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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_HCVVN              Reviewed;        3013 AA.
O92530;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 140.
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 6d (isolate VN235) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=356422;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9714232;
Tokita H., Okamoto H., Iizuka H., Kishimoto J., Tsuda F., Miyakawa Y.,
Mayumi M.;
"The entire nucleotide sequences of three hepatitis C virus isolates
in genetic groups 7-9 and comparison with those in the other eight
genetic groups.";
J. Gen. Virol. 79:1847-1857(1998).
[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 acts 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";
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EMBL; D84263; BAA32665.1; -; Genomic_RNA.
ProteinModelPortal; O92530; -.
SMR; O92530; -.
TCDB; 1.A.53.1.6; the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.
euHCVdb; D84263; -.
OrthoDB; VOG0900004E; -.
Proteomes; UP000008103; 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:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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: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; IPR011492; DEAD_Flavivir.
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; PF07652; Flavi_DEAD; 1.
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;
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_0000045712.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000045713.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000045714.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000045715.
CHAIN 384 744 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000045716.
CHAIN 745 807 p7. {ECO:0000250}.
/FTId=PRO_0000045717.
CHAIN 808 1024 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000045718.
CHAIN 1025 1655 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000045719.
CHAIN 1656 1709 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000045720.
CHAIN 1710 1970 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000045721.
CHAIN 1971 2422 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000045722.
CHAIN 2423 3013 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000045723.
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 380 723 Lumenal. {ECO:0000255}.
TRANSMEM 724 744 Helical. {ECO:0000255}.
TOPO_DOM 745 755 Lumenal. {ECO:0000255}.
TRANSMEM 756 776 Helical. {ECO:0000255}.
TOPO_DOM 777 780 Cytoplasmic. {ECO:0000255}.
TRANSMEM 781 801 Helical. {ECO:0000255}.
TOPO_DOM 802 811 Lumenal. {ECO:0000255}.
TRANSMEM 812 832 Helical. {ECO:0000255}.
TOPO_DOM 833 879 Cytoplasmic. {ECO:0000255}.
TRANSMEM 880 900 Helical. {ECO:0000255}.
TOPO_DOM 901 926 Lumenal. {ECO:0000255}.
TRANSMEM 927 947 Helical. {ECO:0000255}.
TOPO_DOM 948 1655 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1656 1676 Helical. {ECO:0000255}.
TOPO_DOM 1677 1803 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1804 1824 Helical. {ECO:0000255}.
TOPO_DOM 1825 1826 Lumenal. {ECO:0000255}.
TRANSMEM 1827 1847 Helical. {ECO:0000255}.
TOPO_DOM 1848 1848 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1849 1869 Helical. {ECO:0000255}.
TOPO_DOM 1870 1879 Lumenal. {ECO:0000255}.
TRANSMEM 1880 1900 Helical. {ECO:0000255}.
TOPO_DOM 1901 1970 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1971 2000 {ECO:0000250}.
TOPO_DOM 2001 2992 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2993 3013 Helical. {ECO:0000250}.
DOMAIN 901 1024 Peptidase C18. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
DOMAIN 1025 1206 Peptidase S29. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
DOMAIN 1215 1367 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1374 1536 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2636 2754 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1228 1235 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 658 669 PKR/eIF2-alpha phosphorylation homology
domain (PePHD). {ECO:0000250}.
REGION 1677 1688 NS3-binding (by NS4A). {ECO:0000255}.
REGION 2118 2331 Transcriptional activation.
{ECO:0000255}.
REGION 2118 2206 FKBP8-binding. {ECO:0000255}.
REGION 2198 2248 Basal phosphorylation. {ECO:0000250}.
REGION 2208 2273 PKR-binding. {ECO:0000255}.
REGION 2247 2305 NS4B-binding. {ECO:0000255}.
REGION 2350 2422 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 1314 1317 DECH box. {ECO:0000250}.
MOTIF 2321 2324 SH3-binding. {ECO:0000255}.
MOTIF 2326 2334 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 794 801 Poly-Leu.
COMPBIAS 2275 2326 Pro-rich.
COMPBIAS 2994 3001 Poly-Leu.
ACT_SITE 950 950 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 970 970 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 991 991 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 1081 1081 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1105 1105 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1163 1163 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1121 1121 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1123 1123 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1169 1169 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1173 1173 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 2009 2009 Zinc. {ECO:0000250}.
METAL 2027 2027 Zinc. {ECO:0000250}.
METAL 2029 2029 Zinc. {ECO:0000250}.
METAL 2050 2050 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:0000255}.
SITE 744 745 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 807 808 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1024 1025 Cleavage; by protease NS2-3.
{ECO:0000255|PROSITE-ProRule:PRU01030}.
SITE 1655 1656 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1709 1710 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1970 1971 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 2422 2423 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 2192 2192 Phosphoserine; by host; in p56.
{ECO:0000250}.
MOD_RES 2195 2195 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2199 2199 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2202 2202 Phosphoserine; by host; in p58.
{ECO:0000250}.
LIPID 1970 1970 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 250 250 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 476 476 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 621 621 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 643 643 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 2112 2160 {ECO:0000250}.
SEQUENCE 3013 AA; 328200 MW; C9EE9C0231E86EAF CRC64;
MSTLPKPQKR NQRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR QTGRTWAQPG YPWPLYGNEG CGWMGWLLSP RGSRPHWGPN DPRRRSRNLG
KVIDTLTCGF ADLMGYIPVV GAPLGGVAAA LAHGVRAVED GINYATGNLP GCSFSIFLLA
LLSCLTTPAS AVHYANKSGI YHLTNDCPNS SIVYEAEDFI MHLPGCVPCI KSGNGSSCWL
PATLTIAVPN ASIPVRGFRR HVDLMVGAAA FCSAMYVGDL CGGIFLVGQL FSFNPRRHWV
VQDCNCSIYV GHITGHRMAW DMMMNWSPTA TLVLSYVMRI PQVIMDIFTG GHWGILAGIL
YYSMVANWAK VLCILFLFAG VDATTRTTGA QAARATLGFT GLFQTGAKQN IHLINTNGSW
HINRTALNCN DSLNTGFMAA LFYLHKFNST GCPERLSACK SITQFAQGWG PVTYANVSGS
SEDRPYCWHY APRPCGVVSA RSVCGPVYCF TPSPVVVGTT DRRGVPTYTW GENESDVFLL
ESLRPPAGAW YGCTWMNSTG YTKTCGAPPC HIGPPDQFCP TDCFRKHPEA TYRKCGSGPW
LTPRCLVDYP YRLWHYPCTV NYTIHKVRLF INGLEHRFDA ACNWTRGERC ELEDRDRIEM
SPLLFSTTEL AILPCSFTTM PALSTGLVHL HQNIVDIQYL YGLAPALVSW AVRWEYVVLA
FLLLADARIC ACLWMVLLIS QVEAALENLI VLNAASAASS QGWIYCLVFI CCAWYIKGRV
VPGATYAILH LWPLLLLVLA LPQRAYAQDR EQGASIGVVV IAAITIFTLT PAYKTMLVHF
LWWNQYFIAR SEALIQQWVP SLRVRGGRDA VILLTCLLHP SLGFDITKML LALLGPLYLL
QVSLLRVPYY VRAHALLRVC ILVRRVAGGK YIQAALLKLG AWTGTYIYDH LAPLSTWASD
GLRDLAVAVE PVTFSPMEKK IITWGADTAA CGDILAGLPV SARLGHLLFL GPADDMKSMG
WRLLAPITAY CQQTRGLLGT IVTSLTGRDR NVVEGEIQVL STATQSFLGT AINGVMWTVY
HGAGSKTLAG PKGPVCQMYT NVDQDMVGWP APPGTRSLTP CTCGASDLYL VTRNADVIPA
RRRGDTRAGL LSPRPLSTLK GSSGGPLMCP SDHVVGLFRA AVCTRGVAKA LDFVPVENME
TTMRSPVFTD NSTPPAVPQT YQVGYLHAPT GSGKSTKVPA AYASQGYKVL VLNPSVAATL
GFGSYMSTAH GIDPNIRTGV RTITTGGPIT YSTYGKFLAD GGCSGGAYDI IICDECHSTD
PTTVLGIGTV LDQAETAGVR LTVLATATPP GSVTVPHPNI TETALPSTGE VPFYGKAIPL
ECIKGGRHLI FCHSKKKCDE LAKQLRTLGL NAVAFYRGVD VSVIPTAGDV VVCATDALMT
GYTGDFDSVI DCNVAVTQIV DFSLDPTFSI ETTTVPQDAV ARSQRRGRTG RGKPGVYRYV
SQGERPSGMF DTVVLCEAYD VGCAWYELTP SETTVRLRAY LNTPGLPVCQ DHLEFWEGVF
TGMTHIDAHF LSQTKQGGEN FAYLVAYQAT VCARAKAPPP SWDTMWKCLI RLKPMLTGPT
PLLYRLGAVQ NEIITTHPIT KYIMTCMAAD LEVITSTWVL AGGIVAALAA YCLTVGSVVI
CGRIVTSGKP VPLPDREVLY RQFDEMEECS RHIPYLAEGQ QIAEQFKQKI LGLLQNTAKQ
AEDLKPAVQS AWPKLEQFWQ KHLWNFVSGV QYLAGLSTLP GNPAVASLMS FSAALTSPLS
TSTTLLLNIL GGWVASQLAP PTASTAFVVS GLAGAAVGSI GLGKVIIDIL AGYGAGVSGA
LVAFKIMSGE APAVEDMVNL LPALLSPGAL VVGVVCAAVL RRHVGPSEGA TQWMNRLIAF
ASRGNHVSPT HYVPETDASR AVTTILSSLT ITSLLRRLHE WISGDWSAPC SCSWLKDVWD
WVCTVLSDFK TWLRAKLVPT LPGIPFISCQ RGFRGVWRGD GVNYTTCSCG ANITGHVKNG
SMKIVGPKMC SNVWNNRFPI NAITTGPSVP VPEPNYHKAL WRVSAEDYVE VVRVNDHHYI
VGATADNLKC PCQVPAPEFF TEVDGVRLHR FAPPCRPLMR DDITFSVGLS TYVVGSQLPC
EPEPDVVILT SMLTDPDHIT AETAARRLAR GSPPSLASSS ASQLSAPSLK ATCTTAGKHP
DAELIEANLL WRQEVGGNIT RVESENKIIV LDSFDPLIAE TDDREISVGA ECFNPPRPKF
PPALPVWARP DYNPPLLQPW KAPDYEPPLV HGCALPPKGL PPVPPPRKKR VVQLDEGSAK
RALAELAQTS FPPSTATLSE DSGRETSTLS SDMTPPREEA DRASDDGSYS SMPPLEGEPG
DPDLSSGSWS TVSEDHDSVV CCSMSYSWTG ALITPCAAEE EKLPISPLSN ALIRHHNLVY
STTSRSASLR QKKVTFDRVQ VVDQHYYDVL KEIKTKASGV SAKLLSVEEA CALTPPHSAR
SKFGYGAKEV RGLASKAVNH INSVWEDLLE DNSTPIPTTI MAKNEVFCVD AQKGGRKPAR
LIVYPDLGVR VCEKRALYDV TQKLPIAVMG AAYGFQYSPK QRVDYLLKMW RSKKTPMGFS
YDTRCFDSTV TERDIRTEED IYQCCQLDPV AKKAITSLTE RLYCGGPMYN SRGQSCGYRR
CRASGVLTTS LGNTLTCYLK AQAACRAAKL KDFDMLVCGD DLVVISESMG VAEDASALRA
FTEAMTRYSA PPGDDPQPEY DLELITSCSS NVSVAHDGAG QRYYYLTRDP LTPLSRAAWE
TARHTPVNSW LGNIIMYAPT IWVRMVLMTH FFAILQSQEI LHKALDFDMY GVTYSVTPLD
LPYIIQRLHG MAAFSLHGYS PGELNRVASC LRKLGAPPLR AWRHRARAVR AKLIAQGGKH
AICGKYLFNW AVRTKLKLTP LRGAANLDLS GWFVSGGSGG DIFHSVSRAR PRNLLLCLLL
LTVGVGIFLL PAR


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