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

 POLG_FMDV5              Reviewed;        2332 AA.
P03307; Q6PN05;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
25-OCT-2017, entry version 108.
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 -/Germany/A5Westerwald/1951
serotype A) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12113;
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=6194987;
Beck E., Feil G., Strohmaier K.;
"The molecular basis of the antigenic variation of foot-and-mouth
disease virus.";
EMBO J. 2:555-559(1983).
[2]
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).
-!- 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=P03307-1; Sequence=Displayed;
Name=Lb;
IsoId=P03307-2; Sequence=VSP_046529;
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAA24365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY593781; AAT01724.1; -; Genomic_RNA.
EMBL; V01135; CAA24365.1; ALT_INIT; Genomic_RNA.
EMBL; V01135; CAA24366.1; ALT_SEQ; Genomic_RNA.
PIR; A03909; A03909.
ProteinModelPortal; P03307; -.
SMR; P03307; -.
MEROPS; C28.001; -.
OrthoDB; VOG090000PJ; -.
Proteomes; UP000012669; 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.
1: Evidence at protein level;
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 2331 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000422477.
CHAIN 1 201 Leader protease. {ECO:0000250}.
/FTId=PRO_0000422478.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000422479.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000422480.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000422481.
CHAIN 505 725 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039830.
CHAIN 726 935 Protein VP1. {ECO:0000255}.
/FTId=PRO_0000039831.
CHAIN 936 953 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039832.
CHAIN 954 1107 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000422482.
CHAIN 1108 1425 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000422483.
CHAIN 1426 1578 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000422484.
CHAIN 1579 1601 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_0000422485.
CHAIN 1602 1625 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_0000422486.
CHAIN 1626 1649 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_0000422487.
CHAIN 1650 1862 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000422488.
CHAIN 1863 2332 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000422489.
TOPO_DOM 1 1480 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1481 1501 {ECO:0000255}.
TOPO_DOM 1502 2332 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 201 Peptidase C28.
DOMAIN 1189 1353 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1652 1836 Peptidase C3.
DOMAIN 2096 2214 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1217 1224 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 868 870 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 1695 1695 For picornain 3C activity; Proton
donor/acceptor.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
ACT_SITE 1733 1733 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306}.
ACT_SITE 1812 1812 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 725 726 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 935 936 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 953 954 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1107 1108 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1425 1426 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1578 1579 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1601 1602 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1625 1626 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1649 1650 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1862 1863 Cleavage; by picornain 3C. {ECO:0000255}.
MOD_RES 1581 1581 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1604 1604 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1628 1628 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 202 202 N-myristoyl glycine; by host.
{ECO:0000250}.
DISULFID 511 511 Interchain; in VP3 dimer.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_046529.
VARIANT 746 746 E -> D.
VARIANT 753 755 HHT -> YYM.
VARIANT 871 871 T -> M.
VARIANT 874 874 P -> A.
VARIANT 894 894 V -> I.
SEQUENCE 2332 AA; 259336 MW; CD295048EBAA0EFC CRC64;
MHTTDCFIAL VHAIREIRAL FLPRTTGKME LTLHNGEKKT FYSRPNNHDN CWLNTILQLF
RYVDEPFFDW VYNSPENLTL EAINQLEELT GLELHEGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEEFYPW TPDPSDVLVF
VPYDQEPLNG DWKAMVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI
LTTRNGHTIS TTQSSVGVTY GYSTGEDHVA GPNTSGLETR VVQAERFFKK FLFDWTTDKP
FGHLEKLELP ADHHGVFGHL VESYAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKEFEQ
REKYQLTLFP HQFISPRTNM TAHITVPYLG VNRYDQYKKH KPWTLVVMVV SPLTVSDTAA
AQIKVYANIA PTYVHVAGEL PSKEGIFPVA CSDGYGGLVT TDPKTADPAY GKVYNPPRTN
YPGRFTNLLD VAEACPTFLC FDDGKPYVVT RTDDTRLLAK FDVSLAAKHM SNTYLSGIAQ
YYAQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVEVPPDT PERAAHCIHA EWDTGLNSKF
TFSIPYVSAA DYAYTASDTA ETTNVQGWVC IYQITHGKAE NDTLVVSASA GKDFELRLPI
DPRQQTTAVG ESADPVTTTV ENYGGETQTQ RRHHTDVGFI MDRFVKINSL SPTHVIDLMQ
THQHGLVGAL LRAATYYFSD LEIVVRHDGN LTWVPNGAPE AALSNTSNPT AYNKAPFTRL
ALPYTAPHRV LATVYNGTNK YSTGGPRRGD TGSPAARAAK QLPASFNYGA IRAVTIHELL
VRMKRAELYC PRPLLAIEVS SQDRHKQKII APARQLLNFD LLKLAGDVES NPGPFFFSDV
RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAAGV KAIRTGLDEA KPWYKLIKLL
SRLSCMAAVA ARSKDPVLVA IMLADTGLEI LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP
ILLAGLVKVA SSFFRSTPED LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW
IASEEKFVTM TDLVPGILEK QHDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
PAPSKPRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RTDSVWYCPP DPDHFDGYNQ
QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK GKPFNSKVII ATTNLYSGFT
PRTMVCPDAL NRRFHFDIDV SAKDGYKINN KLDITKALED THTNPVAMFQ YDCALLNGMA
VEMKRMQQDM FKPQPPLQNV YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIK
KGQHEAAIEF FEGMVHDSVK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKNPLE TSGASTVGFR ERTLPGQKAR
DDVNSEPAQP AEEQPQAEGP YAGPLERQRP LKVRAKLPQQ EGPYAGPMER QKPLKVKAKA
PVVKEGPYEG PVKKPVALKV RAKNLIVTES GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC
CATGVFGTAY LVPRHLFAEK YDKIMLDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH
RGNRVRDITK HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK MKAHIDPEPH
HEGLIVDTRD AEERVHVMRK TKLAPTVAHG VFNPEFGPAA LSNKDPRLNE GVVLDEVIFS
KHKGDTKMSE EDKALFRRCA ADYASRLHSV LGTANAPLSI YEAIKGVDGL DAMEPDTAPG
LPWALQGKRR GALIDFENGT VGPEVEAALK LMEKREYKFV CQTFLKDEIR PMEKVRAGKT
RIVDVLPVEH ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
VDYSAFDANH CSDAMNIMFE EVFRTDFGFH PNAEWILKTL VNTEHAYENK RHTVEGGMPS
GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD DIVVASDYDL DFEALKPHFK
SLGQTITPAD KSDKGFVLGH SITDVTFLKR HFHMDYGTGF YKPVMASKTL EAILSFARRG
TIQEKLISVA GLAVHSGPDE YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA


Related products :

Catalog number Product name Quantity


 

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