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Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

 POLG_HCVJ4              Reviewed;        3010 AA.
O92972; O92969; O92970; O92971; Q02828;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
02-DEC-2020, entry version 163.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Core protein precursor;
AltName: Full=Capsid protein C;
AltName: Full=p23;
Contains:
RecName: Full=Mature core protein;
AltName: Full=p21;
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=Viroporin p7;
Contains:
RecName: Full=Protease NS2;
Short=p23;
EC=3.4.22.- {ECO:0000269|PubMed:17239391};
AltName: Full=Non-structural protein 2;
Short=NS2;
Contains:
RecName: Full=Serine protease/helicase NS3;
EC=3.4.21.98 {ECO:0000269|PubMed:17239391};
EC=3.6.1.15 {ECO:0000250|UniProtKB:P27958};
EC=3.6.4.13 {ECO:0000250|UniProtKB:P27958};
AltName: Full=Hepacivirin;
AltName: Full=NS3 helicase {ECO:0000250|UniProtKB:P27958};
AltName: Full=NS3 protease {ECO:0000250|UniProtKB:P27958};
AltName: Full=NS3P;
AltName: Full=Viroporin 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=p56/58;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48 {ECO:0000250|UniProtKB:P27958};
AltName: Full=NS5B;
AltName: Full=p68;
Hepatitis C virus genotype 1b (strain HC-J4) (HCV).
Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
Amarillovirales; Flaviviridae; Hepacivirus.
NCBI_TaxID=420174;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HC-J4/91;
PubMed=1325713; DOI=10.1016/0042-6822(92)90933-g;
Okamoto H., Kojima M., Okada S., Yoshizawa H., Iizuka H., Tanaka T.,
Muchmore E.E., Peterson D.A., Ito Y., Mishiro S.;
"Genetic drift of hepatitis C virus during an 8.2-year infection in a
chimpanzee: variability and stability.";
Virology 190:894-899(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HC-J4, Isolate pCV-J4L2S, Isolate pCV-J4L4S, and Isolate pCV-J4L6S;
PubMed=9581788; DOI=10.1006/viro.1998.9092;
Yanagi M., St Claire M., Shapiro M., Emerson S.U., Purcell R.H., Bukh J.;
"Transcripts of a chimeric cDNA clone of hepatitis C virus genotype 1b are
infectious in vivo.";
Virology 244:161-172(1998).
[3]
ACTIVITY REGULATION (VIROPORIN P7), FUNCTION (VIROPORIN P7), AND SUBUNIT
(VIROPORIN P7).
PubMed=12560074; DOI=10.1016/s0014-5793(02)03851-6;
Griffin S.D., Beales L.P., Clarke D.S., Worsfold O., Evans S.D., Jaeger J.,
Harris M.P., Rowlands D.J.;
"The p7 protein of hepatitis C virus forms an ion channel that is blocked
by the antiviral drug, Amantadine.";
FEBS Lett. 535:34-38(2003).
[4]
SUBUNIT (VIROPORIN P7).
PubMed=17032656; DOI=10.1074/jbc.m602434200;
Clarke D., Griffin S., Beales L., Gelais C.S., Burgess S., Harris M.,
Rowlands D.;
"Evidence for the formation of a heptameric ion channel complex by the
hepatitis C virus p7 protein in vitro.";
J. Biol. Chem. 281:37057-37068(2006).
[5]
CHARACTERIZATION (RNA-DIRECTED RNA POLYMERASE), AND SUBUNIT.
STRAIN=Isolate pCV-J4L6S;
PubMed=16533043; DOI=10.1021/bi051483s;
Cramer J., Jaeger J., Restle T.;
"Biochemical and pre-steady-state kinetic characterization of the hepatitis
C virus RNA polymerase (NS5BDelta21, HC-J4).";
Biochemistry 45:3610-3619(2006).
[6]
CATALYTIC ACTIVITY (PROTEASE NS2), CATALYTIC ACTIVITY (SERINE
PROTEASE/HELICASE NS3), ZINC-BINDING (SERINE PROTEASE/HELICASE NS3),
MUTAGENESIS OF CYS-922; CYS-1123; CYS-1125; SER-1165; CYS-1171; HIS-1175
AND CYS-1185, ACTIVE SITE (SERINE PROTEASE/HELICASE NS3), COFACTOR
(PROTEASE NS2), COFACTOR (SERINE PROTEASE/HELICASE NS3), DOMAIN (PROTEASE
NS2), AND DOMAIN (SERINE PROTEASE/HELICASE NS3).
STRAIN=Isolate pCV-J4L6S;
PubMed=17239391; DOI=10.1016/j.jmb.2006.12.062;
Tedbury P.R., Harris M.;
"Characterisation of the role of zinc in the hepatitis C virus NS2/3 auto-
cleavage and NS3 protease activities.";
J. Mol. Biol. 366:1652-1660(2007).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2420-2989.
PubMed=12589751; DOI=10.1016/s0022-2836(02)01439-0;
O'Farrell D., Trowbridge R., Rowlands D., Jager J.;
"Substrate complexes of hepatitis C virus RNA polymerase (HC-J4):
structural evidence for nucleotide import and de-novo initiation.";
J. Mol. Biol. 326:1025-1035(2003).
-!- FUNCTION: [Mature core protein]: Packages viral RNA to form a viral
nucleocapsid, and promotes virion budding (Probable). Participates in
the viral particle production as a result of its interaction with the
non-structural protein 5A (By similarity). Binds RNA and may function
as a RNA chaperone to induce the RNA structural rearrangements taking
place during virus replication (By similarity). Modulates viral
translation initiation by interacting with viral IRES and 40S ribosomal
subunit (By similarity). Affects various cell signaling pathways, host
immunity and lipid metabolism (Probable). Prevents the establishment of
cellular antiviral state by blocking the interferon-alpha/beta (IFN-
alpha/beta) and IFN-gamma signaling pathways and by blocking the
formation of phosphorylated STAT1 and promoting ubiquitin-mediated
proteasome-dependent degradation of STAT1 (By similarity). Activates
STAT3 leading to cellular transformation (By similarity). Regulates the
activity of cellular genes, including c-myc and c-fos (By similarity).
May repress the promoter of p53, and sequester CREB3 and SP110 isoform
3/Sp110b in the cytoplasm (By similarity). Represses cell cycle
negative regulating factor CDKN1A, thereby interrupting an important
check point of normal cell cycle regulation (By similarity). Targets
transcription factors involved in the regulation of inflammatory
responses and in the immune response: suppresses TNF-induced NF-kappa-B
activation, and activates AP-1 (By similarity). Binds to dendritic
cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes
proliferation (By similarity). Alters lipid metabolism by interacting
with hepatocellular proteins involved in lipid accumulation and storage
(By similarity). Induces up-regulation of FAS promoter activity, and
thereby contributes to the increased triglyceride accumulation in
hepatocytes (steatosis) (By similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:P29846, ECO:0000250|UniProtKB:Q99IB8,
ECO:0000305}.
-!- FUNCTION: [Envelope glycoprotein E1]: Forms a heterodimer with envelope
glycoprotein E2, which mediates virus attachment to the host cell,
virion internalization through clathrin-dependent endocytosis and
fusion with host membrane (By similarity). Fusion with the host cell is
most likely mediated by both E1 and E2, through conformational
rearrangements of the heterodimer required for fusion rather than a
classical class II fusion mechanism (By similarity). E1/E2 heterodimer
binds host apolipoproteins such as APOB and APOE thereby forming a
lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP
allows the initial virus attachment to cell surface receptors such as
the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-
1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger
receptor class B type I (SCARB1) (By similarity). The cholesterol
transfer activity of SCARB1 allows E2 exposure and binding of E2 to
SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer
binding on CD81 activates the epithelial growth factor receptor (EGFR)
signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-
SCARB1-CD81 to the cell lateral membrane allows further interaction
with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry
(By similarity). {ECO:0000250|UniProtKB:P27958}.
-!- FUNCTION: [Envelope glycoprotein E2]: Forms a heterodimer with envelope
glycoprotein E1, which mediates virus attachment to the host cell,
virion internalization through clathrin-dependent endocytosis and
fusion with host membrane (By similarity). Fusion with the host cell is
most likely mediated by both E1 and E2, through conformational
rearrangements of the heterodimer required for fusion rather than a
classical class II fusion mechanism (By similarity). The interaction
between envelope glycoprotein E2 and host apolipoprotein E/APOE allows
the proper assembly, maturation and infectivity of the viral particles
(By similarity). This interaction is probably promoted via the up-
regulation of cellular autophagy by the virus (By similarity). E1/E2
heterodimer binds host apolipoproteins such as APOB and APOE thereby
forming a lipo-viro-particle (LVP) (By similarity). APOE associated to
the LVP allows the initial virus attachment to cell surface receptors
such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1),
syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and
scavenger receptor class B type I (SCARB1) (By similarity). The
cholesterol transfer activity of SCARB1 allows E2 exposure and binding
of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2
heterodimer binding on CD81 activates the epithelial growth factor
receptor (EGFR) signaling pathway (By similarity). Diffusion of the
complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows
further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to
finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR
activation, preventing the establishment of an antiviral state (By
similarity). 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 (By similarity). These interactions allow the capture of
circulating HCV particles by these cells and subsequent transmission to
permissive cells (By similarity). 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|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958}.
-!- FUNCTION: [Viroporin p7]: Ion channel protein that acts as a viroporin
and plays an essential role in the assembly, envelopment and secretion
of viral particles (Probable). Regulates the host cell secretory
pathway, which induces the intracellular retention of viral
glycoproteins and favors assembly of viral particles (By similarity).
Creates a pore in acidic organelles and releases Ca(2+) and H(+) in the
cytoplasm of infected cells, leading to a productive viral infection
(Probable). High levels of cytoplasmic Ca(2+) may trigger membrane
trafficking and transport of viral ER-associated proteins to
viroplasms, sites of viral genome replication (Probable). This ionic
imbalance induces the assembly of the inflammasome complex, which
triggers the maturation of pro-IL-1beta into IL-1beta through the
action of caspase-1 (By similarity). Targets also host mitochondria and
induces mitochondrial depolarization (By similarity). In addition of
its role as a viroporin, acts as a lipid raft adhesion factor (By
similarity). {ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8, ECO:0000305,
ECO:0000305|PubMed:12560074}.
-!- FUNCTION: [Protease NS2]: Cysteine protease required for the
proteolytic auto-cleavage between the non-structural proteins NS2 and
NS3 (PubMed:17239391). The N-terminus of NS3 is required for the
function of NS2 protease (active region NS2-3) (PubMed:17239391).
Promotes the initiation of viral particle assembly by mediating the
interaction between structural and non-structural proteins (By
similarity). {ECO:0000250|UniProtKB:P27958,
ECO:0000269|PubMed:17239391}.
-!- FUNCTION: [Serine protease/helicase NS3]: Displays three enzymatic
activities: serine protease with a chymotrypsin-like fold, NTPase and
RNA helicase (By similarity). NS3 serine protease, in association with
NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-
NS5A and NS5A-NS5B (By similarity). The NS3/NS4A complex prevents
phosphorylation of host IRF3, thus preventing the establishment of
dsRNA induced antiviral state (By similarity). NS3 RNA helicase binds
to RNA and unwinds both dsDNA and dsRNA in the 3' to 5' direction, and
likely resolves RNA complicated stable secondary structures in the
template strand (By similarity). Binds a single ATP and catalyzes the
unzipping of a single base pair of dsRNA (By similarity). Inhibits host
antiviral proteins TBK1 and IRF3 thereby preventing the establishment
of an antiviral state (By similarity). Cleaves host MAVS/CARDIF thereby
preventing the establishment of an antiviral state (By similarity).
Cleaves host TICAM1/TRIF, thereby disrupting TLR3 signaling and
preventing the establishment of an antiviral state (By similarity).
{ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q9WMX2}.
-!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
alteration that serves as a scaffold for the virus replication complex
(By similarity). This membrane alteration gives rise to the so-called
ER-derived membranous web that contains the replication complex (By
similarity). NS4B self-interaction contributes to its function in
membranous web formation (By similarity). Promotes host TRIF protein
degradation in a CASP8-dependent manner thereby inhibiting host TLR3-
mediated interferon signaling (By similarity). Disrupts the interaction
between STING and TBK1 contributing to the inhibition of interferon
signaling (By similarity). {ECO:0000250|UniProtKB:P27958}.
-!- FUNCTION: [Non-structural protein 5A]: Phosphorylated protein that is
indispensable for viral replication and assembly (By similarity). Both
hypo- and hyperphosphorylated states are required for the viral life
cycle (By similarity). The hyperphosphorylated form of NS5A is an
inhibitor of viral replication (By similarity). Involved in RNA-binding
and especially in binding to the viral genome (By similarity). Zinc is
essential for RNA-binding (By similarity). Participates in the viral
particle production as a result of its interaction with the mature
viral core protein (By similarity). Its interaction with host VAPB may
target the viral replication complex to vesicles (By similarity). Down-
regulates viral IRES translation initiation (By similarity). Mediates
interferon resistance, presumably by interacting with and inhibiting
host EIF2AK2/PKR (By similarity). Prevents BIN1-induced apoptosis (By
similarity). Acts as a transcriptional activator of some host genes
important for viral replication when localized in the nucleus (By
similarity). Via the interaction with host PACSIN2, modulates lipid
droplet formation in order to promote virion assembly (By similarity).
Modulates TNFRSF21/DR6 signaling pathway for viral propagation (By
similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8, ECO:0000250|UniProtKB:Q9WMX2}.
-!- FUNCTION: [RNA-directed RNA polymerase]: RNA-dependent RNA polymerase
that performs primer-template recognition and RNA synthesis during
viral replication. {ECO:0000250|UniProtKB:P27958}.
-!- CATALYTIC ACTIVITY: [Serine protease/helicase NS3]:
Reaction=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'.; EC=3.4.21.98;
Evidence={ECO:0000250|UniProtKB:P27958};
-!- CATALYTIC ACTIVITY: [Serine protease/helicase NS3]:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000250|UniProtKB:P27958};
-!- CATALYTIC ACTIVITY: [Serine protease/helicase NS3]:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
Evidence={ECO:0000250|UniProtKB:P27958};
-!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- COFACTOR: [Protease NS2]:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17239391};
Note=Activity of protease NS2 is dependent on zinc ions and completely
inhibited by EDTA. This is probably due to the fact that NS2 protease
activity needs NS3 N-terminus that binds a zinc atom (active region
NS2-3). {ECO:0000269|PubMed:17239391};
-!- COFACTOR: [Serine protease/helicase NS3]:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:17239391};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9WMX2};
Note=Binds 1 zinc ion, which has a structural role (PubMed:17239391).
The magnesium ion is essential for the helicase activity (By
similarity). {ECO:0000250|UniProtKB:Q9WMX2,
ECO:0000269|PubMed:17239391};
-!- COFACTOR: [RNA-directed RNA polymerase]:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P26663};
Note=Binds 2 magnesium ion that constitute a dinuclear catalytic metal
center. {ECO:0000250|UniProtKB:P26663};
-!- ACTIVITY REGULATION: Inhibited by the antiviral drug hexamethylene
amiloride (By similarity). Inhibited by amantadine (PubMed:12560074).
Inhibition by amantadine appears to be genotype-dependent (By
similarity). Also inhibited by long-alkyl-chain iminosugar derivatives
(By similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P27958, ECO:0000269|PubMed:12560074}.
-!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Activity is up-
regulated by PRK2/PKN2-mediated phosphorylation.
{ECO:0000250|UniProtKB:P27958}.
-!- SUBUNIT: [Mature core protein]: Homooligomer (By similarity). Interacts
with E1 (via C-terminus) (By similarity). Interacts with the non-
structural protein 5A (By similarity). Interacts (via N-terminus) with
host STAT1 (via SH2 domain); this interaction results in decreased
STAT1 phosphorylation and ubiquitin-mediated proteasome-dependent STAT1
degradation, leading to decreased IFN-stimulated gene transcription (By
similarity). Interacts with host STAT3; this interaction constitutively
activates STAT3 (By similarity). Interacts with host LTBR receptor (By
similarity). Interacts with host TNFRSF1A receptor and possibly induces
apoptosis (By similarity). Interacts with host HNRPK (By similarity).
Interacts with host YWHAE (By similarity). Interacts with host
UBE3A/E6AP (By similarity). Interacts with host DDX3X (By similarity).
Interacts with host APOA2 (By similarity). Interacts with host RXRA
protein (By similarity). Interacts with host SP110 isoform 3/Sp110b;
this interaction sequesters the transcriptional corepressor SP110 away
from the nucleus (By similarity). Interacts with host CREB3 nuclear
transcription protein; this interaction triggers cell transformation
(By similarity). Interacts with host ACY3 (By similarity). Interacts
with host C1QR1 (By similarity). Interacts with host RBM24; this
interaction, which enhances the interaction of the mature core protein
with 5'-UTR, may inhibit viral translation and favor replication (By
similarity). Interacts with host EIF2AK2/PKR; this interaction induces
the autophosphorylation of EIF2AK2 (By similarity). Part of the viral
assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A
and the mature core protein (By similarity).
{ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26664,
ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:P29846,
ECO:0000250|UniProtKB:Q03463, ECO:0000250|UniProtKB:Q5EG65,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Envelope glycoprotein E1]: Forms a heterodimer with envelope
glycoprotein E2 (By similarity). Interacts with mature core protein (By
similarity). Interacts with protease NS2 (By similarity). The
heterodimer E1/E2 interacts with host CLDN1; this interaction plays a
role in viral entry into host cell (By similarity). Interacts with host
SPSB2 (via C-terminus) (By similarity). Part of the viral assembly
initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
mature core protein (By similarity). {ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Envelope glycoprotein E2]: Forms a heterodimer with envelope
glycoprotein E1 (By similarity). Interacts with host CD81 and SCARB1
receptors; these interactions play a role in viral entry into host cell
(By similarity). Interacts with host EIF2AK2/PKR; this interaction
inhibits EIF2AK2 and probably allows the virus to evade the innate
immune response (By similarity). Interacts with host CD209/DC-SIGN and
CLEC4M/DC-SIGNR (By similarity). Interact with host SPCS1; this
interaction is essential for viral particle assembly (By similarity).
Interacts with protease NS2 (By similarity). The heterodimer E1/E2
interacts with host CLDN1; this interaction plays a role in viral entry
into host cell (By similarity). Part of the viral assembly initiation
complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core
protein (By similarity). {ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Viroporin p7]: Homohexamer (PubMed:12560074). Homoheptamer
(PubMed:17032656). Interacts with protease NS2 (By similarity).
{ECO:0000250|UniProtKB:Q99IB8, ECO:0000269|PubMed:12560074,
ECO:0000269|PubMed:17032656}.
-!- SUBUNIT: [Protease NS2]: Homodimer (By similarity). Interacts with host
SPCS1; this interaction is essential for viral particle assembly (By
similarity). Interacts with envelope glycoprotein E1 (By similarity).
Interacts with envelope glycoprotein E2 (By similarity). Interacts with
viroporin p7 (By similarity). Interacts with serine protease/helicase
NS3 (By similarity). Part of the replication complex composed of NS2,
NS3, NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in
an ER-derived membranous web (By similarity). Part of the viral
assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A
and the mature core protein (By similarity).
{ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Serine protease/helicase NS3]: Interacts with protease NS2
(By similarity). Interacts with non-structural protein 4A; this
interaction stabilizes the folding of NS3 serine protease (By
similarity). NS3-NS4A interaction is essential for NS3 activation and
allows membrane anchorage of the latter (By similarity). NS3/NS4A
complex also prevents phosphorylation of host IRF3, thus preventing the
establishment of dsRNA induced antiviral state (By similarity).
Interacts with host MAVS; this interaction leads to the cleavage and
inhibition of host MAVS (By similarity). Interacts with host TICAM1;
this interaction leads to the cleavage and inhibition of host TICAM1
(By similarity). Interacts with host TANK-binding kinase/TBK1; this
interaction results in the inhibition of the association between TBK1
and IRF3, which leads to the inhibition of IRF3 activation (By
similarity). Interacts with host RBM24 (By similarity). Part of the
replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-
directed RNA polymerase embedded in an ER-derived membranous web (By
similarity). Part of the viral assembly initiation complex composed of
NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By
similarity). {ECO:0000250|UniProtKB:P26663,
ECO:0000250|UniProtKB:P27958, ECO:0000250|UniProtKB:Q99IB8,
ECO:0000250|UniProtKB:Q9WMX2}.
-!- SUBUNIT: [Non-structural protein 4A]: Interacts with NS3 serine
protease; this interaction stabilizes the folding of NS3 serine
protease (By similarity). NS3-NS4A interaction is essential for NS3
activation and allows membrane anchorage of the latter (By similarity).
Interacts with non-structural protein 5A (via N-terminus) (By
similarity). Part of the replication complex composed of NS2, NS3,
NS4A, NS4B, NS5A and the RNA-directed RNA polymerase embedded in an ER-
derived membranous web (By similarity). Part of the viral assembly
initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
mature core protein (By similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Non-structural protein 4B]: Homomultimer (By similarity).
Interacts with non-structural protein NS5A (By similarity). Interacts
with host PLA2G4C; this interaction likely initiates the recruitment of
replication complexes to lipid droplets (By similarity). Interacts with
host STING; this interaction disrupts the interaction between STING and
TBK1 thereby suppressing the interferon signaling (By similarity). Part
of the replication complex composed of NS2, NS3, NS4A, NS4B, NS5A and
the RNA-directed RNA polymerase embedded in an ER-derived membranous
web (By similarity). {ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [Non-structural protein 5A]: Monomer (By similarity).
Homodimer; dimerization is required for RNA-binding (By similarity).
Interacts with mature core protein (By similarity). Interacts (via N-
terminus) with non-structural protein 4A (By similarity). Interacts
with non-structural protein 4B (By similarity). Interacts with RNA-
directed RNA polymerase (By similarity). Part of the viral assembly
initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the
mature core protein (By similarity). Part of the replication complex
composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA
polymerase (By similarity). Interacts with host GRB2 (By similarity).
Interacts with host BIN1 (By similarity). Interacts with host PIK3R1
(By similarity). Interacts with host SRCAP (By similarity). Interacts
with host FKBP8 (By similarity). Interacts with host VAPB (By
similarity). Interacts with host EIF2AK2/PKR; this interaction leads to
disruption of EIF2AK2 dimerization by NS5A and probably allows the
virus to evade the innate immune response (By similarity). Interacts
(via N-terminus) with host PACSIN2 (via N-terminus); this interaction
attenuates protein kinase C alpha-mediated phosphorylation of PACSIN2
by disrupting the interaction between PACSIN2 and PRKCA (By
similarity). Interacts (via N-terminus) with host SRC kinase (via SH2
domain) (By similarity). Interacts with most Src-family kinases (By
similarity). Interacts with host IFI27 and SKP2; promotes the
ubiquitin-mediated proteasomal degradation of NS5A (By similarity).
Interacts with host GPS2 (By similarity). Interacts with host TNFRSF21;
this interaction allows the modulation by the virus of JNK, p38 MAPK,
STAT3, and Akt signaling pathways in a DR6-dependent manner (By
similarity). Interacts (via N-terminus) with host CIDEB (via N-
terminus); this interaction seems to regulate the association of HCV
particles with APOE (By similarity). Interacts with host CHKA/Choline
Kinase-alpha; CHKA bridges host PI4KA and NS5A and potentiates NS5A-
stimulated PI4KA activity, which then facilitates the targeting of the
ternary complex to the ER for viral replication (By similarity).
Interacts with host SPSB2 (via C-terminus); this interaction targets
NS5A for ubiquitination and degradation (By similarity). Interacts with
host RAB18; this interaction may promote the association of NS5A and
other replicase components with lipid droplets (By similarity).
{ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P26663,
ECO:0000250|UniProtKB:P26664, ECO:0000250|UniProtKB:P27958,
ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBUNIT: [RNA-directed RNA polymerase]: Homooligomer (By similarity).
Interacts with non-structural protein 5A (By similarity). Interacts
with host VAPB (By similarity). Interacts with host PRK2/PKN2 (By
similarity). Interacts with host HNRNPA1 and SEPT6; these interactions
facilitate viral replication (By similarity). Part of the replication
complex composed of NS2, NS3, NS4A, NS4B, NS5A and the RNA-directed RNA
polymerase (By similarity). {ECO:0000250|UniProtKB:P27958}.
-!- INTERACTION:
O92972; P06241: FYN; Xeno; NbExp=2; IntAct=EBI-710506, EBI-515315;
O92972; P62993: GRB2; Xeno; NbExp=2; IntAct=EBI-710506, EBI-401755;
O92972; P08631: HCK; Xeno; NbExp=2; IntAct=EBI-710506, EBI-346340;
O92972; P06240: Lck; Xeno; NbExp=2; IntAct=EBI-710506, EBI-1401;
O92972; P07948: LYN; Xeno; NbExp=2; IntAct=EBI-710506, EBI-79452;
PRO_0000278742; P84022: SMAD3; Xeno; NbExp=6; IntAct=EBI-9213553, EBI-347161;
PRO_0000278742; P62258: YWHAE; Xeno; NbExp=5; IntAct=EBI-9213553, EBI-356498;
PRO_0000278746; P19525: EIF2AK2; Xeno; NbExp=2; IntAct=EBI-6918883, EBI-640775;
PRO_0000278747; PRO_0000278748 [O92972]: -; NbExp=2; IntAct=EBI-8852105, EBI-8852113;
PRO_0000278753; Q16513: PKN2; Xeno; NbExp=7; IntAct=EBI-10006231, EBI-2511350;
-!- SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P26664}; Single-pass membrane
protein {ECO:0000255}. Host mitochondrion membrane
{ECO:0000250|UniProtKB:P26664}; Single-pass type I membrane protein
{ECO:0000255}. Note=The C-terminal transmembrane domain of the core
protein precursor contains an ER signal leading the nascent polyprotein
to the ER membrane.
-!- SUBCELLULAR LOCATION: [Mature core protein]: Virion
{ECO:0000250|UniProtKB:Q99IB8}. Host cytoplasm
{ECO:0000250|UniProtKB:Q99IB8}. Host nucleus
{ECO:0000250|UniProtKB:P26662}. Host lipid droplet
{ECO:0000250|UniProtKB:Q99IB8}. Note=Only a minor proportion of core
protein is present in the nucleus (By similarity). Probably present on
the surface of lipid droplets (By similarity).
{ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
endoplasmic reticulum membrane; Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P27958}. Note=The C-terminal transmembrane
domain acts as a signal sequence and forms a hairpin structure before
cleavage by host signal peptidase (By similarity). After cleavage, the
membrane sequence is retained at the C-terminus of the protein, serving
as ER membrane anchor (By similarity). A reorientation of the second
hydrophobic stretch occurs after cleavage producing a single reoriented
transmembrane domain (By similarity). These events explain the final
topology of the protein (By similarity).
{ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
endoplasmic reticulum membrane; Single-pass type I membrane protein
{ECO:0000250|UniProtKB:P27958}. Host lipid droplet
{ECO:0000250|UniProtKB:Q9WMX2}. Note=The C-terminal transmembrane
domain acts as a signal sequence and forms a hairpin structure before
cleavage by host signal peptidase (By similarity). After cleavage, the
membrane sequence is retained at the C-terminus of the protein, serving
as ER membrane anchor (By similarity). A reorientation of the second
hydrophobic stretch occurs after cleavage producing a single reoriented
transmembrane domain (By similarity). These events explain the final
topology of the protein (By similarity).
{ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [Viroporin p7]: Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P27958}. Host mitochondrion
{ECO:0000250|UniProtKB:P27958}. Host cell membrane
{ECO:0000250|UniProtKB:P27958}. Note=The C-terminus of p7 membrane
domain acts as a signal sequence (By similarity). After cleavage by
host signal peptidase, the membrane sequence is retained at the C-
terminus of the protein, serving as ER membrane anchor (By similarity).
ER retention of p7 is leaky and a small fraction reaches the plasma
membrane (By similarity). {ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [Protease NS2]: Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P27958}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P27958}. Host lipid droplet
{ECO:0000250|UniProtKB:Q9WMX2}. Note=Probably present on the surface of
lipid droplets. {ECO:0000250|UniProtKB:Q99IB8}.
-!- SUBCELLULAR LOCATION: [Serine protease/helicase NS3]: Host endoplasmic
reticulum membrane {ECO:0000305}; Peripheral membrane protein
{ECO:0000305}. Note=NS3 is associated to the ER membrane through its
binding to NS4A. {ECO:0000305}.
-!- 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|UniProtKB:P27958}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:P27958}. Note=A reorientation of the N-
terminus into the ER lumen occurs post-translationally.
{ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P27958}; Peripheral membrane
protein {ECO:0000250|UniProtKB:P27958}. Host cytoplasm, host
perinuclear region {ECO:0000250|UniProtKB:P27958}. Host mitochondrion
{ECO:0000250|UniProtKB:P26662}. Host cytoplasm
{ECO:0000250|UniProtKB:P27958}. Host nucleus
{ECO:0000250|UniProtKB:P26662}. Host lipid droplet
{ECO:0000250|UniProtKB:Q9WMX2}. Note=Host membrane insertion occurs
after processing by the NS3 protease (By similarity). Localizes at the
surface of lipid droplets (By similarity).
{ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958}.
-!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm
{ECO:0000250|UniProtKB:P27958}. Host endoplasmic reticulum membrane;
Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P27958}.
Note=Host membrane insertion occurs after processing by the NS3
protease. {ECO:0000250|UniProtKB:P27958}.
-!- DOMAIN: [Envelope glycoprotein E1]: The transmembrane regions of
envelope E1 and E2 glycoproteins are involved in heterodimer formation,
ER localization, and assembly of these proteins.
{ECO:0000250|UniProtKB:P27958}.
-!- DOMAIN: [Envelope glycoprotein E2]: The transmembrane regions of
envelope E1 and E2 glycoproteins are involved in heterodimer formation,
ER localization, and assembly of these proteins (By similarity).
Envelope E2 glycoprotein contain two highly variable regions called
hypervariable region 1 and 2 (HVR1 and HVR2) (By similarity). E2 also
contain two segments involved in CD81-binding (By similarity). HVR1 is
implicated in the SCARB1-mediated cell entry and probably acts as a
regulator of the association of particles with lipids (By similarity).
{ECO:0000250|UniProtKB:P26663, ECO:0000250|UniProtKB:P27958}.
-!- DOMAIN: [Protease NS2]: The N-terminus of NS3 is required for the
catalytic activity of protease NS2 (PubMed:17239391). The minimal
catalytic region includes the C-terminus of NS2 and the N-terminus NS3
protease domain (active region NS2-3) (PubMed:17239391).
{ECO:0000269|PubMed:17239391}.
-!- DOMAIN: [Serine protease/helicase NS3]: The N-terminal one-third
contains the protease activity (By similarity). This region contains a
zinc atom that does not belong to the active site, but may play a
structural rather than a catalytic role (PubMed:17239391). This region
is essential for the activity of protease NS2, maybe by contributing to
the folding of the latter (PubMed:17239391). The NTPase/helicase
activity is located in the twothirds C-terminus of NS3, this domain
contains the NTPase and RNA-binding regions (By similarity).
{ECO:0000250|UniProtKB:P26662, ECO:0000250|UniProtKB:P27958,
ECO:0000269|PubMed:17239391}.
-!- DOMAIN: [Non-structural protein 4B]: Contains a glycine zipper region
that critically contributes to the biogenesis of functional ER-derived
replication organelles. {ECO:0000250|UniProtKB:Q99IB8}.
-!- DOMAIN: [Non-structural protein 5A]: The N-terminus of NS5A acts as
membrane anchor (By similarity). The central part of NS5A contains a
variable region called interferon sensitivity determining region (ISDR)
and seems to be intrinsically disordered and interacts with NS5B and
host EIF2AK2 (By similarity). The C-terminus of NS5A contains a
variable region called variable region 3 (V3) (By similarity). ISDR and
V3 may be involved in sensitivity and/or resistance to IFN-alpha
therapy (By similarity). The C-terminus contains a nuclear localization
signal (By similarity). The SH3-binding domain is involved in the
interaction with host BIN1, GRB2 and Src-family kinases (By
similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
mature proteins (By similarity). The structural proteins, core, E1, E2
and p7 are produced by proteolytic processing by host signal peptidases
(By similarity). The core protein precursor is synthesized as a 23 kDa,
which is retained in the ER membrane through the hydrophobic signal
peptide (By similarity). Cleavage by the signal peptidase releases the
21 kDa mature core protein (By similarity). The cleavage of the core
protein precursor occurs between aminoacids 176 and 188 but the exact
cleavage site is not known (By similarity). Some degraded forms of the
core protein appear as well during the course of infection (By
similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and
NS5B) are cleaved by the viral proteases (By similarity).
Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine
protease catalytic domain and regulated by the NS3 N-terminal domain
(By similarity). {ECO:0000250|UniProtKB:P26664,
ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Mature core protein]: Phosphorylated by host PKC and PKA.
{ECO:0000250|UniProtKB:Q01403}.
-!- PTM: [Mature core protein]: Ubiquitinated; mediated by UBE3A and
leading to core protein subsequent proteasomal degradation.
{ECO:0000250|UniProtKB:Q03463}.
-!- PTM: [Envelope glycoprotein E1]: Highly N-glycosylated.
{ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Envelope glycoprotein E2]: Highly N-glycosylated.
{ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Protease NS2]: Palmitoylation is required for NS2/3
autoprocessing and E2 recruitment to membranes.
{ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Non-structural protein 4B]: Palmitoylated. This modification may
play a role in its polymerization or in protein-protein interactions.
{ECO:0000250|UniProtKB:P27958}.
-!- PTM: [Non-structural protein 5A]: Phosphorylated on serines in a basal
form termed p56 (By similarity). p58 is a hyperphosphorylated form of
p56 (By similarity). p56 and p58 coexist in the cell in roughly
equivalent amounts (By similarity). Hyperphosphorylation is dependent
on the presence of NS4A (By similarity). Host CSNK1A1/CKI-alpha or
RPS6KB1 kinases may be responsible for NS5A phosphorylation (By
similarity). {ECO:0000250|UniProtKB:P26662,
ECO:0000250|UniProtKB:P26664}.
-!- PTM: [Non-structural protein 5A]: Tyrosine phosphorylation is essential
for the interaction with host SRC. {ECO:0000250|UniProtKB:Q99IB8}.
-!- PTM: [RNA-directed RNA polymerase]: The N-terminus is phosphorylated by
host PRK2/PKN2. {ECO:0000250|UniProtKB:P26662}.
-!- MISCELLANEOUS: Viral particle assembly takes place at the surface of
ER-derived membranes in close proximity to lipid droplets. NS2
associates with E1/E2 glycoproteins, NS3 and NS5A, which interacts with
the viral RNA and core protein to promote genome encapsidation. The
nucleocapsid buds at the ER membrane where E1/E2 glycoproteins are
anchored and afterward associate with nascent lipid droplet to acquire
APOE and APOC. Secretion of viral particles is probably regulated by
viroporin p7. {ECO:0000305}.
-!- MISCELLANEOUS: [Non-structural protein 5A]: Cell culture adaptation of
the virus leads to mutations in NS5A, reducing its inhibitory effect on
replication. {ECO:0000305}.
-!- MISCELLANEOUS: [Mature 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|UniProtKB:P26662}.
-!- 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="https://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
---------------------------------------------------------------------------
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EMBL; D10750; BAA01583.1; -; Genomic_RNA.
EMBL; AF054247; AAC15722.1; -; Genomic_RNA.
EMBL; AF054248; AAC15723.1; -; Genomic_RNA.
EMBL; AF054249; AAC15724.1; -; Genomic_RNA.
EMBL; AF054250; AAC15725.1; -; Genomic_RNA.
PIR; A61196; A61196.
PIR; PQ0246; PQ0246.
PIR; PQ0804; PQ0804.
PIR; PS0329; PS0329.
PDB; 1NB4; X-ray; 2.00 A; A/B=2420-2989.
PDB; 1NB6; X-ray; 2.60 A; A/B=2420-2989.
PDB; 1NB7; X-ray; 2.90 A; A/B=2420-2989.
PDB; 2F55; X-ray; 3.30 A; A/B/C=1216-1650.
PDB; 2MTS; NMR; -; A=747-809.
PDB; 2XHU; X-ray; 2.29 A; A/B=2420-2989.
PDB; 2XHV; X-ray; 1.90 A; A/B=2420-2989.
PDB; 2XHW; X-ray; 2.66 A; A=2420-2989.
PDB; 2YOJ; X-ray; 1.76 A; A/B=2420-2989.
PDB; 3CSO; X-ray; 2.71 A; A/B=2420-2989.
PDB; 3GNV; X-ray; 2.75 A; A/B=2420-2989.
PDB; 3GNW; X-ray; 2.39 A; A/B=2420-2989.
PDB; 3GOL; X-ray; 2.85 A; A/B=2420-2989.
PDB; 3HKY; X-ray; 1.90 A; A/B=2420-2989.
PDB; 3LKH; X-ray; 2.05 A; A/B=2420-2989.
PDB; 3MWV; X-ray; 2.20 A; A/B=2420-2989.
PDB; 3MWW; X-ray; 2.80 A; A/B=2420-2989.
PDB; 3SKA; X-ray; 1.73 A; A/B=2420-2989.
PDB; 3SKE; X-ray; 1.97 A; A/B=2420-2989.
PDB; 3SKH; X-ray; 2.50 A; A/B=2420-2989.
PDB; 3TYQ; X-ray; 1.60 A; A/B=2420-2989.
PDB; 3TYV; X-ray; 1.65 A; A/B=2420-2989.
PDB; 3U4O; X-ray; 1.77 A; A/B=2420-2989.
PDB; 3U4R; X-ray; 2.00 A; A/B=2420-2989.
PDB; 3UPH; X-ray; 2.00 A; A/B=2420-2989.
PDB; 3UPI; X-ray; 2.00 A; A/B=2420-2989.
PDB; 4DRU; X-ray; 2.10 A; A/B=2420-2982.
PDB; 4EAW; X-ray; 2.00 A; A/B=2420-2981.
PDB; 4GMC; X-ray; 2.70 A; A/B=2420-2989.
PDB; 4IZ0; X-ray; 2.22 A; A/B=2420-2989.
PDB; 4J02; X-ray; 2.00 A; A/B=2420-2989.
PDB; 4J04; X-ray; 2.00 A; A/B=2420-2989.
PDB; 4J06; X-ray; 2.00 A; A/B=2420-2989.
PDB; 4J08; X-ray; 2.10 A; A/B=2420-2989.
PDB; 4J0A; X-ray; 2.40 A; A/B=2420-2989.
PDB; 4JJS; X-ray; 2.20 A; A/B=2420-2989.
PDB; 4JJU; X-ray; 1.91 A; A/B=2420-2989.
PDB; 4JTW; X-ray; 3.00 A; A/B=2420-2989.
PDB; 4JTY; X-ray; 2.60 A; A/B=2420-2989.
PDB; 4JTZ; X-ray; 2.80 A; A/B=2420-2989.
PDB; 4JU1; X-ray; 2.90 A; A/B=2420-2989.
PDB; 4JU2; X-ray; 2.70 A; A/B=2420-2989.
PDB; 4JU3; X-ray; 2.00 A; A/B=2420-2989.
PDB; 4JU4; X-ray; 2.40 A; A/B=2420-2989.
PDB; 4JU6; X-ray; 2.20 A; A/B=2420-2989.
PDB; 4JU7; X-ray; 2.20 A; A/B=2420-2989.
PDB; 4JVQ; X-ray; 2.40 A; A/B=2420-2989.
PDB; 4JY0; X-ray; 2.20 A; A/B=2420-2989.
PDB; 4JY1; X-ray; 2.60 A; A/B=2420-2989.
PDB; 4MZ4; X-ray; 1.63 A; A/B=2420-2989.
PDB; 4OOW; X-ray; 2.57 A; A/B=2420-2989.
PDB; 4RY4; X-ray; 2.59 A; A/B=2420-2989.
PDB; 4RY5; X-ray; 2.71 A; A/B=2420-2989.
PDB; 4RY6; X-ray; 2.52 A; A/B=2420-2989.
PDB; 4RY7; X-ray; 3.00 A; A/B=2420-2989.
PDB; 5CZB; X-ray; 1.96 A; A/B=2420-2981.
PDB; 5NPH; X-ray; 1.70 A; A=529-540.
PDB; 5NPI; X-ray; 2.00 A; D/E=529-540.
PDBsum; 1NB4; -.
PDBsum; 1NB6; -.
PDBsum; 1NB7; -.
PDBsum; 2F55; -.
PDBsum; 2MTS; -.
PDBsum; 2XHU; -.
PDBsum; 2XHV; -.
PDBsum; 2XHW; -.
PDBsum; 2YOJ; -.
PDBsum; 3CSO; -.
PDBsum; 3GNV; -.
PDBsum; 3GNW; -.
PDBsum; 3GOL; -.
PDBsum; 3HKY; -.
PDBsum; 3LKH; -.
PDBsum; 3MWV; -.
PDBsum; 3MWW; -.
PDBsum; 3SKA; -.
PDBsum; 3SKE; -.
PDBsum; 3SKH; -.
PDBsum; 3TYQ; -.
PDBsum; 3TYV; -.
PDBsum; 3U4O; -.
PDBsum; 3U4R; -.
PDBsum; 3UPH; -.
PDBsum; 3UPI; -.
PDBsum; 4DRU; -.
PDBsum; 4EAW; -.
PDBsum; 4GMC; -.
PDBsum; 4IZ0; -.
PDBsum; 4J02; -.
PDBsum; 4J04; -.
PDBsum; 4J06; -.
PDBsum; 4J08; -.
PDBsum; 4J0A; -.
PDBsum; 4JJS; -.
PDBsum; 4JJU; -.
PDBsum; 4JTW; -.
PDBsum; 4JTY; -.
PDBsum; 4JTZ; -.
PDBsum; 4JU1; -.
PDBsum; 4JU2; -.
PDBsum; 4JU3; -.
PDBsum; 4JU4; -.
PDBsum; 4JU6; -.
PDBsum; 4JU7; -.
PDBsum; 4JVQ; -.
PDBsum; 4JY0; -.
PDBsum; 4JY1; -.
PDBsum; 4MZ4; -.
PDBsum; 4OOW; -.
PDBsum; 4RY4; -.
PDBsum; 4RY5; -.
PDBsum; 4RY6; -.
PDBsum; 4RY7; -.
PDBsum; 5CZB; -.
PDBsum; 5NPH; -.
PDBsum; 5NPI; -.
BMRB; O92972; -.
SMR; O92972; -.
IntAct; O92972; 12.
BindingDB; O92972; -.
ChEMBL; CHEMBL3638332; -.
DrugBank; DB08747; (11R)-10-acetyl-11-(2,4-dichlorophenyl)-6-hydroxy-3,3-dimethyl-2,3,4,5,10,11-hexahydro-1H-dibenzo[b,e][1,4]diazepin-1-one.
PRIDE; O92972; -.
ABCD; O92972; 1 sequenced antibody.
euHCVdb; AF054247; -.
euHCVdb; AF054248; -.
euHCVdb; AF054249; -.
euHCVdb; AF054250; -.
euHCVdb; D10750; -.
BRENDA; 2.7.7.48; 2642.
BRENDA; 3.4.21.98; 2642.
EvolutionaryTrace; O92972; -.
Proteomes; UP000008094; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
GO; GO:0044164; C:host cell cytosol; IDA:AgBase.
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:0033644; C:host cell membrane; IDA:AgBase.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:AgBase.
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:0071889; F:14-3-3 protein binding; IPI:AgBase.
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:0019901; F:protein kinase binding; IPI:AgBase.
GO; GO:0005080; F:protein kinase C binding; IPI:AgBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0046332; F:SMAD binding; IPI:AgBase.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0032147; P:activation of protein kinase activity; IDA:AgBase.
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:0032091; P:negative regulation of protein binding; IDA:AgBase.
GO; GO:0010991; P:negative regulation of SMAD protein complex assembly; IMP:AgBase.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:AgBase.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; 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: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.
DisProt; DP01142; -.
Gene3D; 1.20.1280.150; -; 1.
Gene3D; 2.20.25.210; -; 1.
Gene3D; 2.20.25.220; -; 1.
Gene3D; 2.30.30.710; -; 1.
Gene3D; 2.40.10.10; -; 1.
Gene3D; 3.30.70.270; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR043502; DNA/RNA_pol_sf.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR042205; HCV_NS2_C.
InterPro; IPR042209; HCV_NS2_N.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR038568; HCV_NS5A_1B_sf.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR038170; NS5A_1a_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR004109; Peptidase_S29_NS3.
InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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.
SMART; SM00487; DEXDc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF56672; SSF56672; 1.
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; 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;
Isopeptide bond; Lipoprotein; Magnesium; 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; 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
/note="Removed; by host"
/evidence="ECO:0000250|UniProtKB:P26664"
CHAIN 2..3010
/note="Genome polyprotein"
/id="PRO_0000450912"
CHAIN 2..191
/note="Core protein precursor"
/id="PRO_0000278742"
CHAIN 2..177
/note="Mature core protein"
/id="PRO_0000278743"
PROPEP 178..191
/note="ER anchor for the core protein, removed in mature
form by host signal peptidase"
/id="PRO_0000278744"
CHAIN 192..383
/note="Envelope glycoprotein E1"
/id="PRO_0000278745"
CHAIN 384..746
/note="Envelope glycoprotein E2"
/id="PRO_0000278746"
CHAIN 747..809
/note="Viroporin p7"
/id="PRO_0000278747"
CHAIN 810..1026
/note="Protease NS2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
/id="PRO_0000278748"
CHAIN 1027..1657
/note="Serine protease/helicase NS3"
/id="PRO_0000278749"
CHAIN 1658..1711
/note="Non-structural protein 4A"
/id="PRO_0000278750"
CHAIN 1712..1972
/note="Non-structural protein 4B"
/id="PRO_0000278751"
CHAIN 1973..2419
/note="Non-structural protein 5A"
/id="PRO_0000278752"
CHAIN 2420..3010
/note="RNA-directed RNA polymerase"
/id="PRO_0000278753"
TOPO_DOM 2..168
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 169..189
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 190..358
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 359..379
/note="Helical"
/evidence="ECO:0000250|UniProtKB:P27958"
TOPO_DOM 380..725
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 726..746
/note="Helical"
/evidence="ECO:0000250|UniProtKB:P27958"
TOPO_DOM 747..757
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 758..778
/note="Helical"
/evidence="ECO:0000250|UniProtKB:P27958"
TOPO_DOM 779..781
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 782..803
/note="Helical"
/evidence="ECO:0000250|UniProtKB:P27958"
TOPO_DOM 804..813
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 814..834
/note="Helical"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TOPO_DOM 835..838
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TRANSMEM 839..859
/note="Helical"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TOPO_DOM 860..881
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TRANSMEM 882..902
/note="Helical"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TOPO_DOM 903..1657
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
TRANSMEM 1658..1678
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1679..1805
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1806..1824
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1825..1828
/note="Lumenal"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 1829..1849
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1850
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1851..1871
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1872..1881
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 1882..1902
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1903..1972
/note="Cytoplasmic"
/evidence="ECO:0000255"
INTRAMEM 1973..2002
/evidence="ECO:0000250|UniProtKB:P27958"
TOPO_DOM 2003..2989
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P27958"
TRANSMEM 2990..3010
/note="Helical"
/evidence="ECO:0000250|UniProtKB:P27958"
DOMAIN 903..1026
/note="Peptidase C18"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
DOMAIN 1027..1208
/note="Peptidase S29"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
DOMAIN 1217..1369
/note="Helicase ATP-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
DOMAIN 2633..2751
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
NP_BIND 1230..1237
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
REGION 2..75
/note="Disordered; RNA-binding and RNA chaperoning"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 2..59
/note="Interaction with DDX3X"
/evidence="ECO:0000250|UniProtKB:Q5EG65"
REGION 2..58
/note="Interaction with EIF2AK2/PKR"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 2..23
/note="Interaction with STAT1"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 112..152
/note="Important for endoplasmic reticulum and
mitochondrial localization"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 122..173
/note="Interaction with APOA2"
/evidence="ECO:0000250|UniProtKB:P29846"
REGION 164..167
/note="Important for lipid droplets localization"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 265..296
/note="Important for fusion"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 385..411
/note="HVR1"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 474..479
/note="HVR2"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 480..493
/note="CD81-binding 1"
/evidence="ECO:0000250|UniProtKB:P26663"
REGION 544..551
/note="CD81-binding 2"
/evidence="ECO:0000250|UniProtKB:P26663"
REGION 660..671
/note="PKR/eIF2-alpha phosphorylation homology domain
(PePHD)"
/evidence="ECO:0000250"
REGION 904..1206
/note="Protease NS2-3"
/evidence="ECO:0000250|UniProtKB:P26663"
REGION 929..949
/note="Interaction with host SCPS1"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
REGION 1486..1497
/note="RNA-binding"
/evidence="ECO:0000250|UniProtKB:P26663"
REGION 1679..1690
/note="NS3-binding"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 2120..2332
/note="Transcriptional activation"
/evidence="ECO:0000255"
REGION 2120..2208
/note="FKBP8-binding"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 2135..2139
/note="Interaction with non-structural protein 4A"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 2189..2441
/note="Interaction with host SKP2"
/evidence="ECO:0000250|UniProtKB:P27958"
REGION 2210..2275
/note="Interaction with EIF2AK2/PKR"
/evidence="ECO:0000250|UniProtKB:P26663"
REGION 2210..2249
/note="ISDR"
/evidence="ECO:0000250|UniProtKB:P26662"
REGION 2249..2306
/note="NS4B-binding"
/evidence="ECO:0000255"
REGION 2354..2377
/note="V3"
/evidence="ECO:0000250"
MOTIF 5..13
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOTIF 38..43
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOTIF 58..64
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOTIF 66..71
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOTIF 1316..1319
/note="DECH box"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOTIF 2322..2325
/note="SH3-binding"
/evidence="ECO:0000255"
MOTIF 2326..2334
/note="Nuclear localization signal"
/evidence="ECO:0000250|UniProtKB:P26662"
COMPBIAS 796..803
/note="Poly-Leu"
COMPBIAS 1432..1435
/note="Poly-Val"
COMPBIAS 2282..2327
/note="Pro-rich"
COMPBIAS 2993..2998
/note="Poly-Leu"
ACT_SITE 952
/note="For protease NS2 activity; shared with dimeric
partner"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
ACT_SITE 972
/note="For protease NS2 activity; shared with dimeric
partner"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
ACT_SITE 993
/note="For protease NS2 activity; shared with dimeric
partner"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
ACT_SITE 1083
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
ACT_SITE 1107
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166"
ACT_SITE 1165
/note="Charge relay system; for serine protease NS3
activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166,
ECO:0000269|PubMed:17239391"
METAL 1123
/note="Zinc; structural; required for NS3 protease activity
and NS2/3 auto-cleavage activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166,
ECO:0000269|PubMed:17239391"
METAL 1125
/note="Zinc; required for NS3 protease activity and NS2/3
auto-cleavage activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166,
ECO:0000269|PubMed:17239391"
METAL 1171
/note="Zinc; required for NS3 protease activity and NS2/3
auto-cleavage activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166,
ECO:0000269|PubMed:17239391"
METAL 1175
/note="Zinc; required for NS3 protease activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01166,
ECO:0000269|PubMed:17239391"
METAL 1237
/note="Magnesium; catalytic; for NS3 helicase activity"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 1317
/note="Magnesium; catalytic; for NS3 helicase activity"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 2011
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 2029
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 2031
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 2052
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
METAL 2639
/note="Magnesium; catalytic; for RNA-directed RNA
polymerase activity"
/evidence="ECO:0000250|UniProtKB:P26663"
METAL 2737
/note="Magnesium; catalytic; for RNA-directed RNA
polymerase activity"
/evidence="ECO:0000250|UniProtKB:P26663"
METAL 2738
/note="Magnesium; catalytic; for RNA-directed RNA
polymerase activity"
/evidence="ECO:0000250|UniProtKB:P26663"
SITE 177..178
/note="Cleavage; by host signal peptide peptidase"
/evidence="ECO:0000250|UniProtKB:P26662"
SITE 191..192
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P26662"
SITE 383..384
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250|UniProtKB:P26662"
SITE 746..747
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250"
SITE 809..810
/note="Cleavage; by host signal peptidase"
/evidence="ECO:0000250"
SITE 1026..1027
/note="Cleavage; by protease NS2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01030"
SITE 1657..1658
/note="Cleavage; by serine protease/helicase NS3"
/evidence="ECO:0000250|UniProtKB:P27958"
SITE 1711..1712
/note="Cleavage; by serine protease/helicase NS3"
/evidence="ECO:0000250|UniProtKB:P27958"
SITE 1972..1973
/note="Cleavage; by serine protease/helicase NS3"
/evidence="ECO:0000250|UniProtKB:P27958"
SITE 2419..2420
/note="Cleavage; by serine protease/helicase NS3"
/evidence="ECO:0000250|UniProtKB:P27958"
MOD_RES 2
/note="N-acetylserine; by host"
/evidence="ECO:0000250|UniProtKB:Q913V3"
MOD_RES 53
/note="Phosphoserine; by host"
/evidence="ECO:0000250|UniProtKB:Q01403"
MOD_RES 99
/note="Phosphoserine; by host"
/evidence="ECO:0000250|UniProtKB:Q01403"
MOD_RES 116
/note="Phosphoserine; by host PKA"
/evidence="ECO:0000250|UniProtKB:Q01403"
MOD_RES 2194
/note="Phosphoserine; by host; in p56"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
MOD_RES 2197
/note="Phosphoserine; by host; in p58"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
MOD_RES 2201
/note="Phosphoserine; by host; in p58"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
MOD_RES 2204
/note="Phosphoserine; by host; in p58"
/evidence="ECO:0000250|UniProtKB:Q9WMX2"
MOD_RES 2207
/note="Phosphoserine; by host; in p58"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOD_RES 2210
/note="Phosphoserine; by host; in p58"
/evidence="ECO:0000250|UniProtKB:Q99IB8"
MOD_RES 2448
/note="Phosphoserine; by host"
/evidence="ECO:0000250|UniProtKB:P26662"
MOD_RES 2461
/note="Phosphoserine; by host"
/evidence="ECO:0000250|UniProtKB:P26662"
LIPID 922
/note="S-palmitoyl cysteine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
LIPID 1968
/note="S-palmitoyl cysteine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
LIPID 1972
/note="S-palmitoyl cysteine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 196
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 209
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 234
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 250
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 305
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255"
CARBOHYD 417
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 423
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 430
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 448
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 478
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255"
CARBOHYD 532
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 540
/note="N-linked (GlcNAc...) asparagine; by host"
/evidence="ECO:0000255"
CARBOHYD 556
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 576
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 623
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
CARBOHYD 645
/note="N-linked (GlcNAc...) (high mannose) asparagine; by
host"
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 429..552
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 452..459
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 486..494
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 503..508
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 564..569
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 581..585
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 597..620
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 607..644
/evidence="ECO:0000250|UniProtKB:P27958"
DISULFID 652..677
/evidence="ECO:0000250|UniProtKB:P27958"
CROSSLNK 2350
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P27958"
VARIANT 52
/note="A -> T (in strain: Isolate pCV-J4L4S and Isolate HC-
J4/91)"
VARIANT 70
/note="R -> Q (in strain: Isolate HC-J4/91)"
VARIANT 231
/note="R -> Q (in strain: Isolate pCV-J4L2S and Isolate
pCV-J4L6S)"
VARIANT 250
/note="N -> D (in strain: Isolate HC-J4/91 and Isolate pCV-
J4L4S)"
VARIANT 304
/note="C -> Y (in strain: Isolate pCV-J4L2S)"
VARIANT 384..390
/note="ETHTTGR -> ATYTSGG (in strain: Isolate HC-J4/91)"
VARIANT 394
/note="H -> R (in strain: Isolate HC-J4/91 and Isolate pCV-
J4L4S)"
VARIANT 434
/note="Q -> H (in strain: Isolate HC-J4/91)"
VARIANT 438
/note="F -> L (in strain: Isolate pCV-J4L4S)"
VARIANT 444
/note="A -> T (in strain: Isolate pCV-J4L4S and Isolate HC-
J4/91)"
VARIANT 450
/note="S -> P (in strain: Isolate pCV-J4L4S)"
VARIANT 464
/note="W -> G (in strain: Isolate HC-J4/91)"
VARIANT 476
/note="K -> E (in strain: Isolate pCV-J4L4S and Isolate HC-
J4/91)"
VARIANT 480
/note="S -> P (in strain: Isolate HC-J4/91)"
VARIANT 496
/note="V -> I (in strain: Isolate pCV-J4L4S and Isolate HC-
J4/91)"
VARIANT 536
/note="V -> M (in strain: Isolate pCV-J4L2S)"
VARIANT 934
/note="V -> I (in strain: Isolate pCV-J4L2S)"
VARIANT 937
/note="A -> V (in strain: Isolate pCV-J4L6S)"
VARIANT 1043
/note="I -> V (in strain: Isolate pCV-J4L2S and Isolate
pCV-J4L4S)"
VARIANT 1215
/note="S -> T (in strain: Isolate pCV-J4L6S)"
VARIANT 1223
/note="F -> S (in strain: Isolate pCV-J4L2S)"
VARIANT 1528
/note="Y -> H (in strain: Isolate pCV-J4L4S)"
VARIANT 1662
/note="L -> P (in strain: Isolate pCV-J4L2S)"
VARIANT 1753
/note="K -> R (in strain: Isolate pCV-J4L2S)"
VARIANT 1805
/note="N -> H (in strain: Isolate pCV-J4L2S)"
VARIANT 1949
/note="S -> P (in strain: Isolate pCV-J4L4S)"
VARIANT 2138
/note="K -> R (in strain: Isolate pCV-J4L4S)"
VARIANT 2385
/note="Y -> H (in strain: Isolate pCV-J4L4S)"
VARIANT 2785
/note="C -> R (in strain: Isolate pCV-J4L2S)"
VARIANT 2824
/note="I -> V (in strain: Isolate pCV-J4L2S)"
VARIANT 2999
/note="S -> F (in strain: Isolate HC-J4/91)"
MUTAGEN 922
/note="C->A: Almost complete loss of NS2/3 auto-cleavage
activity; slight loss of NS3 protease activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1123
/note="C->A: Almost complete loss of NS3 protease activity
and NS2/3 auto-cleavage activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1125
/note="C->A: Almost complete loss of NS3 protease activity
and NS2/3 auto-cleavage activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1165
/note="S->A: Almost complete loss of NS3 protease activity;
no effect on NS2/3 auto-cleavage activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1171
/note="C->A: Almost complete loss of NS3 protease activity
and NS2/3 auto-cleavage activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1175
/note="H->A: Slight loss of NS2/3 auto-cleavage activity
and 70% loss of NS3 protease activity."
/evidence="ECO:0000269|PubMed:17239391"
MUTAGEN 1185
/note="C->A: No effect on NS2/3 auto-cleavage activity;
slight loss of NS3 protease activity."
/evidence="ECO:0000269|PubMed:17239391"
HELIX 535..538
/evidence="ECO:0000244|PDB:5NPH"
HELIX 750..760
/evidence="ECO:0000244|PDB:2MTS"
HELIX 762..767
/evidence="ECO:0000244|PDB:2MTS"
HELIX 769..777
/evidence="ECO:0000244|PDB:2MTS"
HELIX 786..789
/evidence="ECO:0000244|PDB:2MTS"
HELIX 790..792
/evidence="ECO:0000244|PDB:2MTS"
HELIX 797..802
/evidence="ECO:0000244|PDB:2MTS"
STRAND 1224..1227
/evidence="ECO:0000244|PDB:2F55"
STRAND 1232..1235
/evidence="ECO:0000244|PDB:2F55"
TURN 1236..1238
/evidence="ECO:0000244|PDB:2F55"
HELIX 1239..1245
/evidence="ECO:0000244|PDB:2F55"
TURN 1246..1248
/evidence="ECO:0000244|PDB:2F55"
STRAND 1251..1256
/evidence="ECO:0000244|PDB:2F55"
HELIX 1258..1270
/evidence="ECO:0000244|PDB:2F55"
STRAND 1277..1279
/evidence="ECO:0000244|PDB:2F55"
STRAND 1292..1295
/evidence="ECO:0000244|PDB:2F55"
HELIX 1296..1301
/evidence="ECO:0000244|PDB:2F55"
TURN 1302..1306
/evidence="ECO:0000244|PDB:2F55"
STRAND 1311..1315
/evidence="ECO:0000244|PDB:2F55"
HELIX 1323..1335
/evidence="ECO:0000244|PDB:2F55"
HELIX 1337..1339
/evidence="ECO:0000244|PDB:2F55"
STRAND 1342..1346
/evidence="ECO:0000244|PDB:2F55"
STRAND 1362..1366
/evidence="ECO:0000244|PDB:2F55"
HELIX 1382..1385
/evidence="ECO:0000244|PDB:2F55"
STRAND 1386..1393
/evidence="ECO:0000244|PDB:2F55"
HELIX 1397..1408
/evidence="ECO:0000244|PDB:2F55"
TURN 1409..1411
/evidence="ECO:0000244|PDB:2F55"
STRAND 1414..1417
/evidence="ECO:0000244|PDB:2F55"
HELIX 1423..1425
/evidence="ECO:0000244|PDB:2F55"
STRAND 1428..1436
/evidence="ECO:0000244|PDB:2F55"
STRAND 1448..1453
/evidence="ECO:0000244|PDB:2F55"
STRAND 1456..1462
/evidence="ECO:0000244|PDB:2F55"
STRAND 1467..1469
/evidence="ECO:0000244|PDB:2F55"
STRAND 1471..1478
/evidence="ECO:0000244|PDB:2F55"
HELIX 1483..1486
/evidence="ECO:0000244|PDB:2F55"
HELIX 1488..1490
/evidence="ECO:0000244|PDB:2F55"
STRAND 1491..1495
/evidence="ECO:0000244|PDB:2F55"
STRAND 1497..1503
/evidence="ECO:0000244|PDB:2F55"
HELIX 1514..1525
/evidence="ECO:0000244|PDB:2F55"
HELIX 1532..1543
/evidence="ECO:0000244|PDB:2F55"
HELIX 1555..1563
/evidence="ECO:0000244|PDB:2F55"
HELIX 1570..1577
/evidence="ECO:0000244|PDB:2F55"
TURN 1578..1580
/evidence="ECO:0000244|PDB:2F55"
HELIX 1584..1596
/evidence="ECO:0000244|PDB:2F55"
HELIX 1615..1617
/evidence="ECO:0000244|PDB:2F55"
STRAND 1627..1629
/evidence="ECO:0000244|PDB:2F55"
HELIX 1640..1648
/evidence="ECO:0000244|PDB:2F55"
STRAND 2421..2425
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2444..2449
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2453..2455
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2456..2458
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2461..2463
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2464..2471
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2481..2494
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2504..2509
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2513..2515
/evidence="ECO:0000244|PDB:4JU1"
STRAND 2519..2521
/evidence="ECO:0000244|PDB:4JJU"
HELIX 2524..2528
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2532..2547
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2549..2551
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2555..2559
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2563..2565
/evidence="ECO:0000244|PDB:3TYQ"
TURN 2568..2570
/evidence="ECO:0000244|PDB:3HKY"
STRAND 2578..2581
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2584..2606
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2607..2609
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2611..2613
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2616..2629
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2630..2638
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2643..2646
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2649..2659
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2666..2678
/evidence="ECO:0000244|PDB:3TYQ"
TURN 2679..2681
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2683..2686
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2692..2696
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2701..2703
/evidence="ECO:0000244|PDB:4J08"
HELIX 2706..2724
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2728..2735
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2738..2744
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2748..2764
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2769..2771
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2776..2778
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2779..2781
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2787..2793
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2799..2805
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2808..2819
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2826..2834
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2838..2842
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2844..2854
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2858..2860
/evidence="ECO:0000244|PDB:1NB4"
STRAND 2862..2866
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2869..2873
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2875..2877
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2878..2886
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2888..2891
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2898..2911
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2916..2933
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2935..2944
/evidence="ECO:0000244|PDB:3TYQ"
HELIX 2946..2948
/evidence="ECO:0000244|PDB:3TYQ"
STRAND 2949..2951
/evidence="ECO:0000244|PDB:5CZB"
HELIX 2959..2963
/evidence="ECO:0000244|PDB:3TYQ"
TURN 2967..2970
/evidence="ECO:0000244|PDB:3TYQ"
TURN 2975..2977
/evidence="ECO:0000244|PDB:4RY7"
SEQUENCE 3010 AA; 326767 MW; 0480D428ABDE9847 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KASERSQPRG
RRQPIPKARR PEGRAWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTIPAS AYEVRNVSGI YHVTNDCSNS SIVYEAADVI MHTPGCVPCV REGNSSRCWV
ALTPTLAARN ASVPTTTIRR HVDLLVGTAA FCSAMYVGDL CGSIFLVSQL FTFSPRRHET
VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG AHWGVLAGLA
YYSMVGNWAK VLIVALLFAG VDGETHTTGR VAGHTTSGFT SLFSSGASQK IQLVNTNGSW
HINRTALNCN DSLQTGFFAA LFYAHKFNSS GCPERMASCR PIDWFAQGWG PITYTKPNSS
DQRPYCWHYA PRPCGVVPAS QVCGPVYCFT PSPVVVGTTD RSGVPTYSWG ENETDVMLLN
NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNRTLI CPTDCFRKHP EATYTKCGSG
PWLTPRCLVD YPYRLWHYPC TLNFSIFKVR MYVGGVEHRL NAACNWTRGE RCNLEDRDRS
ELSPLLLSTT EWQILPCAFT TLPALSTGLI HLHQNIVDVQ YLYGVGSAFV SFAIKWEYIL
LLFLLLADAR VCACLWMMLL IAQAEAALEN LVVLNAASVA GAHGILSFLV FFCAAWYIKG
RLAPGAAYAF YGVWPLLLLL LALPPRAYAL DREMAASCGG AVLVGLVFLT LSPYYKVFLT
RLIWWLQYFI TRAEAHMQVW VPPLNVRGGR DAIILLTCAV HPELIFDITK LLLAILGPLM
VLQAGITRVP YFVRAQGLIR ACMLVRKVAG GHYVQMAFMK LGALTGTYVY NHLTPLRDWA
HAGLRDLAVA VEPVVFSAME TKVITWGADT AACGDIILGL PVSARRGKEI FLGPADSLEG
QGWRLLAPIT AYSQQTRGVL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCINGVCWT
VYHGAGSKTL AGPKGPITQM YTNVDLDLVG WQAPPGARSM TPCSCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPVSY LKGSSGGPLL CPSGHVVGVF RAAVCTRGVA KAVDFIPVES
METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGIDPNIRT GVRTITTGGS ITYSTYGKFL ADGGCSGGAY DIIICDECHS
TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEIGLSNN GEIPFYGKAI
PIEAIKGGRH LIFCHSKKKC DELAAKLTGL GLNAVAYYRG LDVSVIPPIG DVVVVATDAL
MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRSGIYR
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEVILTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
VIVGRIILSG KPAVVPDREV LYQEFDEMEE CASQLPYIEQ GMQLAEQFKQ KALGLLQTAT
KQAEAAAPVV ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
LTTQNTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
GALVAFKVMS GEVPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV
WDWICTVLTD FKTWLQSKLL PRLPGVPFLS CQRGYKGVWR GDGIMQTTCP CGAQIAGHVK
NGSMRIVGPR TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPACKPL LREDVTFQVG LNQYLVGSQL
PCEPEPDVTV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTHHD
SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFEPLH AEGDEREISV AAEILRKSRK
FPSALPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPTK APPIPPPRRK RTVVLTESNV
SSALAELATK TFGSSGSSAV DSGTATALPD LASDDGDKGS DVESYSSMPP LEGEPGDPDL
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINPLSNSLL RHHNMVYATT
SRSASLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK LLSIEEACKL TPPHSAKSKF
GYGAKDVRNL SSRAVNHIRS VWEDLLEDTE TPIDTTIMAK SEVFCVQPEK GGRKPARLIV
FPDLGVRVCE KMALYDVVST LPQAVMGSSY GFQYSPKQRV EFLVNTWKSK KCPMGFSYDT
RCFDSTVTES DIRVEESIYQ CCDLAPEARQ AIRSLTERLY IGGPLTNSKG QNCGYRRCRA
SGVLTTSCGN TLTCYLKATA ACRAAKLQDC TMLVNGDDLV VICESAGTQE DAAALRAFTE
AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETAR
HTPINSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ
IIERLHGLSA FTLHSYSPGE INRVASCLRK LGVPPLRTWR HRARSVRAKL LSQGGRAATC
GRYLFNWAVR TKLKLTPIPA ASQLDLSGWF VAGYSGGDIY HSLSRARPRW FPLCLLLLSV
GVGIYLLPNR


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DS-MB-01485 Mouse Anti-Hepatitis C Virus Non-structural Protein 4a (NS4a) Antigen 100
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 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