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

Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

 POLG_HCVEV              Reviewed;        3014 AA.
O39928;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 141.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Core protein p21;
AltName: Full=Capsid protein C;
AltName: Full=p21;
Contains:
RecName: Full=Core protein p19;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp32;
AltName: Full=gp35;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=NS1;
AltName: Full=gp68;
AltName: Full=gp70;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Protease NS2-3;
Short=p23;
EC=3.4.22.-;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.98;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Hepacivirin;
AltName: Full=NS3P;
AltName: Full=p70;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
AltName: Full=p8;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
AltName: Full=p56;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
AltName: Full=p68;
Hepatitis C virus genotype 5a (isolate EUH1480) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=356419;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9223423; DOI=10.1006/bbrc.1997.6902;
Chamberlain R.W., Adams N.J., Taylor L.A., Simmonds P., Elliot R.M.;
"The complete coding sequence of hepatitis C virus genotype 5a, the
predominant genotype in South Africa.";
Biochem. Biophys. Res. Commun. 236:44-49(1997).
[2]
REVIEW.
PubMed=10718937; DOI=10.1046/j.1365-2893.2000.00201.x;
McLauchlan J.;
"Properties of the hepatitis C virus core protein: a structural
protein that modulates cellular processes.";
J. Viral Hepat. 7:2-14(2000).
[3]
REVIEW, AND SUBCELLULAR LOCATION.
PubMed=14752815; DOI=10.1002/hep.20032;
Penin F., Dubuisson J., Rey F.A., Moradpour D., Pawlotsky J.-M.;
"Structural biology of hepatitis C virus.";
Hepatology 39:5-19(2004).
[4]
INTERACTION WITH HNRNPA1 AND SEPT6.
PubMed=17229681; DOI=10.1128/JVI.01311-06;
Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.;
"An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6,
facilitate hepatitis C virus replication.";
J. Virol. 81:3852-3865(2007).
-!- FUNCTION: Core protein packages viral RNA to form a viral
nucleocapsid, and promotes virion budding. Modulates viral
translation initiation by interacting with HCV IRES and 40S
ribosomal subunit. Also regulates many host cellular functions
such as signaling pathways and apoptosis. Prevents the
establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling
pathways and by inducing human STAT1 degradation. Thought to play
a role in virus-mediated cell transformation leading to
hepatocellular carcinomas. Interacts with, and activates STAT3
leading to cellular transformation. May repress the promoter of
p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the
cytoplasm. Also represses cell cycle negative regulating factor
CDKN1A, thereby interrupting an important check point of normal
cell cycle regulation. Targets transcription factors involved in
the regulation of inflammatory responses and in the immune
response: suppresses NK-kappaB activation, and activates AP-1.
Could mediate apoptotic pathways through association with TNF-type
receptors TNFRSF1A and LTBR, although its effect on death
receptor-induced apoptosis remains controversial. Enhances TRAIL
mediated apoptosis, suggesting that it might play a role in
immune-mediated liver cell injury. Seric core protein is able to
bind C1QR1 at the T-cell surface, resulting in down-regulation of
T-lymphocytes proliferation. May transactivate human MYC, Rous
sarcoma virus LTR, and SV40 promoters. May suppress the human FOS
and HIV-1 LTR activity. Alters lipid metabolism by interacting
with hepatocellular proteins involved in lipid accumulation and
storage. Core protein induces up-regulation of FAS promoter
activity, and thereby probably contributes to the increased
triglyceride accumulation in hepatocytes (steatosis) (By
similarity). {ECO:0000250}.
-!- FUNCTION: E1 and E2 glycoproteins form a heterodimer that is
involved in virus attachment to the host cell, virion
internalization through clathrin-dependent endocytosis and fusion
with host membrane. E1/E2 heterodimer binds to human LDLR, CD81
and SCARB1/SR-BI receptors, but this binding is not sufficient for
infection, some additional liver specific cofactors may be needed.
The fusion function may possibly be carried by E1. E2 inhibits
human EIF2AK2/PKR activation, preventing the establishment of an
antiviral state. E2 is a viral ligand for CD209/DC-SIGN and
CLEC4M/DC-SIGNR, which are respectively found on dendritic cells
(DCs), and on liver sinusoidal endothelial cells and macrophage-
like cells of lymph node sinuses. These interactions allow capture
of circulating HCV particles by these cells and subsequent
transmission to permissive cells. DCs act as sentinels in various
tissues where they entrap pathogens and convey them to local
lymphoid tissue or lymph node for establishment of immunity.
Capture of circulating HCV particles by these SIGN+ cells may
facilitate virus infection of proximal hepatocytes and lymphocyte
subpopulations and may be essential for the establishment of
persistent infection (By similarity). {ECO:0000250}.
-!- FUNCTION: P7 seems to be a heptameric ion channel protein
(viroporin) and is inhibited by the antiviral drug amantadine.
Also inhibited by long-alkyl-chain iminosugar derivatives.
Essential for infectivity (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease NS2-3 is a cysteine protease responsible for
the autocatalytic cleavage of NS2-NS3. Seems to undergo self-
inactivation following maturation (By similarity). {ECO:0000250}.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase. NS3 serine protease, in
association with NS4A, is responsible for the cleavages of NS3-
NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also
prevents phosphorylation of human IRF3, thus preventing the
establishment of dsRNA induced antiviral state. NS3 RNA helicase
binds to RNA and unwinds dsRNA in the 3' to 5' direction, and
likely RNA stable secondary structure in the template strand.
Cleaves and inhibits the host antiviral protein MAVS (By
similarity). {ECO:0000250}.
-!- FUNCTION: NS4B induces a specific membrane alteration that serves
as a scaffold for the virus replication complex. This membrane
alteration gives rise to the so-called ER-derived membranous web
that contains the replication complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: NS5A is a component of the replication complex involved
in RNA-binding. Its interaction with Human VAPB may target the
viral replication complex to vesicles. Down-regulates viral IRES
translation initiation. Mediates interferon resistance, presumably
by interacting with and inhibiting human EIF2AK2/PKR. Seems to
inhibit apoptosis by interacting with BIN1 and FKBP8. The
hyperphosphorylated form of NS5A is an inhibitor of viral
replication (By similarity). {ECO:0000250}.
-!- FUNCTION: NS5B is an RNA-dependent RNA polymerase that plays an
essential role in the virus replication. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of four peptide bonds in the viral
precursor polyprotein, commonly with Asp or Glu in the P6
position, Cys or Thr in P1 and Ser or Ala in P1'.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
-!- ENZYME REGULATION: Activity of auto-protease NS2-3 is dependent on
zinc ions and completely inhibited by EDTA. Serine protease NS3 is
also activated by zinc ions (By similarity). {ECO:0000250}.
-!- SUBUNIT: Core protein is a homomultimer that binds the C-terminal
part of E1 and interacts with numerous cellular proteins.
Interaction with human STAT1 SH2 domain seems to result in
decreased STAT1 phosphorylation, leading to decreased IFN-
stimulated gene transcription. In addition to blocking the
formation of phosphorylated STAT1, the core protein also promotes
ubiquitin-mediated proteasome-dependent degradation of STAT1.
Interacts with, and constitutively activates human STAT3.
Associates with human LTBR and TNFRSF1A receptors and possibly
induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK,
C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins.
Interacts with human CREB3 nuclear transcription protein,
triggering cell transformation. May interact with human p53. Also
binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1
and E2 glycoproteins form a heterodimer that binds to human LDLR,
CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human
EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR.
p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing
a pair of composite active sites at the dimerization interface.
NS2 seems to interact with all other non-structural (NS) proteins.
NS4A interacts with NS3 serine protease and stabilizes its
folding. NS3-NS4A complex is essential for the activation of the
latter and allows membrane anchorage of NS3. NS3 interacts with
human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form
homodimers and seem to interact with all other non-structural (NS)
proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2,
BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B
is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Core protein p21: Host endoplasmic reticulum
membrane {ECO:0000250}; Single-pass membrane protein
{ECO:0000250}. Host mitochondrion membrane {ECO:0000250}; Single-
pass type I membrane protein {ECO:0000250}. Host lipid droplet
{ECO:0000250}. Note=The C-terminal transmembrane domain of core
protein p21 contains an ER signal leading the nascent polyprotein
to the ER membrane. Only a minor proportion of core protein is
present in the nucleus and an unknown proportion is secreted.
-!- SUBCELLULAR LOCATION: Core protein p19: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Secreted
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E1 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E2 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: p7: Host endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
cell membrane {ECO:0000250}. Note=The C-terminus of p7 membrane
domain acts as a signal sequence. After cleavage by host signal
peptidase, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. Only a fraction
localizes to the plasma membrane.
-!- SUBCELLULAR LOCATION: Protease NS2-3: Host endoplasmic reticulum
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=NS3 is associated to the ER membrane through
its binding to NS4A.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000305}; Single-pass type I membrane
protein {ECO:0000305}. Note=Host membrane insertion occurs after
processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5A: Host endoplasmic
reticulum membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Host cytoplasm, host perinuclear region
{ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Host
membrane insertion occurs after processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host
endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Note=Host membrane insertion
occurs after processing by the NS3 protease.
-!- DOMAIN: The transmembrane regions of envelope E1 and E2
glycoproteins are involved in heterodimer formation, ER
localization, and assembly of these proteins. Envelope E2
glycoprotein contain a highly variable region called hypervariable
region 1 (HVR1). E2 also contains two segments involved in CD81-
binding. HVR1 is implicated in the SCARB1-mediated cell entry.
CD81-binding regions may be involved in sensitivity and/or
resistance to IFN-alpha therapy (By similarity). {ECO:0000250}.
-!- DOMAIN: The N-terminus of NS5A act as membrane anchor. The central
part of NS5A seems to be intrinsically disordered and interacts
with NS5B and host PKR (By similarity). {ECO:0000250}.
-!- DOMAIN: The SH3-binding domain of NS5A is involved in the
interaction with human Bin1, GRB2 and Src-family kinases.
{ECO:0000250}.
-!- DOMAIN: The N-terminal one-third of serine protease NS3 contains
the protease activity. This region contains a zinc atom that does
not belong to the active site, but may play a structural rather
than a catalytic role. This region is essential for the activity
of protease NS2-3, maybe by contributing to the folding of the
latter. The helicase activity is located in the C-terminus of NS3
(By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The structural proteins, core, E1, E2 and p7 are produced by
proteolytic processing by host signal peptidases. The core protein
is synthesized as a 21 kDa precursor which is retained in the ER
membrane through the hydrophobic signal peptide. Cleavage by the
signal peptidase releases the 19 kDa mature core protein. The
other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are
cleaved by the viral proteases (By similarity). {ECO:0000250}.
-!- PTM: Envelope E1 and E2 glycoproteins are highly N-glycosylated.
{ECO:0000250}.
-!- PTM: Core protein is phosphorylated by host PKC and PKA.
{ECO:0000250}.
-!- PTM: NS5A is phosphorylated in a basal form termed p56. p58 is a
hyperphosphorylated form of p56. p56 and p58 coexist in the cell
in roughly equivalent amounts. Hyperphosphorylation is dependent
on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1,
MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for
NS5A phosphorylation (By similarity). {ECO:0000250}.
-!- PTM: NS4B is palmitoylated. This modification may play a role in
its polymerization or in protein-protein interactions (By
similarity). {ECO:0000250}.
-!- PTM: The N-terminus of a fraction of NS4B molecules seems to be
relocated post-translationally from the cytoplasm to the ER lumen,
with a 5th transmembrane segment. The C-terminus of NS2 may be
lumenal with a fourth transmembrane segment (By similarity).
{ECO:0000250}.
-!- PTM: Core protein is ubiquitinated; mediated by UBE3A and leading
to core protein subsequent proteasomal degradation. {ECO:0000250}.
-!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
mutations in NS5A, reducing its inhibitory effect on replication.
{ECO:0000250}.
-!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
B virus when HCV and HBV coinfect the same cell, by suppressing
HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
{ECO:0000305}.
-!- CAUTION: The core gene probably also codes for alternative reading
frame proteins (ARFPs). Many functions depicted for the core
protein might belong to the ARFPs. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y13184; CAA73640.1; -; Genomic_RNA.
PIR; JC5620; JC5620.
RefSeq; YP_001469633.1; NC_009826.1.
PDB; 2M6X; NMR; -; A/B/C/D/E/F=748-810.
PDBsum; 2M6X; -.
ProteinModelPortal; O39928; -.
SMR; O39928; -.
GeneID; 11027170; -.
KEGG; vg:11027170; -.
euHCVdb; Y13184; -.
KO; K19358; -.
OrthoDB; VOG09000032; -.
Proteomes; UP000007536; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR004109; Peptidase_S29.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
Pfam; PF01543; HCV_capsid; 1.
Pfam; PF01542; HCV_core; 1.
Pfam; PF01539; HCV_env; 1.
Pfam; PF01560; HCV_NS1; 1.
Pfam; PF01538; HCV_NS2; 1.
Pfam; PF01006; HCV_NS4a; 1.
Pfam; PF01001; HCV_NS4b; 1.
Pfam; PF01506; HCV_NS5a; 1.
Pfam; PF08300; HCV_NS5a_1a; 1.
Pfam; PF08301; HCV_NS5a_1b; 1.
Pfam; PF12941; HCV_NS5a_C; 1.
Pfam; PF02907; Peptidase_S29; 1.
Pfam; PF00998; RdRP_3; 1.
ProDom; PD001388; HCV_env; 1.
SMART; SM00487; DEXDc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51693; HCV_NS2_PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activation of host autophagy by virus;
Apoptosis; ATP-binding; 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;
G1/S host cell cycle checkpoint dysregulation by virus; Glycoprotein;
Helicase; Host cell membrane; Host cytoplasm;
Host endoplasmic reticulum; Host lipid droplet; Host membrane;
Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host TRAFs by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Lipoprotein; Membrane; Metal-binding;
Modulation of host cell cycle by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Oncogene; Palmitate;
Phosphoprotein; Protease; Ribonucleoprotein; RNA-binding;
RNA-directed RNA polymerase; Secreted; Serine protease; SH3-binding;
Thiol protease; Transcription; Transcription regulation; Transferase;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral ion channel; Viral nucleoprotein;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 191 Core protein p21. {ECO:0000255}.
/FTId=PRO_0000045556.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000045557.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000045558.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000045559.
CHAIN 384 747 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000045560.
CHAIN 748 810 p7. {ECO:0000250}.
/FTId=PRO_0000045561.
CHAIN 811 1027 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000045562.
CHAIN 1028 1658 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000045563.
CHAIN 1659 1712 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000045564.
CHAIN 1713 1973 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000045565.
CHAIN 1974 2423 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000045566.
CHAIN 2424 3014 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000045567.
TOPO_DOM 2 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TOPO_DOM 190 358 Lumenal. {ECO:0000255}.
TRANSMEM 359 379 Helical. {ECO:0000255}.
TOPO_DOM 380 726 Lumenal. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TOPO_DOM 748 758 Lumenal. {ECO:0000255}.
TRANSMEM 759 779 Helical. {ECO:0000255}.
TOPO_DOM 780 783 Cytoplasmic. {ECO:0000255}.
TRANSMEM 784 804 Helical. {ECO:0000255}.
TOPO_DOM 805 814 Lumenal. {ECO:0000255}.
TRANSMEM 815 835 Helical. {ECO:0000255}.
TOPO_DOM 836 882 Cytoplasmic. {ECO:0000255}.
TRANSMEM 883 903 Helical. {ECO:0000255}.
TOPO_DOM 904 929 Lumenal. {ECO:0000255}.
TRANSMEM 930 950 Helical. {ECO:0000255}.
TOPO_DOM 951 1658 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1659 1679 Helical. {ECO:0000255}.
TOPO_DOM 1680 1806 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1807 1827 Helical. {ECO:0000255}.
TOPO_DOM 1828 1829 Lumenal. {ECO:0000255}.
TRANSMEM 1830 1850 Helical. {ECO:0000255}.
TOPO_DOM 1851 1851 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1852 1872 Helical. {ECO:0000255}.
TOPO_DOM 1873 1882 Lumenal. {ECO:0000255}.
TRANSMEM 1883 1903 Helical. {ECO:0000255}.
TOPO_DOM 1904 1973 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1974 2003 {ECO:0000250}.
TOPO_DOM 2004 2993 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2994 3014 Helical. {ECO:0000250}.
DOMAIN 904 1027 Peptidase C18. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
DOMAIN 1028 1209 Peptidase S29. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
DOMAIN 1218 1351 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1362 1539 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2637 2755 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1231 1238 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 59 Interaction with DDX3X. {ECO:0000250}.
REGION 2 23 Interaction with STAT1. {ECO:0000250}.
REGION 122 173 Interaction with APOA2. {ECO:0000250}.
REGION 150 159 Mitochondrial targeting signal.
{ECO:0000250}.
REGION 164 167 Important for lipid droplets
localization. {ECO:0000250}.
REGION 265 296 Fusion peptide. {ECO:0000255}.
REGION 385 411 HVR1. {ECO:0000250}.
REGION 483 495 CD81-binding 1. {ECO:0000255}.
REGION 523 554 CD81-binding 2. {ECO:0000255}.
REGION 661 672 PKR/eIF2-alpha phosphorylation homology
domain (PePHD). {ECO:0000250}.
REGION 1680 1691 NS3-binding (by NS4A). {ECO:0000255}.
REGION 2121 2334 Transcriptional activation.
{ECO:0000255}.
REGION 2121 2209 FKBP8-binding. {ECO:0000255}.
REGION 2201 2251 Basal phosphorylation. {ECO:0000250}.
REGION 2211 2276 PKR-binding. {ECO:0000255}.
REGION 2250 2307 NS4B-binding. {ECO:0000255}.
REGION 2353 2423 Basal phosphorylation. {ECO:0000250}.
MOTIF 5 13 Nuclear localization signal.
{ECO:0000255}.
MOTIF 38 43 Nuclear localization signal.
{ECO:0000255}.
MOTIF 58 64 Nuclear localization signal.
{ECO:0000255}.
MOTIF 66 71 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1317 1320 DECH box. {ECO:0000250}.
MOTIF 2323 2326 SH3-binding. {ECO:0000255}.
MOTIF 2328 2337 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 757 761 Poly-Ala.
COMPBIAS 2280 2328 Pro-rich.
COMPBIAS 2995 3002 Poly-Leu.
ACT_SITE 953 953 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 973 973 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 994 994 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 1084 1084 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1108 1108 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1166 1166 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1124 1124 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1126 1126 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1172 1172 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1176 1176 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 2012 2012 Zinc. {ECO:0000250}.
METAL 2030 2030 Zinc. {ECO:0000250}.
METAL 2032 2032 Zinc. {ECO:0000250}.
METAL 2053 2053 Zinc. {ECO:0000250}.
SITE 177 178 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 191 192 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 383 384 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 747 748 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 810 811 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1027 1028 Cleavage; by protease NS2-3.
{ECO:0000255|PROSITE-ProRule:PRU01030}.
SITE 1658 1659 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1712 1713 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1973 1974 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 2423 2424 Cleavage; by serine protease NS3.
{ECO:0000255}.
MOD_RES 2 2 N-acetylserine; by host. {ECO:0000250}.
MOD_RES 53 53 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 99 99 Phosphoserine; by host. {ECO:0000250}.
MOD_RES 116 116 Phosphoserine; by host PKA.
{ECO:0000250}.
MOD_RES 2195 2195 Phosphoserine; by host; in p56.
{ECO:0000250}.
MOD_RES 2198 2198 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2202 2202 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2205 2205 Phosphoserine; by host; in p58.
{ECO:0000250}.
LIPID 1973 1973 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 577 577 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 2115 2163 {ECO:0000250}.
HELIX 749 763 {ECO:0000244|PDB:2M6X}.
HELIX 766 787 {ECO:0000244|PDB:2M6X}.
HELIX 795 803 {ECO:0000244|PDB:2M6X}.
SEQUENCE 3014 AA; 327671 MW; 84934E2B77A1964B CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPKLGVRATR KNSERSQPRG
RRQPIPKARR PTGRSWGQPG YPWPLYANEG LGWAGWLLSP RSSRPNWGPN DPRRKSPNLG
RVIHTLTCGF PHLMGYIPLV GGPVGGVSRA LAHGVKVLED GINYATGNLP GCPFSIFVLA
LLWCLTVPAS AVPYRNASGV YHVTNDCPNS SIVYEADNLI LHAPGCVPCV LEDNVSRCWV
QITPTLSAPS FGAVTALLRR AVDYLAGGAA FCSALYVGDA CGALSLVGQM FTYKPRQHTT
VQDCNCSIYS GHITGHRMAW DMMMKWSPTT ALLMAQLLRI PQVVIDIIAG GHWGVLLAAA
YFASTANWAK VILVLFLFAG VDGRTHTVGG TVGQGLKSLT SFFNPGPQRQ LQFVNTNGSW
HINSTALNCN DSLQTGFIAG LMYAHKFNSS GCPERMSSCR PLAAFDQGWG TISYATISGP
SDDKPYCWHY PPRPCGVVPA RDVCGPVYCF TPSPVVVGTT DRRGCPTYNW GSNETDILLL
NNIRPPAGNW FGCTWMNSTG FVKNCGAPPC NLGPTGNNSL KCPTDCFRKH PDATYTRCGS
GPWLTPRCLV HYPYRLWHYP CTVNYTIFKV RMFIGGLEHR LEAACNWTYG ERCDLEDRDR
AELSPLLHTT TQWAILPCSF TPTPALSTGL IHLHQNIVDT QYLYGLSSSI VSWAVKWEYI
MLVFLLLADA RICTCLLILL LICQAEATCK NVIVLNAAAA AGNHGFFWGL LVVCLAWHVK
GRLVPGATYL CLGVWPLLLV RLLRPHRALA LDSSDGGTVG CLVLIVLTIF TLTPGYKKKV
VLVMWWLQYF IARVEAIIHV WVPPLQVKGG RDAVIMLTCL FHPALGFEIT KILFGILGPL
YLLQHSLTKV PYFLRARALL RLCLLAKHLV YGKYVQAALL HLGRLTGTYI YDHLAPMKDW
AASGLRELTV ATEPIVFSAM ETKVITWGAD TAACGNILAV LPVSARRGRE IFLGPADDIK
TSGWRLLAPI TAYAQQTRGV LGAIVLSLTG RDKNEAEGEV QFLSTATQTF LGICINGVMW
TLFHGAGSKT LAGPKGPVVQ MYTNVDKDLV GWPSPPGKGS LTRCTCGSAD LYLVTRHADV
IPARRRGDTR ASLLSPRPIS YLKGSSGGPI MCPSGHVVGV FRAAVCTRGV AKALEFVPVE
NLETTMRSPV FTDNSTPPAV PHEFQVGHLH APTGSGKSTK VPAAYAAQGY KVLVLNPSVA
ATFGFGAYMS RAYGVDPNIR TGVRTVTTGA GITYSTYGKF FADGGCSGGA YDVIICDECH
SQDATTILGI GTVLDQAETA GARLVVLATA IPPGSVTTPH PNIEEVALPS EGEIPFYGRA
IPLVLIKGGR HLIFCHSKKK CDELAKQLTS LGVNAVAYYR GLDVAVIPAT GDVVVCSTDA
LMTGFTGDFD SVIDCNSAVT QTVDFSLDPT FTIETTTVPQ DAVSRSQRRG RTGRGRHGIY
RYVSSGERPS GIFDSVVLCE CYDAGCAWYD LTPAETTVRL RAYLNTPGLP VCQEHLEFWE
GVFTGLTNID AHMLSQAKQG GENFPYLVAY QATVCVRAKA PPPSWDTMWK CMICLKPTLT
GPTPLLYRLG AVQNEITLTH PITKYIMACM SADLEVITST WVLVGGVVAA LAAYCLTVGS
VAIVGRIILS GRPAITPDRE VLYQQFDEME ECSASLPYVD EARAIAGQFK EKVLGLIGTA
GQKAETLKPA ATSMWSKAEQ FWAKHMWNFV SGIQYLAGLS TLPGNPAVAT LMSFTAAVTS
PLTTHQTLLF NILGGWVASQ IAPPTAATAF VVSGMAGAAV GNIGLGRVLI DILAGYGTGV
AGALVAFKIM CGERPTAEEL VNLLPSILCP GALVVGVICA AVLRRHIGPG EGAVQWMNRL
IAFASRGNHG SPTHYVPETD ASAKVTQLLS SLTVTSLLKR LHTWIGEDYS TPCDGTWLRA
IWDWVCTALT DFKAWLQAKL LPQLPGVPFF SCQKGYKGVW RGDGVNSTKC PCGATISGHV
KNGTMRIVGP KLCSNTWQGT FPINATTTGP SVPAPAPNYK FALWRVGAAD YAEVRRVGDY
HYITGVTQDN LKCPCQVPSP EFFTELDGVR IHRFAPPCNP LLREEVTFSV GLHSYVVGSQ
LPCEPEPDVT VLTSMLSDPA HITAETAKRR LNRGSPPSLA NSSASQLSAP SLKATCTIQG
HHPDADLIKA NLLWRQCMGG NITRVEAENK VEILDCFKPL KEEEDDREIS VSADCFKKGP
AFPPALPVWA RPGYDPPLLE TWKRPDYDPP QVWGCPIPPA GPPPVPLPRR KRKPMELSDS
TVSQVMADLA DARFKVDTPS IEGQDSALGT SSQHDSGPEE KRDDNSDAAS YSSMPPLEGE
PGDPDLSSGS WSTVSGEDNV VCCSMSYTWT GALITPCSAE EEKLPINPLS NTLLRHHNLV
YSTSSRSAGL RQKKVTFDRL QVLDDHYREV VDEMKRLASK VKARLLPLEE ACGLTPPHSA
RSKYGYGAKE VRSLDKKALK HIEGVWQDLL DDSDTPLPTT IMAKNEVFAV EPSKGGKKPA
RLIVYPDLGV RVCEKRALYD VAQKLPTALM GPSYGFQYSP AQRVDFLLKA WKSKKIPMAF
SYDTRCFDST ITEHDIMTEE SIYQSCDLQP EARVAIRSLT QRLYCGGPMY NSKGQQCGYR
RCRASGVFTT SMGNTMTCYI KALASCRAAK LRDCTLLVCG DDLVAICESQ GTHEDEASLR
AFTEAMTRYS APPGDPPVPA YDLELVTSCS SNVSVARDAS GNRIYYLTRD PQVPLAKAAW
ETAKHSPVNS WLGNIIMYAP TLWARIVLMT HFFSVLQSQE QLEKTLAFEM YGSVYSVTPL
DLPAIIQRLH GLSAFSLHSY SPSEINRVAS CLRKLGVPPL RAWRHRARAV RAKLIAQGGR
AAICGIYLFN WAVKTKRKLT PLADADRLDL SSWFTVGAGG GDIYHSMSRA RPRNLLLCLL
LLSVGVGIFL LPAR


Related products :

Catalog number Product name Quantity
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein The E.coli derived recombinant protein contains the Non-Structural C-Protein immunodominant regions, 1-51 amino acids. For research use only. 100
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
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 1 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.5 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.1 mg
EIAAB13002 Envelope polyprotein,ERV3,ERV3 envelope protein,ERV-3 envelope protein,ERV3-1,ERV3-1 envelope protein,ERV-R envelope protein,HERV-R envelope protein,HERV-R_7q21.2 provirus ancestral Env polyprotein,Ho
EIAAB13041 Endogenous retrovirus group W member 1,Envelope polyprotein gPr73,Enverin,Env-W,ERVW-1,ERVWE1,HERV-7q Envelope protein,HERV-W envelope protein,HERV-W_7q21.2 provirus ancestral Env polyprotein,Homo sap
MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
SCH-MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
25-030 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. This gene encodes a protein that contains a tetr 0.05 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.5 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.1 mg
orb81732 HIV-2 gp32 protein HIV-2 gp32 recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32. The protein is fused with -galactosidase (114 kDa) at N-terminus. For resear 100
EIAAB38762 Cape,Chromosome-associated protein E,FGF-inducible protein 16,Fin16,Mouse,Mus musculus,SMC protein 2,Smc2,SMC-2,Smc2l1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
228-10674-3 Recombinant Hepatitis C Virus Non-structural Protein 4b (NS4b) Antigen 1000
MD-05-0217 Goat Anti-Hepatitis C Virus Non-structural Protein 5 a + b (NS5a+b) Antigen 1 mL
27-617 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. 0.1 mg
DS-MB-01485 Mouse Anti-Hepatitis C Virus Non-structural Protein 4a (NS4a) Antigen 100
MD-05-0210 Mouse Anti-Hepatitis C Virus Non-structural Protein 4b (NS4b) Antigen (aa 1710-1730) 100
MD-14-0870 Mouse Anti-Hepatitis C Virus Non-structural Protein 4b (NS4b) Antigen (aa 1689-1735) 100
MD-14-0388P Recombinant Hepatitis C Virus Non-structural Protein 4 a + b (NS4a+b) Antigen (aa 1658-1863) 500
MD-14-0390P Recombinant Hepatitis C Virus Non-structural Protein 4 a + b ( NS4a+b ) Antigen (aa 1658-1863) 100
MD-14-0389P Recombinant Hepatitis C Virus Non-structural Protein 4 a + b ( NS4a+b ) Antigen (aa 1658-1863) 100
EIAAB39885 Chondroitin sulfate proteoglycan core protein,Cytolytic granule proteoglycan core protein,PG19 core protein,Pgsg,Prg,Prg1,Proteoglycan 10K core protein,Rat,Rattus norvegicus,Secretory granule proteogl


 

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