBY939;
PubMed=2061310;
Vai M., Gatti E., Lacana E., Popolo L., Alberghina L.;
"Isolation and deduced amino acid sequence of the gene encoding gp115,
a yeast glycophospholipid-anchored protein containing a serine-rich
region.";
J. Biol. Chem. 266:12242-12248(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[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]
SUBCELLULAR LOCATION, AND GPI-ANCHOR.
PubMed=3046936;
Conzelmann A., Riezman H., Desponds C., Bron C.;
"A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae is
attached to the lipid bilayer through an inositol-containing
phospholipid.";
EMBO J. 7:2233-2240(1988).
[6]
SUBCELLULAR LOCATION.
PubMed=3072201;
Popolo L., Grandori R., Vai M., Lacana E., Alberghina L.;
"Immunochemical characterization of gp115, a yeast glycoprotein
modulated by the cell cycle.";
Eur. J. Cell Biol. 47:173-180(1988).
[7]
GPI-ANCHOR.
PubMed=2160276; DOI=10.1016/0167-4838(90)90237-A;
Vai M., Popolo L., Grandori R., Lacana E., Alberghina L.;
"The cell cycle modulated glycoprotein GP115 is one of the major yeast
proteins containing glycosylphosphatidylinositol.";
Biochim. Biophys. Acta 1038:277-285(1990).
[8]
SUBCELLULAR LOCATION.
PubMed=10564469; DOI=10.1046/j.1365-2958.1999.01585.x;
De Sampaio G., Bourdineaud J.-P., Lauquin G.J.-M.;
"A constitutive role for GPI anchors in Saccharomyces cerevisiae: cell
wall targeting.";
Mol. Microbiol. 34:247-256(1999).
[9]
FUNCTION.
PubMed=10809732; DOI=10.1074/jbc.275.20.14882;
Mouyna I., Fontaine T., Vai M., Monod M., Fonzi W.A., Diaquin M.,
Popolo L., Hartland R.P., Latge J.-P.;
"Glycosylphosphatidylinositol-anchored glucanosyltransferases play an
active role in the biosynthesis of the fungal cell wall.";
J. Biol. Chem. 275:14882-14889(2000).
[10]
FUNCTION, AND MUTAGENESIS OF CYS-74; CYS-103; GLU-161; GLU-262 AND
CYS-265.
PubMed=15355340; DOI=10.1111/j.1432-1033.2004.04297.x;
Carotti C., Ragni E., Palomares O., Fontaine T., Tedeschi G.,
Rodriguez R., Latge J.-P., Vai M., Popolo L.;
"Characterization of recombinant forms of the yeast Gas1 protein and
identification of residues essential for glucanosyltransferase
activity and folding.";
Eur. J. Biochem. 271:3635-3645(2004).
[11]
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
GPI-ANCHOR.
PubMed=15781460; DOI=10.1074/jbc.M500334200;
Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
de Koster C.G.;
"Comprehensive proteomic analysis of Saccharomyces cerevisiae cell
walls: identification of proteins covalently attached via
glycosylphosphatidylinositol remnants or mild alkali-sensitive
linkages.";
J. Biol. Chem. 280:20894-20901(2005).
[12]
LEVEL OF PROTEIN EXPRESSION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
"Mass spectrometric quantitation of covalently bound cell wall
proteins in Saccharomyces cerevisiae.";
FEMS Yeast Res. 7:887-896(2007).
[13]
MUTAGENESIS OF CYS-348.
PubMed=18468997; DOI=10.1074/jbc.M801562200;
Popolo L., Ragni E., Carotti C., Palomares O., Aardema R., Back J.W.,
Dekker H.L., de Koning L.J., de Jong L., de Koster C.G.;
"Disulfide bond structure and domain organization of yeast beta(1,3)-
glucanosyltransferases involved in cell wall biogenesis.";
J. Biol. Chem. 283:18553-18565(2008).
[14]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18434410; DOI=10.1128/JVI.00412-08;
Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I.,
Lee F.-H., Montefiori D., Smith D.F., Doms R.W., Geng Y.;
"An engineered Saccharomyces cerevisiae strain binds the broadly
neutralizing human immunodeficiency virus type 1 antibody 2G12 and
elicits mannose-specific gp120-binding antibodies.";
J. Virol. 82:6447-6457(2008).
-!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and
transfers the newly generated reducing end (the donor) to the non-
reducing end of another 1,3-beta-glucan molecule (the acceptor)
forming a 1,3-beta linkage, resulting in the elongation of 1,3-
beta-glucan chains in the cell wall. Involved in cell wall
biosynthesis and morphogenesis. {ECO:0000269|PubMed:10809732,
ECO:0000269|PubMed:15355340}.
-!- INTERACTION:
P06700:SIR2; NbExp=2; IntAct=EBI-7327, EBI-17219;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18434410,
ECO:0000269|PubMed:3046936, ECO:0000269|PubMed:3072201}; Lipid-
anchor, GPI-anchor {ECO:0000269|PubMed:2160276,
ECO:0000269|PubMed:3046936}. Secreted, cell wall
{ECO:0000269|PubMed:10564469, ECO:0000269|PubMed:15781460}.
Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP)
as well as covalently-linked GPI-modified cell wall protein (GPI-
CWP) in the outer cell wall layer. {ECO:0000269|PubMed:15781460,
ECO:0000269|PubMed:3046936}.
-!- PTM: Extensively N- and O-glycosylated.
{ECO:0000269|PubMed:18434410}.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer.
-!- MISCELLANEOUS: Present with 11000 wall-bound molecules/cell in log
phase YPD medium. {ECO:0000269|PubMed:17617218}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X53424; CAA37512.1; -; Genomic_DNA.
EMBL; X56399; CAA39809.1; -; Genomic_DNA.
EMBL; Z49212; CAA89140.1; -; Genomic_DNA.
EMBL; BK006946; DAA10208.1; -; Genomic_DNA.
PIR; S53977; RWBYS1.
RefSeq; NP_014038.1; NM_001182818.1.
ProteinModelPortal; P22146; -.
SMR; P22146; -.
BioGrid; 35487; 796.
DIP; DIP-4390N; -.
IntAct; P22146; 11.
MINT; P22146; -.
STRING; 4932.YMR307W; -.
CAZy; CBM43; Carbohydrate-Binding Module Family 43.
CAZy; GH72; Glycoside Hydrolase Family 72.
COMPLUYEAST-2DPAGE; P22146; -.
MaxQB; P22146; -.
PaxDb; P22146; -.
PRIDE; P22146; -.
EnsemblFungi; YMR307W; YMR307W; YMR307W.
GeneID; 855355; -.
KEGG; sce:YMR307W; -.
EuPathDB; FungiDB:YMR307W; -.
SGD; S000004924; GAS1.
GeneTree; ENSGT00910000145562; -.
HOGENOM; HOG000164982; -.
InParanoid; P22146; -.
OMA; NCTRDLP; -.
OrthoDB; EOG092C1TYR; -.
BioCyc; YEAST:G3O-32971-MONOMER; -.
PRO; PR:P22146; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
GO; GO:0005621; C:cellular bud scar; IDA:SGD.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
GO; GO:0045121; C:membrane raft; IDA:SGD.
GO; GO:0034399; C:nuclear periphery; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0000936; C:primary cell septum; IDA:SGD.
GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
GO; GO:0006342; P:chromatin silencing; IMP:SGD.
GO; GO:0030447; P:filamentous growth; IMP:SGD.
GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
InterPro; IPR004886; Glucanosyltransferase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR012946; X8.
PANTHER; PTHR31468; PTHR31468; 1.
Pfam; PF03198; Glyco_hydro_72; 1.
Pfam; PF07983; X8; 1.
SMART; SM00768; X8; 1.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
Cell membrane; Cell wall; Cell wall biogenesis/degradation;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
Secreted; Signal; Transferase.
SIGNAL 1 22 {ECO:0000269|PubMed:1824714}.
CHAIN 23 528 1,3-beta-glucanosyltransferase GAS1.
/FTId=PRO_0000010473.
PROPEP 529 559 Removed in mature form.
/FTId=PRO_0000010474.
REGION 119 127 Donor substrate binding. {ECO:0000250}.
COMPBIAS 438 525 Ser-rich.
ACT_SITE 161 161 Proton donor.
ACT_SITE 262 262 Nucleophile.
BINDING 92 92 Donor substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 160 160 Donor substrate. {ECO:0000250}.
BINDING 161 161 Acceptor substrate. {ECO:0000250}.
BINDING 202 202 Acceptor substrate; via carbonyl oxygen.
{ECO:0000250}.
BINDING 207 207 Acceptor substrate. {ECO:0000250}.
BINDING 294 294 Donor substrate. {ECO:0000250}.
LIPID 528 528 GPI-anchor amidated asparagine.
{ECO:0000269|PubMed:1824714}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 74 103 {ECO:0000250}.
DISULFID 216 348 {ECO:0000250}.
DISULFID 234 265 {ECO:0000250}.
DISULFID 370 421 {ECO:0000250}.
DISULFID 372 462 {ECO:0000250}.
DISULFID 379 445 {ECO:0000250}.
DISULFID 398 403 {ECO:0000250}.
MUTAGEN 74 74 C->S: Impairs the folding and stability
of the protein.
{ECO:0000269|PubMed:15355340}.
MUTAGEN 103 103 C->S: Partially impairs the folding and
stability of the protein.
{ECO:0000269|PubMed:15355340}.
MUTAGEN 161 161 E->Q: Loss of function.
{ECO:0000269|PubMed:15355340}.
MUTAGEN 262 262 E->Q: Loss of function.
{ECO:0000269|PubMed:15355340}.
MUTAGEN 265 265 C->S: Partially impairs the folding and
stability of the protein.
{ECO:0000269|PubMed:15355340}.
MUTAGEN 348 348 C->S: Impairs the folding and stability
of the protein.
{ECO:0000269|PubMed:18468997}.
CONFLICT 211 211 T -> A (in Ref. 1; CAA37512).
{ECO:0000305}.
SEQUENCE 559 AA; 59582 MW; D6E39568DCB4C5AE CRC64;
MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA YQADTANETS
GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH SECMKALNDA DIYVIADLAA
PATSINRDDP TWTVDLFNSY KTVVDTFANY TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR
DVRQYISDKN YRKIPVGYSS NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK
TSGYADRTAE FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET
NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA TGKYWSAATE
LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE VDCSGISANG TAGKYGAYSF
CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS ATLQTATTQA SCSSALKEIG SMGTNSASGS
VDLGSGTESS TASSNASGSS SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV
VFTSIISLSI AAGVGFALV


Related products :

Catalog number Product name Quantity
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
EIAAB05294 CAPRIN1,Caprin-1,Cell cycle-associated protein 1,Cytoplasmic activation- and proliferation-associated protein 1,GPI-anchored membrane protein 1,GPI-anchored protein p137,GPIAP1,GPIP137,GPI-p137,Homo s
EIAAB25058 CD200 cell surface glycoprotein receptor,CD200R,CD200R1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,CRTR2,Homo sapiens,Human,MOX2R,OX2R,UNQ2522_PRO6015
E0310m ELISA kit Activated protein C-binding protein,APC inhibitor,Apoh,Apo-H,Apolipoprotein H,B2gp1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Mouse,Mus musculus 96T
E0310m ELISA Activated protein C-binding protein,APC inhibitor,Apoh,Apo-H,Apolipoprotein H,B2gp1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Mouse,Mus musculus 96T
U0310m CLIA Activated protein C-binding protein,APC inhibitor,Apoh,Apo-H,Apolipoprotein H,B2gp1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Mouse,Mus musculus 96T
10-663-45662 beta-2 Glycoprotein-I_Apolipoprotein H Human - Beta-2-glycoprotein I; Apolipoprotein H; Apo-H; B2GPI; Beta(2)GPI; Activated protein C-binding protein; APC inhibitor; Anticardiolipin cofactor N_A 0.02 mg
10-663-45662 beta-2 Glycoprotein-I_Apolipoprotein H Human - Beta-2-glycoprotein I; Apolipoprotein H; Apo-H; B2GPI; Beta(2)GPI; Activated protein C-binding protein; APC inhibitor; Anticardiolipin cofactor N_A 1 mg
10-663-45662 beta-2 Glycoprotein-I_Apolipoprotein H Human - Beta-2-glycoprotein I; Apolipoprotein H; Apo-H; B2GPI; Beta(2)GPI; Activated protein C-binding protein; APC inhibitor; Anticardiolipin cofactor N_A 0.005 mg
E0310h ELISA kit Activated protein C-binding protein,Anticardiolipin cofactor,APC inhibitor,APOH,Apo-H,Apolipoprotein H,B2G1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Homo sapiens,Human 96T
E0310h ELISA Activated protein C-binding protein,Anticardiolipin cofactor,APC inhibitor,APOH,Apo-H,Apolipoprotein H,B2G1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Homo sapiens,Human 96T
U0310h CLIA Activated protein C-binding protein,Anticardiolipin cofactor,APC inhibitor,APOH,Apo-H,Apolipoprotein H,B2G1,B2GPI,Beta(2)GPI,Beta-2-glycoprotein 1,Beta-2-glycoprotein I,Homo sapiens,Human 96T
EIAAB25056 CD200 cell surface glycoprotein receptor,Cd200r1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,Mox2r,OX102 antigen,Ox2r,Rat,Rattus norvegicus
29-576 MUC1 is a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell typ 0.05 mg
29-577 MUC1 is a membrane bound, glycosylated phosphoprotein. The protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell typ 0.1 mg
30-721 Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor fo 0.05 mg
EIAAB05297 Caprin1,Caprin-1,Cytoplasmic activation- and proliferation-associated protein 1,G5E5,GPI-anchored membrane protein 1,GPI-anchored protein p137,Gpiap,Gpiap1,Gpip137,GPI-p137,M11s1,Membrane component ch
EIAAB25059 CD200 cell surface glycoprotein receptor,Cd200r1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,Mouse,Mox2r,Mus musculus,Ox2r
65-903 anti_prion antibody(clone 7A1) Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neurons and glial cells, as well as immune and reproductive c 50 ug
65-904 anti_prion antibody(clone 7A1) Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neurons and glial cells, as well as immune and reproductive c 250 ug
E0953m ELISA Cd8a,Lyt2,Lyt-2,Mouse,Mus musculus,T-cell surface glycoprotein CD8 alpha chain,T-cell surface glycoprotein Lyt-2 96T
U0953m CLIA Cd8a,Lyt2,Lyt-2,Mouse,Mus musculus,T-cell surface glycoprotein CD8 alpha chain,T-cell surface glycoprotein Lyt-2 96T
E0953m ELISA kit Cd8a,Lyt2,Lyt-2,Mouse,Mus musculus,T-cell surface glycoprotein CD8 alpha chain,T-cell surface glycoprotein Lyt-2 96T
65-902 anti_prion antibody(clone 2C5_5) Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neurons and glial cells, as well as immune and reproductive 250 ug
65-901 anti_prion antibody(clone 2C5_5) Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neurons and glial cells, as well as immune and reproductive 50 ug


 

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