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 POLG_FMDVI              Reviewed;        2328 AA.
P03310; Q65066; Q6PMY0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
25-OCT-2017, entry version 106.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protease;
Short=Lpro;
EC=3.4.22.46;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
AltName: Full=P52;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B-1;
Short=P3B-1;
AltName: Full=Genome-linked protein VPg1;
Contains:
RecName: Full=Protein 3B-2;
Short=P3B-2;
AltName: Full=Genome-linked protein VPg2;
Contains:
RecName: Full=Protein 3B-3;
Short=P3B-3;
AltName: Full=Genome-linked protein VPg3;
Contains:
RecName: Full=Picornain 3C;
EC=3.4.22.28;
AltName: Full=Protease 3C;
Short=P3C;
AltName: Full=Protease P20B;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
AltName: Full=P56A;
Foot-and-mouth disease virus (isolate -/Brazil/C3Indaial/1971 serotype
C) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12117;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9850; Cervidae (deer).
NCBI_TaxID=9363; Erinaceidae (hedgehogs).
NCBI_TaxID=9785; Loxodonta africana (African elephant).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15858032; DOI=10.1128/JVI.79.10.6487-6504.2005;
Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A.,
Kutish G.F., Rock D.L.;
"Comparative genomics of foot-and-mouth disease virus.";
J. Virol. 79:6487-6504(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 202-933.
PubMed=1316467;
Martinez M.A., Dopazo J., Hernandez J., Mateu M.G., Sobrino F.,
Domingo E., Knowles N.J.;
"Evolution of the capsid protein genes of foot-and-mouth disease
virus: antigenic variation without accumulation of amino acid
substitutions over six decades.";
J. Virol. 66:3557-3565(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 714-947.
PubMed=6298715; DOI=10.1093/nar/10.24.8285;
Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.;
"Comparison of the amino acid sequence of the major immunogen from
three serotypes of foot and mouth disease virus.";
Nucleic Acids Res. 10:8285-8295(1982).
-!- FUNCTION: The leader protease autocatalytically cleaves itself
from the polyprotein at the L/VP0 junction. It cleaves the host
translation initiation factors EIF4G1 and EIF4G3, in order to shut
down the capped cellular mRNA transcription. Increases translation
driven by the viral internal ribosome entry site (IRES).
{ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P03311}.
-!- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed
capsid enclosing the viral positive strand RNA genome. VP4 lies on
the inner surface of the protein shell formed by VP1, VP2 and VP3.
All the three latter proteins contain a beta-sheet structure
called beta-barrel jelly roll. Together they form an icosahedral
capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with
a diameter of approximately 300 Angstroms. VP1 is situated at the
12 fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The capsid interacts with host heparan sulfate and
various integrins (alphavbeta1, alphavbeta3, alpha5beta1,
alphavbeta6, alphavbeta8) to provide virion attachment to target
Attachment via host integrins induces virion internalization
predominantly through clathrin-mediated endocytosis (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the
5'-end of both the positive-strand and negative-strand genomic
RNAs. They acts as a genome-linked replication primer (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Autocatalytically cleaves itself from the
polyprotein of the foot-and-mouth disease virus by hydrolysis of a
Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-
4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: VP1 interacts (via RGD) with integrins heterodimers
alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B-1: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-2: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-3: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Lab;
IsoId=P03310-1; Sequence=Displayed;
Name=Lb;
IsoId=P03310-2; Sequence=VSP_046531;
-!- PTM: Specific enzymatic cleavages in vivo by the viral proteases
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates such as VP0 which is a VP4-VP2 precursor
are produced. During virion maturation, non-infectious particles
are rendered infectious following cleavage of VP0. This maturation
cleavage is followed by a conformational change of the particle.
The polyprotein seems to be cotranslationally cleaved at the 2A/2B
junction by a ribosomal skip from one codon to the next without
formation of a peptide bond. This process would release the L-P1-
2A peptide from the translational complex (By similarity).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the
polymerase and are covalently linked to the 5'-end of genomic RNA.
These uridylylated forms act as a nucleotide-peptide primer for
the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The capsid protein VP1 contains the main antigenic
determinants of the virion; therefore, changes in its sequence
must be responsible for the high antigenic variability of the
virus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
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EMBL; AY593806; AAT01749.1; -; Genomic_RNA.
EMBL; M90376; AAA91492.1; -; Genomic_RNA.
EMBL; J02184; AAA42618.1; -; Genomic_RNA.
PIR; A03912; A03912.
ProteinModelPortal; P03310; -.
SMR; P03310; -.
PRIDE; P03310; -.
OrthoDB; VOG0900006M; -.
Proteomes; UP000012668; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR004080; FMDV_VP1_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008739; Peptidase_C28.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF05408; Peptidase_C28; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
PRINTS; PR00918; CALICVIRUSNS.
PRINTS; PR01542; FMDVP1COAT.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
Alternative initiation; ATP-binding; Capsid protein;
Clathrin- and caveolin-independent endocytosis of virus by host;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
Host-virus interaction; Hydrolase; Ion channel; Ion transport;
Lipoprotein; Membrane; Modulation of host chromatin by virus;
Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Translation regulation; Transport;
Viral attachment to host cell; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 2328 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000422504.
CHAIN 1 201 Leader protease. {ECO:0000250}.
/FTId=PRO_0000422505.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000422506.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000422507.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000422508.
CHAIN 505 723 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039869.
CHAIN 724 931 Protein VP1. {ECO:0000250}.
/FTId=PRO_0000039870.
CHAIN 932 949 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039871.
CHAIN 950 1103 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000422509.
CHAIN 1104 1421 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000422510.
CHAIN 1422 1574 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000422511.
CHAIN 1575 1597 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_0000422512.
CHAIN 1598 1621 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_0000422513.
CHAIN 1622 1645 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_0000422514.
CHAIN 1646 1858 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000422515.
CHAIN 1859 2328 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000422516.
TOPO_DOM 1 1476 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1477 1497 {ECO:0000255}.
TOPO_DOM 1498 2328 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 201 Peptidase C28.
DOMAIN 1185 1349 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1648 1832 Peptidase C3.
DOMAIN 2092 2210 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1213 1220 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 865 867 Cell attachment site. {ECO:0000250}.
ACT_SITE 51 51 For leader protease activity.
{ECO:0000250}.
ACT_SITE 148 148 For leader protease activity.
{ECO:0000250}.
ACT_SITE 163 163 For leader protease activity.
{ECO:0000250}.
ACT_SITE 1691 1691 For picornain 3C activity; Proton
donor/acceptor.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
ACT_SITE 1729 1729 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306}.
ACT_SITE 1808 1808 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
SITE 201 202 Cleavage; by leader protease.
{ECO:0000255}.
SITE 286 287 Cleavage. {ECO:0000255}.
SITE 504 505 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 723 724 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 931 932 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 949 950 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1103 1104 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1421 1422 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1574 1575 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1597 1598 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1621 1622 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1645 1646 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1858 1859 Cleavage; by picornain 3C. {ECO:0000255}.
MOD_RES 1577 1577 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1600 1600 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1624 1624 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 202 202 N-myristoyl glycine; by host.
{ECO:0000250}.
DISULFID 511 511 Interchain; in VP3 dimer. {ECO:0000250}.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_046531.
VARIANT 330 330 S -> A.
VARIANT 376 376 V -> A.
VARIANT 420 420 D -> E.
VARIANT 458 458 N -> K.
VARIANT 515 515 Y -> F.
VARIANT 560 560 T -> M.
VARIANT 638 638 N -> S.
VARIANT 677 677 E -> D.
VARIANT 722 722 Q -> L.
VARIANT 747 747 T -> I.
VARIANT 766 766 Q -> H.
VARIANT 805 805 H -> Q.
VARIANT 825 825 T -> A.
VARIANT 852 852 A -> T.
VARIANT 861 863 TGV -> ASA.
VARIANT 917 917 A -> T.
SEQUENCE 2328 AA; 258282 MW; B2D0CE9A4BA94622 CRC64;
MNTTDCFIAL VHAIREIKTH FFSRYTGRME FTLHNGEKKI FYSRPNNHDN CWLNTILQLF
RYVDEPFFDW VYNSPENLTL SAIEQLEKLT GLELREGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSDGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG GWKANVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTY GYATTEDSTS GPNTSGLETR VHQAERFFKM TLFEWVPSQS
FGHMHKVVLP SEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD
REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYNQH KPWTLVVMVV APLTVNTSGA
QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CADGYGNMVT TDPKTADPAY GKVYNPPRTA
LPGRFTNYLD VAEACPTLLT FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
YTQYAGTINL HFMFTGPTDA KARYMVAYVP PGMEAPDNPE EAAHCIHAEW DTGLNSKFTF
SIPYISAADY AYTASSEAET TSVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA
RQQTTTTGES ADPVTTTVEN YGGETQTQRR HHTDVAFVLD RFVKVQVSGN QHTLDVMQVH
KDSIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LDNTTNPTAY HKGPLTRLAL
PYTAPHRVLA TAYTGTTAYT TGVRRGDLAH LAAAHARHLP TSFNFGAVKA ETITELLVRM
KRAELYCPRP VLPVQPAGDR HKQPLIAPAK QLLNFDLLKL AGDVESNPGP FFFSDVRSNF
SKLVETINQM QEDMSTKHGP DFNRLVSAFE ELATGVKAIR TGLDEAKPWY KLIKLLSRLS
CMAAVAARSK DPVLVAIMLA DTGLEILDST FVVKKISDSL SSLFHVPAPV FSFGAPILLA
GLVKVASSFF RSTPEDLERA EKQLKARDIN DIFAILKNGE WLVKLILAIR DWIKAWIASE
EKFVTMTDLV PGILEKQRDL NDPSKYKEAK EWLDNARQAC LKNGNTHIAN LCKVVAPAPS
KSRPEPVVVC LRGKSGQGKS FLANVLAQAI STHFTGRTDS VWYCPPDPDH FDGYNQQTVV
VMDDLGQNPD GKDFKYFAQM VSTTGFIPPM ASLEDKGKPF NSKVIIATTN LYSGFTPRTM
VCPDALNRRF HFDIDVSAKD GYKINNKLDI IKALEDTHTN PVAMFQYDCA LLNGMAVEMK
RMQQDMFKPQ PPLQNVYQLV QEVIERVELH EKVSSHPIFK QISIPSQKSV LYFLIEKGQH
EAAIEFFEGM VHDSIKEELR PLIQQTSFVK RAFKRLKENF EIVALCLTLL ANIVIMIRET
RKRQQMVDDA VNEYIEKANI TTDDKTLDEA EKNPLETSGA STVGFRERTL PGHKARDDVN
SEPAQPVEEQ PQAEGPYAGP LERQKPLKVR AKLPQQEGPY AGPMERQKPL KVKAKAPVVK
EGPYEGPVKK PVALKVKAKN LIVTESGAPP TDLQKMVMGN TKPVELILDG KTVAICCATG
VFGTAYLVPR HLFAEKYDKI MLDGRAMTDS DYRVFEFEIK VKGQDMLSDA ALMVLHRGNR
VRDITKHFRD TARMKKGTPV VGVINNADVG RLIFSGEALT YKDIVVCMDG DTMPGLFAYR
AATKAGYCGG AVLAKDGADT FIVGTHSAGG NGVGYCSCVS RSMLLKMKAH IDPEPHHEGL
IVDTRDVEER VHVMRKTKLA PTVAHGVFNP DFGPAALSNR DPRLNEGVVL DEVIFSKHKG
DTKMSEEDKA LFRRCAADYA SRLHSVLGTA NAPLSIYEAI KGVDGLDAME PDTAPGLPWA
LQGKRRGALI DFENGTVGPE VEAALKLMEK REYKFACQTF LKDEIRPMEK VRAGKTRIVD
VLPVEHILYT RMMIGRFCAQ MHSNNGPQIG SAVGCNPDVD WQRFGTHFAQ YRNVWDVDYS
AFDANHCSDA MNIMFEEVFR TEFGFHPNAE WILKTLVNTE HAYENKRITV EGGMPSGCSA
TSIINTILNN IYVLYALRRH YEGVELDTYT MISYGDDIVV ASDYDLDFEA LKPHFKSIGQ
TITPADKSDK GFVLGHSITD VTFLKRHFHM DYGTGFYKPV MASKTLEAIL SFARRGTIQE
KLISVAGLAV HSGPDEYRRL FEPFQGLFEI PSYRSLYLRW VNAVCGDA


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