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

Structural polyprotein (p110) [Cleaved into: Capsid protein (Coat protein) (C); Spike glycoprotein E2 (E2 envelope glycoprotein); Spike glycoprotein E1 (E1 envelope glycoprotein)]

 POLS_RUBVT              Reviewed;        1063 AA.
P07566;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
10-OCT-2018, entry version 101.
RecName: Full=Structural polyprotein;
AltName: Full=p110;
Contains:
RecName: Full=Capsid protein;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=Spike glycoprotein E2;
AltName: Full=E2 envelope glycoprotein;
Contains:
RecName: Full=Spike glycoprotein E1;
AltName: Full=E1 envelope glycoprotein;
Rubella virus (strain Therien) (RUBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Rubivirus.
NCBI_TaxID=11045;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2353453; DOI=10.1016/0042-6822(90)90476-8;
Dominguez G., Wang C.Y., Frey T.K.;
"Sequence of the genome RNA of rubella virus: evidence for genetic
rearrangement during togavirus evolution.";
Virology 177:225-238(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-621.
PubMed=2836271; DOI=10.1016/0378-1119(88)90582-3;
Frey T.K., Marr L.D.;
"Sequence of the region coding for virion proteins C and E2 and the
carboxy terminus of the nonstructural proteins of rubella virus:
comparison with alphaviruses.";
Gene 62:85-99(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 551-1063.
PubMed=3755848; DOI=10.1016/0042-6822(86)90446-0;
Frey T.K., Marr L.D., Hemphill M.L., Dominguez G.;
"Molecular cloning and sequencing of the region of the rubella virus
genome coding for glycoprotein E1.";
Virology 154:228-232(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-319.
PubMed=3351478; DOI=10.1099/0022-1317-69-3-603;
Takkinen K., Vidgren G., Ekstrand J., Hellman U., Kalkkinen N.,
Wernstedt C., Pettersson R.F.;
"Nucleotide sequence of the rubella virus capsid protein gene reveals
an unusually high G/C content.";
J. Gen. Virol. 69:603-612(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 278-1063.
PubMed=3655744; DOI=10.1099/0022-1317-68-9-2347;
Vidgren G., Takkinen K., Kalkkinen N., Kaeaeriaeinen L.,
Pettersson R.F.;
"Nucleotide sequence of the genes coding for the membrane
glycoproteins E1 and E2 of rubella virus.";
J. Gen. Virol. 68:2347-2357(1987).
[6]
OLIGOMERIZATION.
PubMed=1962452; DOI=10.1016/0042-6822(91)90552-M;
Baron M.D., Forsell K.;
"Oligomerization of the structural proteins of rubella virus.";
Virology 185:811-819(1991).
[7]
DISULFIDE BOND.
PubMed=9143273; DOI=10.1006/viro.1997.8462;
Gros C., Linder M., Wengler G., Wengler G.;
"Analyses of disulfides present in the rubella virus E1
glycoprotein.";
Virology 230:179-186(1997).
[8]
FUNCTION (SPIKE GLYCOPROTEIN E1).
PubMed=15557740; DOI=10.1111/j.1348-0421.2004.tb03614.x;
Kee S.H., Cho E.J., Song J.W., Park K.S., Baek L.J., Song K.J.;
"Effects of endocytosis inhibitory drugs on rubella virus entry into
VeroE6 cells.";
Microbiol. Immunol. 48:823-829(2004).
-!- FUNCTION: Capsid protein: Capsid protein interacts with genomic
RNA and assembles into icosahedric core particles 65-70 nm in
diameter. The resulting nucleocapsid eventually associates with
the cytoplasmic domain of E2 at the cell membrane, leading to
budding and formation of mature virions from host Golgi membranes.
Phosphorylation negatively regulates RNA-binding activity,
possibly delaying virion assembly during the viral replication
phase. Capsid protein dimerizes and becomes disulfide-linked in
the virion. Modulates genomic RNA replication. Modulates
subgenomic RNA synthesis by interacting with human C1QBP/SF2P32.
Induces both perinuclear clustering of mitochondria and the
formation of electron-dense intermitochondrial plaques, both
hallmarks of rubella virus infected cells. Induces apoptosis when
expressed in transfected cells. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E2: Responsible for viral attachment
to target host cell, by binding to the cell receptor. Its
transport to the plasma membrane depends on interaction with E1
protein. The surface glycoproteins display an irregular helical
organization and a pseudo-tetrameric inner nucleocapsid
arrangement. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E1: Class II viral fusion protein (By
similarity). Fusion activity is inactive as long as E1 is bound to
E2 in mature virion. After virus attachment to target cell and
clathrin-mediated endocytosis, acidification of the endosome would
induce dissociation of E1/E2 heterodimer and concomitant
trimerization of the E1 subunits (PubMed:15557740). This E1
homotrimer is fusion active, and promotes release of viral
nucleocapsid in cytoplasm after endosome and viral membrane
fusion. The cytoplasmic tail of spike glycoprotein E1 modulates
virus release. The surface glycoproteins display an irregular
helical organization and a pseudo-tetrameric inner nucleocapsid
arrangement (By similarity). {ECO:0000250|UniProtKB:P08563,
ECO:0000269|PubMed:15557740}.
-!- SUBUNIT: Capsid protein: Homodimer; further assembles into
homooligomer. Interacts with human C1QBP. Spike glycoprotein E1:
Heterodimer with spike glycoprotein E2. Spike glycoprotein E2:
Heterodimer with spike glycoprotein E1.
{ECO:0000250|UniProtKB:P08563}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion
{ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion
{ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is
concentrated around Golgi region (By similarity). In the virion,
it is probably associated to the viral membrane (By similarity).
{ECO:0000250|UniProtKB:P08563}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus
membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2
form heterodimer in the endoplasmic reticulum before they are
transported to and retained in the Golgi complex, where virus
assembly occurs. E1 possesses an endoplasmic reticulum retention
signal, and unassembled E2 and E1 subunits are retained in the
endoplasmic reticulum. Presumably, assembly of E2 and E1 would
mask the signal, thereby allowing transport of the heterodimer to
the Golgi complex. {ECO:0000250|UniProtKB:P08563}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus
membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I
membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2
form heterodimer in the endoplasmic reticulum before they are
transported to and retained in the Golgi complex, where virus
assembly occurs. E1 possesses an endoplasmic reticulum retention
signal, and unassembled E2 and E1 subunits are retained in the
endoplasmic reticulum. Presumably, assembly of E2 and E1 would
mask the signal, thereby allowing transport of the heterodimer to
the Golgi complex. {ECO:0000250|UniProtKB:P08563}.
-!- DOMAIN: Structural polyprotein: Contains two internal signal
peptides that are necessary for directing translocation of the
glycoproteins into the lumen of the endoplasmic reticulum.
{ECO:0000250|UniProtKB:P08563}.
-!- DOMAIN: Capsid protein: The capsid protein is probably attached to
the viral membrane through the E2 signal peptide. This domain is
also required for the localization of the capsid protein to the
juxtanuclear region and subsequent virus assembly at the Golgi
complex. {ECO:0000250|UniProtKB:P08563}.
-!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Two signal peptidase-mediated cleavages
within the polyprotein produce the structural proteins capsid, E2,
and E1. The E2 signal peptide remains attached to the C-terminus
of the capsid protein after cleavage by the signal peptidase.
Another signal peptide at E2 C-terminus directs E1 to the ER, with
a similar mechanism. {ECO:0000250|UniProtKB:P08563}.
-!- PTM: Spike glycoprotein E1: Contains three N-linked
oligosaccharides. {ECO:0000250|UniProtKB:P08563}.
-!- PTM: Capsid is phosphorylated on Ser-46 by host. This
phosphorylation negatively regulates capsid protein RNA-binding
activity (By similarity). Dephosphorylated by human PP1A (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08563}.
-!- MISCELLANEOUS: Structural polyprotein: Translated from a
subgenomic RNA synthesized during togaviruses replication.
{ECO:0000250|UniProtKB:P08563}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M15240; AAA88529.1; -; Genomic_RNA.
EMBL; D00242; BAA00172.1; -; Genomic_RNA.
EMBL; D00156; BAA28178.1; -; Genomic_RNA.
PIR; A24309; A24309.
PIR; A29822; GNWVR4.
RefSeq; NP_062884.1; NC_001545.2.
PDB; 5KHE; EM; 35.00 A; A/B=9-277.
PDB; 5KHF; EM; 35.00 A; A/B=9-277.
PDBsum; 5KHE; -.
PDBsum; 5KHF; -.
SMR; P07566; -.
IntAct; P07566; 2.
GeneID; 1502162; -.
KEGG; vg:1502162; -.
OrthoDB; VOG0900007P; -.
Proteomes; UP000000571; Genome.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR008819; Rubella_Capsid.
InterPro; IPR008820; Rubella_E1.
InterPro; IPR008821; Rubella_E2.
Pfam; PF05750; Rubella_Capsid; 1.
Pfam; PF05748; Rubella_E1; 1.
Pfam; PF05749; Rubella_E2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Capsid protein;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cytoplasm; Host Golgi apparatus; Host membrane;
Host mitochondrion; Host-virus interaction; Lipoprotein; Membrane;
Metal-binding; Palmitate; Phosphoprotein; Reference proteome;
RNA-binding; T=4 icosahedral capsid protein; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 300 Capsid protein.
/FTId=PRO_0000041308.
CHAIN 301 582 Spike glycoprotein E2.
/FTId=PRO_0000041309.
CHAIN 583 1063 Spike glycoprotein E1.
/FTId=PRO_0000041310.
TOPO_DOM 301 534 Extracellular. {ECO:0000255}.
TRANSMEM 535 555 Helical; Note=Golgi retention signal.
{ECO:0000250|UniProtKB:P08563}.
TOPO_DOM 556 582 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 583 1028 Extracellular. {ECO:0000255}.
TRANSMEM 1029 1049 Helical; Note=Endoplasmic reticulum
retention signal.
{ECO:0000250|UniProtKB:P08563}.
TOPO_DOM 1050 1063 Extracellular. {ECO:0000255}.
REGION 30 69 Human C1QBP/SF2P32-binding.
{ECO:0000250|UniProtKB:P08563}.
REGION 279 300 Functions as E2 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
REGION 563 582 Functions as E1 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
METAL 670 670 Calcium. {ECO:0000250|UniProtKB:P08563}.
METAL 671 671 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P08563}.
METAL 718 718 Calcium. {ECO:0000250|UniProtKB:P08563}.
METAL 719 719 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P08563}.
SITE 300 301 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 582 583 Cleavage; by host signal peptidase.
{ECO:0000255}.
MOD_RES 46 46 Phosphoserine; by host.
{ECO:0000250|UniProtKB:P08563}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P08563}.
CARBOHYD 759 759 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P08563}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P08563}.
CARBOHYD 1011 1011 O-linked (GalNAc...) threonine; by host.
{ECO:0000250|UniProtKB:P08563}.
CARBOHYD 1012 1012 O-linked (GalNAc...) threonine; by host.
{ECO:0000250|UniProtKB:P08563}.
DISULFID 153 197 {ECO:0000250|UniProtKB:P08563}.
DISULFID 590 595 {ECO:0000269|PubMed:9143273}.
DISULFID 619 824 {ECO:0000269|PubMed:9143273}.
DISULFID 641 653 {ECO:0000269|PubMed:9143273}.
DISULFID 699 712 {ECO:0000269|PubMed:9143273}.
DISULFID 758 767 {ECO:0000269|PubMed:9143273}.
DISULFID 807 817 {ECO:0000269|PubMed:9143273}.
DISULFID 931 934 {ECO:0000269|PubMed:9143273}.
DISULFID 950 983 {ECO:0000269|PubMed:9143273}.
VARIANT 87 87 T -> S.
VARIANT 163 163 E -> Q.
VARIANT 319 319 C -> R.
VARIANT 395 395 D -> A.
VARIANT 545 545 L -> S.
VARIANT 613 613 K -> R.
VARIANT 825 825 S -> A.
VARIANT 959 959 L -> V.
VARIANT 991 991 T -> S.
VARIANT 1037 1037 I -> T.
SEQUENCE 1063 AA; 114679 MW; F39B475ACA15C7D1 CRC64;
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR
RRRGNRGRGQ RRDWSRAPPP PEERQETRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP
ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH
RLLRMPVRGL DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL ATVAVGTARA
GLQPRADMAA PPTLPQPPCA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH YRNASDVLPG
HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTPLTTAAN STTAATPATA
PAPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP
WELVVLTARP EDGWTCRGVP AHPGARCPEL VSPMGRATCS PASALWLATA NALSLDHALA
AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQAP
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPA APCARIWNGT
QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE VEPAFGHSDA ACWGFPTDTV
MSVFALASYV QHPHKTVRVK FHTETRTVWQ LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP
DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV
DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
PGPLGLKFKT VRPVALPRTL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDLG
AVPPGKFVTA ALLNTPPPYQ VSCGGESDRA TARVIDPAAQ SFTGVVYGTH TTAVSETRQT
WAEWAAAHWW QLTLGAICAL PLAGLLACCA KCLYYLRGAI APR


Related products :

Catalog number Product name Quantity
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.1 mg
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.2 mg
OBT0754 MOUSE ANTI EPSTEIN_BARR VIRUS ENVELOPE GLYCOPROTEIN COMPLEX, Product Type Monoclonal Antibody, Specificity EPSTEIN_BARR VIRUS ENVELOPE GLYCOPROTEIN COMPLEX, Target Species Viral, Host Mouse, Forma 0.1 mg
SCH-OBT0754 MOUSE ANTI EPSTEIN_BARR VIRUS ENVELOPE GLYCOPROTEIN COMPLEX, Product Type Monoclonal Antibody, Specificity EPSTEIN_BARR VIRUS ENVELOPE GLYCOPROTEIN COMPLEX, Target Species Viral, Host Mouse, Forma 0.1 mg
10-271-82346 SARS-Associated Coronavirus Spike mosaic S(C) - S glycoprotein; Peplomer protein; E2 1 mg
10-271-82347 SARS-Associated Coronavirus Spike mosaic S(M) - S glycoprotein; Peplomer protein; E2 1 mg
18-003-44267 Erythrocyte membrane glycoprotein Rh50 - Rh-associated glycoprotein. isoform CRA_b; Rh-associated glycoprotein; Rh50 glycoprotein Polyclonal 0.1 mg Protein A
U0674r CLIA Adipocyte membrane protein,Cd36,Fat,Fatty acid translocase,Fatty acid transport protein,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV,Rat,Rattus norv 96T
EIAAB34629 Ammonium transporter Rh type C,C15orf6,CDRC2,Homo sapiens,Human,PDRC2,Rh family type C glycoprotein,Rh glycoprotein kidney,Rh type C glycoprotein,RHCG,Rhesus blood group family type C glycoprotein,RHG
E0674r ELISA kit Adipocyte membrane protein,Cd36,Fat,Fatty acid translocase,Fatty acid transport protein,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV,Rat,Rattu 96T
E0674r ELISA Adipocyte membrane protein,Cd36,Fat,Fatty acid translocase,Fatty acid transport protein,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV,Rat,Rattus nor 96T
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
65-102 anti_SARS spike glycoprotein antibody (clone 3A2) 250ug
65-101 anti_SARS spike glycoprotein antibody (clone 3A2) 50ug
EIAAB12958 Envelope polyprotein,EnvK2 protein,ERVK6,HERV-K(C7) envelope protein,HERV-K(HML-2.HOM) envelope protein,HERV-K_7p22.1 provirus ancestral Env polyprotein,HERV-K108 envelope protein,Homo sapiens,Human
MAB7942 SARS spike glycoprotein monoclonal antibody, clone 3A2 250 ug
E0674b ELISA kit Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674b ELISA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674b CLIA Bos taurus,Bovine,CD36,Glycoprotein IIIb,GPIIIB,GPIV,PAS IV,PAS4,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
U0674m CLIA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 96T
E0674m ELISA kit Cd36,Glycoprotein IIIb,GPIIIB,GPIV,Mouse,Mus musculus,PAS IV,PAS-4,Platelet glycoprotein 4,Platelet glycoprotein IV 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