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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_HCVJA              Reviewed;        3010 AA.
P26662; P89966; Q81755;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 181.
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 1b (isolate Japanese) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=11116;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2175903; DOI=10.1073/pnas.87.24.9524;
Kato N., Hijikata M., Ootsuyama Y., Nakagawa M., Ohkoshi S.,
Sugimura T., Shimotohno K.;
"Molecular cloning of the human hepatitis C virus genome from Japanese
patients with non-A, non-B hepatitis.";
Proc. Natl. Acad. Sci. U.S.A. 87:9524-9528(1990).
[2]
DISCUSSION OF SEQUENCE.
PubMed=1849488; DOI=10.1016/0014-5793(91)80322-T;
Kato N., Hijikata M., Nakagawa M., Ootsuyama Y., Muraiso K.,
Ohkoshi S., Shimotohno K.;
"Molecular structure of the Japanese hepatitis C viral genome.";
FEBS Lett. 280:325-328(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Tanaka T.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 723-1908, IDENTIFICATION OF BOTH
PROTEASES, AND MUTAGENESIS OF CYS-922; HIS-932; HIS-952; GLU-972;
GLU-980; CYS-993; GLU-1009; GLU-1058; HIS-1083; ASP-1107; CYS-1123;
CYS-1125; HIS-1136; SER-1165; CYS-1171; HIS-1175; CYS-1185; GLU-1199;
GLU-1202; HIS-1227 AND HIS-1229.
PubMed=8392606;
Hijikata M., Mizushima H., Akagi T., Mori S., Kakiuchi N., Kato N.,
Tanaka T., Kimura K., Shimotohno K.;
"Two distinct proteinase activities required for the processing of a
putative nonstructural precursor protein of hepatitis C virus.";
J. Virol. 67:4665-4675(1993).
[5]
INHIBITION OF HEPATITIS B VIRUS GENE EXPRESSION.
PubMed=8396658;
Shih C.-M., Lo S.J., Miyamura T., Chen S.-Y., Lee Y.-H.W.;
"Suppression of hepatitis B virus expression and replication by
hepatitis C virus core protein in HuH-7 cells.";
J. Virol. 67:5823-5832(1993).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF HIS-1083;
ASP-1107 AND SER-1165, AND IDENTIFICATION OF THE SERINE PROTEASE.
PubMed=8389908;
Bartenschlager R., Ahlborn-Laake L., Mous J., Jacobsen H.;
"Nonstructural protein 3 of the hepatitis C virus encodes a serine-
type proteinase required for cleavage at the NS3/4 and NS4/5
junctions.";
J. Virol. 67:3835-3844(1993).
[7]
PHOSPHORYLATION OF NS5A.
PubMed=7999043; DOI=10.1006/bbrc.1994.2667;
Kaneko T., Tanji Y., Satoh S., Hijikata M., Asabe S., Kimura K.,
Shimotohno K.;
"Production of two phosphoproteins from the NS5A region of the
hepatitis C viral genome.";
Biochem. Biophys. Res. Commun. 205:320-326(1994).
[8]
MUTAGENESIS OF SER-2194; SER-2197; SER-2200; SER-2201; SER-2202;
SER-2204; SER-2207; SER-2210 AND SER-2221.
PubMed=7769656;
Tanji Y., Kaneko T., Satoh S., Shimotohno K.;
"Phosphorylation of hepatitis C virus-encoded nonstructural protein
NS5A.";
J. Virol. 69:3980-3986(1995).
[9]
FUNCTION OF NS5A.
PubMed=8531962; DOI=10.1056/NEJM199601113340203;
Enomoto N., Sakuma I., Asahina Y., Kurosaki M., Murakami T.,
Yamamoto C., Ogura Y., Izumi N., Marumo F., Sato C.;
"Mutations in the nonstructural protein 5A gene and response to
interferon in patients with chronic hepatitis C virus 1b infection.";
N. Engl. J. Med. 334:77-81(1996).
[10]
FUNCTION OF NS5A.
PubMed=9343247;
Kato N., Lan K.H., Ono-Nita S.K., Shiratori Y., Omata M.;
"Hepatitis C virus nonstructural region 5A protein is a potent
transcriptional activator.";
J. Virol. 71:8856-8859(1997).
[11]
ZINC-BINDING REGION (SERINE PROTEASE NS3), COFACTOR (SERINE PROTEASE
NS3), AND MUTAGENESIS OF CYS-1042; CYS-1073; CYS-1078; HIS-1083;
HIS-1136; SER-1165; HIS-1175; CYS-1185; HIS-1227 AND HIS-1229.
PubMed=9060645;
Stempniak M., Hostomska Z., Nodes B.R., Hostomsky Z.;
"The NS3 proteinase domain of hepatitis C virus is a zinc-containing
enzyme.";
J. Virol. 71:2881-2886(1997).
[12]
SUBCELLULAR LOCATION OF CORE PROTEIN.
PubMed=9621068;
Yasui K., Wakita T., Tsukiyama-Kohara K., Funahashi S., Ichikawa M.,
Kajita T., Moradpour D., Wands J.R., Kohara M.;
"The native form and maturation process of hepatitis C virus core
protein.";
J. Virol. 72:6048-6055(1998).
[13]
DOMAIN ISDR REGION.
PubMed=9525599;
Pawlotsky J.-M., Germanidis G., Neumann A.U., Pellerin M.,
Frainais P.-O., Dhumeaux D.;
"Interferon resistance of hepatitis C virus genotype 1b: relationship
to nonstructural 5A gene quasispecies mutations.";
J. Virol. 72:2795-2805(1998).
[14]
SUBCELLULAR LOCATION OF NS5A.
PubMed=10793006; DOI=10.1006/viro.2000.0287;
Satoh S., Hirota M., Noguchi T., Hijikata M., Handa H., Shimotohno K.;
"Cleavage of hepatitis C virus nonstructural protein 5A by a caspase-
like protease(s) in mammalian cells.";
Virology 270:476-487(2000).
[15]
OLIGOMERIZATION OF NS5B.
PubMed=11907226; DOI=10.1128/JVI.76.8.3865-3872.2002;
Wang Q.M., Hockman M.A., Staschke K., Johnson R.B., Case K.A., Lu J.,
Parsons S., Zhang F., Rathnachalam R., Kirkegaard K., Colacino J.M.;
"Oligomerization and cooperative RNA synthesis activity of hepatitis C
virus RNA-dependent RNA polymerase.";
J. Virol. 76:3865-3872(2002).
[16]
INHIBITION OF P7 BY AMANTADINE.
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).
[17]
INTERACTION OF CORE PROTEIN WITH HUMAN SP110.
PubMed=14559998; DOI=10.1128/MCB.23.21.7498-7509.2003;
Watashi K., Hijikata M., Tagawa A., Doi T., Marusawa H.,
Shimotohno K.;
"Modulation of retinoid signaling by a cytoplasmic viral protein via
sequestration of Sp110b, a potent transcriptional corepressor of
retinoic acid receptor, from the nucleus.";
Mol. Cell. Biol. 23:7498-7509(2003).
[18]
CLEAVAGE OF CORE PROTEIN BY THE SIGNAL PEPTIDASE, AND MUTAGENESIS OF
LEU-139; VAL-140; LEU-144; ILE-176; PHE-177; LEU-178; LEU-179;
LEU-181; LEU-182; SER-183 AND CYS-184.
PubMed=15163730; DOI=10.1128/JVI.78.12.6370-6380.2004;
Okamoto K., Moriishi K., Miyamura T., Matsuura Y.;
"Intramembrane proteolysis and endoplasmic reticulum retention of
hepatitis C virus core protein.";
J. Virol. 78:6370-6380(2004).
[19]
FUNCTION OF CORE PROTEIN.
PubMed=15760888; DOI=10.1074/jbc.M501826200;
Boni S., Lavergne J.-P., Boulant S., Cahour A.;
"Hepatitis C virus core protein acts as a trans-modulating factor on
internal translation initiation of the viral RNA.";
J. Biol. Chem. 280:17737-17748(2005).
[20]
INTERACTION OF CORE PROTEIN WITH HUMAN STAT1.
PubMed=15825084; DOI=10.1053/j.gastro.2005.02.006;
Lin W., Choe W.H., Hiasa Y., Kamegaya Y., Blackard J.T., Schmidt E.V.,
Chung R.T.;
"Hepatitis C virus expression suppresses interferon signaling by
degrading STAT1.";
Gastroenterology 128:1034-1041(2005).
[21]
SUBCELLULAR LOCATION OF CORE PROTEIN.
PubMed=15613354; DOI=10.1128/JVI.79.2.1271-1281.2005;
Suzuki R., Sakamoto S., Tsutsumi T., Rikimaru A., Tanaka K.,
Shimoike T., Moriishi K., Iwasaki T., Mizumoto K., Matsuura Y.,
Miyamura T., Suzuki T.;
"Molecular determinants for subcellular localization of hepatitis C
virus core protein.";
J. Virol. 79:1271-1281(2005).
[22]
CHARACTERIZATION OF NS5A.
PubMed=16126720; DOI=10.1074/jbc.M508175200;
Huang L., Hwang J., Sharma S.D., Hargittai M.R., Chen Y., Arnold J.J.,
Raney K.D., Cameron C.E.;
"Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding
protein.";
J. Biol. Chem. 280:36417-36428(2005).
[23]
INTERACTION OF NS5A AND NS5B WITH HUMAN VAPB.
PubMed=16227268; DOI=10.1128/JVI.79.21.13473-13482.2005;
Hamamoto I., Nishimura Y., Okamoto T., Aizaki H., Liu M., Mori Y.,
Abe T., Suzuki T., Lai M.M., Miyamura T., Moriishi K., Matsuura Y.;
"Human VAP-B is involved in hepatitis C virus replication through
interaction with NS5A and NS5B.";
J. Virol. 79:13473-13482(2005).
[24]
INTERACTION OF CORE PROTEIN WITH HUMAN STAT1.
PubMed=16940534; DOI=10.1128/JVI.00459-06;
Lin W., Kim S.S., Yeung E., Kamegaya Y., Blackard J.T., Kim K.A.,
Holtzman M.J., Chung R.T.;
"Hepatitis C virus core protein blocks interferon signaling by
interaction with the STAT1 SH2 domain.";
J. Virol. 80:9226-9235(2006).
[25]
INTERACTION OF NS5A WITH HUMAN FKBP8, AND SUBCELLULAR LOCATION OF
NS5A.
PubMed=16844119; DOI=10.1016/j.febslet.2006.07.002;
Wang J., Tong W., Zhang X., Chen L., Yi Z., Pan T., Hu Y., Xiang L.,
Yuan Z.;
"Hepatitis C virus non-structural protein NS5A interacts with FKBP38
and inhibits apoptosis in Huh7 hepatoma cells.";
FEBS Lett. 580:4392-4400(2006).
[26]
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).
[27]
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).
[28]
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).
[29]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1027-1213.
PubMed=10702283; DOI=10.1074/jbc.275.10.7152;
Di Marco S., Rizzi M., Volpari C., Walsh M.A., Narjes F.,
Colarusso S., De Francesco R., Matassa V.G., Sollazzo M.;
"Inhibition of the hepatitis C virus NS3/4A protease. The crystal
structures of two protease-inhibitor complexes.";
J. Biol. Chem. 275:7152-7157(2000).
[30]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1027-1213 IN COMPLEX WITH A
PEPTIDOMIMETIC INHIBITOR.
PubMed=15588076; DOI=10.1021/jm049435d;
Ontoria J.M., Di Marco S., Conte I., Di Francesco M.E., Gardelli C.,
Koch U., Matassa V.G., Poma M., Steinkuehler C., Volpari C.,
Harper S.;
"The design and enzyme-bound crystal structure of indoline based
peptidomimetic inhibitors of hepatitis C virus NS3 protease.";
J. Med. Chem. 47:6443-6446(2004).
-!- 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.
-!- 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.
-!- 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: Serine protease NS3:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:9060645};
Note=Binds 1 zinc ion. {ECO:0000269|PubMed:9060645};
-!- COFACTOR: Non-structural protein 5A:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion in the 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.
-!- 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 transcription. In addition to
blocking the formation of phosphorylated STAT1, the core protein
also promotes ubiquitin-mediated proteasome-dependent degradation
of STAT1. Interacts 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}.
-!- INTERACTION:
Q07812:BAX (xeno); NbExp=3; IntAct=EBI-9099462, EBI-516580;
P62993:GRB2 (xeno); NbExp=3; IntAct=EBI-9099462, EBI-401755;
-!- 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; Peripheral membrane protein. Host cytoplasm,
host perinuclear region. Host mitochondrion. 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 two highly variable regions called
hypervariable region 1 and 2 (HVR1 and HVR2). E2 also contain two
segments involved in CD81-binding. HVR1 is implicated in the
SCARB1-mediated cell entry. HVR2 and 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 contains a variable region called interferon
sensitivity determining region (ISDR) and seems to be
intrinsically disordered and interacts with NS5B and host PKR. The
C-terminus of NS5A contains a variable region called variable
region 3 (V3). ISDR and V3 may be involved in sensitivity and/or
resistance to IFN-alpha therapy. {ECO:0000269|PubMed:9525599}.
-!- 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.
{ECO:0000269|PubMed:9525599}.
-!- 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.
-!- 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.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D90208; BAA14233.1; -; Genomic_RNA.
EMBL; D89872; BAA14035.1; -; Genomic_RNA.
EMBL; D11397; BAA20975.1; -; Genomic_RNA.
PIR; A39253; GNWVCJ.
PDB; 1DXP; X-ray; 2.40 A; A/B=1027-1213, C/D=1678-1691.
PDB; 1DY8; X-ray; 2.40 A; A/B=1027-1213, C/D=1678-1692.
PDB; 1DY9; X-ray; 2.10 A; A/B=1027-1213, C/D=1678-1692.
PDB; 1W3C; X-ray; 2.30 A; A/B=1027-1213, C/D=1678-1692.
PDB; 2K8J; NMR; -; X=781-809.
PDB; 3OYP; X-ray; 2.76 A; A/B=1027-1213, C/D=1678-1691.
PDB; 3P8N; X-ray; 1.90 A; A/B=1027-1206, C/D=1678-1691.
PDB; 3P8O; X-ray; 2.30 A; A/B=1027-1206, C/D=1678-1691.
PDB; 4A1T; X-ray; 2.05 A; A/B=1028-1206, A/B=1678-1690.
PDB; 4A1V; X-ray; 2.20 A; A/B=1028-1206, A/B=1678-1690.
PDB; 4A1X; X-ray; 1.90 A; A/B=1028-1206.
PDB; 4I31; X-ray; 1.93 A; A/B=1027-1206, C/D=1678-1691.
PDB; 4I32; X-ray; 2.30 A; A/B=1027-1206, C/D=1678-1691.
PDB; 4I33; X-ray; 1.90 A; A/B=1027-1206, C/D=1678-1691.
PDB; 4JMY; X-ray; 1.95 A; C/D=1678-1691.
PDB; 4KTC; X-ray; 2.30 A; A/C=1028-1213.
PDBsum; 1DXP; -.
PDBsum; 1DY8; -.
PDBsum; 1DY9; -.
PDBsum; 1W3C; -.
PDBsum; 2K8J; -.
PDBsum; 3OYP; -.
PDBsum; 3P8N; -.
PDBsum; 3P8O; -.
PDBsum; 4A1T; -.
PDBsum; 4A1V; -.
PDBsum; 4A1X; -.
PDBsum; 4I31; -.
PDBsum; 4I32; -.
PDBsum; 4I33; -.
PDBsum; 4JMY; -.
PDBsum; 4KTC; -.
ProteinModelPortal; P26662; -.
SMR; P26662; -.
ELM; P26662; -.
IntAct; P26662; 5.
MINT; MINT-6803641; -.
BindingDB; P26662; -.
DrugBank; DB01720; (2z)-2-(Benzoylamino)-3-[4-(2-Bromophenoxy)Phenyl]-2-Propenoic Acid.
DrugBank; DB04005; Uridine 5'-Triphosphate.
iPTMnet; P26662; -.
euHCVdb; D89872; -.
euHCVdb; D90208; -.
OrthoDB; VOG0900004E; -.
EvolutionaryTrace; P26662; -.
Proteomes; UP000008095; Genome.
Proteomes; UP000165187; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; 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:0032993; C:protein-DNA complex; IMP:CAFA.
GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
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:0003677; F:DNA binding; IMP:CAFA.
GO; GO:1990814; F:DNA/DNA annealing activity; IMP:CAFA.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IMP:CAFA.
GO; GO:0003724; F:RNA helicase activity; IDA:CACAO.
GO; GO:0033592; F:RNA strand annealing activity; IMP:CAFA.
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: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:0043066; P:negative regulation of apoptotic process; IDA:AgBase.
GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IDA:AgBase.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IDA:AgBase.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0043489; P:RNA stabilization; IMP:CAFA.
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.
CDD; cd00079; HELICc; 1.
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_NS3.
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.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51693; HCV_NS2_PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activation of host autophagy by virus;
Apoptosis; ATP-binding; Capsid protein;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane;
G1/S host cell cycle checkpoint dysregulation by virus; Glycoprotein;
Helicase; Host cell membrane; Host cytoplasm;
Host endoplasmic reticulum; Host lipid droplet; Host membrane;
Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host TRAFs by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Lipoprotein; Membrane; Metal-binding;
Modulation of host cell cycle by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Oncogene; Palmitate;
Phosphoprotein; Protease; Ribonucleoprotein; RNA-binding;
RNA-directed RNA polymerase; Secreted; Serine protease;
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_0000037637.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000037638.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000037639.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000037640.
CHAIN 384 746 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000037641.
CHAIN 747 809 p7. {ECO:0000250}.
/FTId=PRO_0000037642.
CHAIN 810 1026 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000037643.
CHAIN 1027 1657 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000037644.
CHAIN 1658 1711 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000037645.
CHAIN 1712 1972 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000037646.
CHAIN 1973 2419 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000037647.
CHAIN 2420 3010 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000037648.
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 380 725 Lumenal. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 757 Lumenal. {ECO:0000255}.
TRANSMEM 758 778 Helical. {ECO:0000255}.
TOPO_DOM 779 782 Cytoplasmic. {ECO:0000255}.
TRANSMEM 783 803 Helical. {ECO:0000255}.
TOPO_DOM 804 813 Lumenal. {ECO:0000255}.
TRANSMEM 814 834 Helical. {ECO:0000255}.
TOPO_DOM 835 881 Cytoplasmic. {ECO:0000255}.
TRANSMEM 882 902 Helical. {ECO:0000255}.
TOPO_DOM 903 928 Lumenal. {ECO:0000255}.
TRANSMEM 929 949 Helical. {ECO:0000255}.
TOPO_DOM 950 1657 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1658 1678 Helical. {ECO:0000255}.
TOPO_DOM 1679 1805 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1806 1826 Helical. {ECO:0000255}.
TOPO_DOM 1827 1828 Lumenal. {ECO:0000255}.
TRANSMEM 1829 1849 Helical. {ECO:0000255}.
TOPO_DOM 1850 1850 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1851 1871 Helical. {ECO:0000255}.
TOPO_DOM 1872 1881 Lumenal. {ECO:0000255}.
TRANSMEM 1882 1902 Helical. {ECO:0000255}.
TOPO_DOM 1903 1972 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1973 2002 {ECO:0000250}.
TOPO_DOM 2003 2989 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2990 3010 Helical. {ECO:0000250}.
DOMAIN 903 1026 Peptidase C18. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
DOMAIN 1027 1208 Peptidase S29. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
DOMAIN 1217 1369 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 2633 2751 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1230 1237 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 59 Interaction with DDX3X. {ECO:0000250}.
REGION 2 23 Interaction with STAT1.
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 475 481 HVR2. {ECO:0000250}.
REGION 482 494 CD81-binding 1. {ECO:0000255}.
REGION 522 553 CD81-binding 2. {ECO:0000255}.
REGION 660 671 PKR/eIF2-alpha phosphorylation homology
domain (PePHD).
REGION 1679 1690 NS3-binding (by NS4A). {ECO:0000255}.
REGION 2120 2332 Transcriptional activation.
{ECO:0000255}.
REGION 2120 2208 FKBP8-binding. {ECO:0000255}.
REGION 2200 2250 Basal phosphorylation.
REGION 2210 2275 PKR-binding. {ECO:0000255}.
REGION 2210 2249 ISDR. {ECO:0000250}.
REGION 2249 2306 NS4B-binding. {ECO:0000255}.
REGION 2351 2419 Basal phosphorylation.
REGION 2354 2377 V3. {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 1316 1319 DECH box.
MOTIF 2322 2325 SH3-binding. {ECO:0000255}.
MOTIF 2327 2335 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 796 803 Poly-Leu.
COMPBIAS 1432 1435 Poly-Val.
COMPBIAS 2282 2327 Pro-rich.
COMPBIAS 2993 2998 Poly-Leu.
ACT_SITE 952 952 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 972 972 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 993 993 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
ACT_SITE 1083 1083 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1107 1107 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
ACT_SITE 1165 1165 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1123 1123 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1125 1125 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1171 1171 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 1175 1175 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01166}.
METAL 2011 2011 Zinc. {ECO:0000250}.
METAL 2029 2029 Zinc. {ECO:0000250}.
METAL 2031 2031 Zinc. {ECO:0000250}.
METAL 2052 2052 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 746 747 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 809 810 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 1026 1027 Cleavage; by protease NS2-3.
{ECO:0000255|PROSITE-ProRule:PRU01030}.
SITE 1657 1658 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1711 1712 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 1972 1973 Cleavage; by serine protease NS3.
{ECO:0000255}.
SITE 2419 2420 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 2194 2194 Phosphoserine; by host; in p56.
{ECO:0000269|PubMed:7999043}.
MOD_RES 2197 2197 Phosphoserine; by host; in p58.
{ECO:0000269|PubMed:7999043}.
MOD_RES 2201 2201 Phosphoserine; by host; in p58.
{ECO:0000269|PubMed:7999043}.
MOD_RES 2204 2204 Phosphoserine; by host; in p58.
{ECO:0000269|PubMed:7999043}.
LIPID 1968 1968 S-palmitoyl cysteine; by host.
{ECO:0000250}.
LIPID 1972 1972 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 532 532 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 576 576 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 2114 2162 {ECO:0000250}.
VARIANT 464 464 E -> K.
VARIANT 475 479 DMPES -> VVPNI.
VARIANT 492 492 R -> Q.
VARIANT 522 524 FGA -> SGV.
VARIANT 538 540 LLS -> VLN.
VARIANT 580 580 V -> I.
VARIANT 608 608 M -> L.
VARIANT 622 622 V -> I.
VARIANT 626 626 V -> I.
VARIANT 674 674 I -> V.
VARIANT 694 694 R -> Q.
VARIANT 705 705 I -> V.
VARIANT 708 708 A -> V.
VARIANT 712 713 FA -> VV.
VARIANT 719 719 I -> V.
VARIANT 906 906 I -> M.
VARIANT 983 983 L -> I.
VARIANT 1140 1140 V -> I.
VARIANT 1158 1158 I -> V.
VARIANT 1252 1252 L -> R.
VARIANT 1297 1297 C -> G.
VARIANT 1323 1323 S -> W.
VARIANT 1477 1477 L -> V.
VARIANT 1485 1485 A -> S.
VARIANT 1536 1536 S -> T.
VARIANT 1583 1583 L -> F.
VARIANT 1635 1635 V -> I.
VARIANT 1644 1645 YI -> FV.
VARIANT 1695 1695 I -> V.
VARIANT 1703 1703 Q -> R.
VARIANT 1710 1710 E -> A.
VARIANT 1713 1713 S -> P.
VARIANT 1753 1753 K -> R.
VARIANT 1759 1759 V -> A.
VARIANT 1839 1839 V -> I.
VARIANT 1873 1873 M -> A.
VARIANT 1876 1876 T -> A.
VARIANT 1896 1896 V -> I.
VARIANT 1978 1978 K -> R.
VARIANT 1989 1989 S -> T.
VARIANT 2002 2002 R -> K.
VARIANT 2006 2006 L -> V.
VARIANT 2009 2009 L -> F.
VARIANT 2093 2093 V -> I.
VARIANT 2125 2125 V -> L.
VARIANT 2136 2138 VCK -> ACR.
VARIANT 2143 2146 EEVV -> VDVT.
VARIANT 2190 2190 L -> P.
VARIANT 2196 2196 P -> S.
VARIANT 2199 2199 A -> G.
VARIANT 2199 2199 A -> V.
VARIANT 2200 2200 S -> T.
VARIANT 2204 2204 S -> R.
VARIANT 2205 2205 Q -> H.
VARIANT 2208 2208 A -> T.
VARIANT 2209 2209 P -> H.
VARIANT 2209 2209 P -> L.
VARIANT 2209 2209 P -> S.
VARIANT 2210 2210 S -> P.
VARIANT 2211 2211 L -> S.
VARIANT 2212 2212 K -> E.
VARIANT 2212 2212 K -> R.
VARIANT 2214 2214 T -> A.
VARIANT 2215 2215 C -> Y.
VARIANT 2216 2216 T -> I.
VARIANT 2217 2217 T -> A.
VARIANT 2218 2218 H -> A.
VARIANT 2218 2218 H -> L.
VARIANT 2218 2218 H -> Q.
VARIANT 2218 2218 H -> R.
VARIANT 2218 2218 H -> T.
VARIANT 2219 2219 H -> R.
VARIANT 2219 2219 H -> Y.
VARIANT 2220 2220 D -> G.
VARIANT 2222 2222 P -> L.
VARIANT 2222 2222 P -> S.
VARIANT 2223 2223 D -> G.
VARIANT 2224 2224 A -> V.
VARIANT 2225 2225 D -> G.
VARIANT 2225 2225 D -> N.
VARIANT 2227 2227 I -> V.
VARIANT 2228 2228 E -> A.
VARIANT 2228 2228 E -> D.
VARIANT 2228 2228 E -> G.
VARIANT 2228 2228 E -> K.
VARIANT 2230 2230 N -> D.
VARIANT 2230 2230 N -> S.
VARIANT 2233 2233 W -> R.
VARIANT 2259 2259 I -> L.
VARIANT 2262 2262 V -> E.
VARIANT 2268 2268 I -> V.
VARIANT 2271 2271 P -> A.
VARIANT 2278 2279 PR -> SK.
VARIANT 2303 2303 D -> S.
VARIANT 2310 2310 V -> A.
VARIANT 2318 2321 STKA -> PTTG.
VARIANT 2329 2329 R -> K.
VARIANT 2367 2367 G -> A.
VARIANT 2372 2372 A -> T.
VARIANT 2379 2379 G -> E.
VARIANT 2382 2382 V -> I.
VARIANT 2414 2416 EDV -> DDI.
VARIANT 2673 2673 R -> K.
VARIANT 2681 2681 V -> I.
VARIANT 2754 2754 A -> S.
VARIANT 2757 2757 A -> V.
VARIANT 2950 2950 K -> R.
MUTAGEN 139 139 L->A: Complete loss of core protein
processing by host signal peptidase, no
effect on the cleavage at core-E1
junction; when associated with A-140 and
A-144. {ECO:0000269|PubMed:15163730}.
MUTAGEN 140 140 V->A: Complete loss of core protein
processing by host signal peptidase, no
effect on the cleavage at core-E1
junction; when associated with A-139 and
A-144. {ECO:0000269|PubMed:15163730}.
MUTAGEN 144 144 L->A: Complete loss of core protein
processing by host signal peptidase, no
effect on the cleavage at core-E1
junction; when associated with A-139 and
A-140. {ECO:0000269|PubMed:15163730}.
MUTAGEN 176 176 I->A: Complete loss of core protein
processing by host signal peptidase; when
associated with L-177.
{ECO:0000269|PubMed:15163730}.
MUTAGEN 177 177 F->L: Complete loss of core protein
processing by host signal peptidase; when
associated with A-176.
{ECO:0000269|PubMed:15163730}.
MUTAGEN 178 178 L->V: No effect on processing of the core
protein; when associated with V-179.
{ECO:0000269|PubMed:15163730}.
MUTAGEN 179 179 L->V: No effect on processing of the core
protein; when associated with V-178.
{ECO:0000269|PubMed:15163730}.
MUTAGEN 181 181 L->V: No effect on processing of the core
protein. {ECO:0000269|PubMed:15163730}.
MUTAGEN 182 182 L->V: No effect on processing of the core
protein. {ECO:0000269|PubMed:15163730}.
MUTAGEN 183 183 S->L: No effect on processing of the core
protein; when associated with A-184 or V-
184. {ECO:0000269|PubMed:15163730}.
MUTAGEN 184 184 C->A,V: No effect on processing of the
core protein; when associated with L-183.
{ECO:0000269|PubMed:15163730}.
MUTAGEN 922 922 C->A: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 932 932 H->A: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 952 952 H->A,R: Complete loss of protease NS2-3
activity. {ECO:0000269|PubMed:8392606}.
MUTAGEN 972 972 E->Q: Reduced protease NS2-3 activity.
{ECO:0000269|PubMed:8392606}.
MUTAGEN 980 980 E->Q: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 993 993 C->A: Complete loss of protease NS2-3
activity. {ECO:0000269|PubMed:8392606}.
MUTAGEN 1009 1009 E->Q: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 1042 1042 C->A: No effect on zinc-binding by serine
protease NS3.
{ECO:0000269|PubMed:9060645}.
MUTAGEN 1058 1058 E->Q: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 1073 1073 C->S: No effect on zinc-binding by serine
protease NS3.
{ECO:0000269|PubMed:9060645}.
MUTAGEN 1078 1078 C->L: No effect on zinc-binding by serine
protease NS3.
{ECO:0000269|PubMed:9060645}.
MUTAGEN 1083 1083 H->A: Complete loss of serine protease
NS3 activity. No effect on zinc-binding
by serine protease NS3.
{ECO:0000269|PubMed:8389908,
ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1107 1107 D->A: Complete loss of serine protease
NS3 activity.
{ECO:0000269|PubMed:8389908,
ECO:0000269|PubMed:8392606}.
MUTAGEN 1123 1123 C->A: Reduced protease NS2-3 and serine
protease NS3 activities.
{ECO:0000269|PubMed:8392606}.
MUTAGEN 1125 1125 C->A: Reduced protease NS2-3 and serine
protease NS3 activities.
{ECO:0000269|PubMed:8392606}.
MUTAGEN 1136 1136 H->A: No effect on polyprotein
processing. No effect on zinc-binding by
serine protease NS3.
{ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1165 1165 S->A: Complete loss of serine protease
NS3 activity. No effect on zinc-binding
by serine protease NS3.
{ECO:0000269|PubMed:8389908,
ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1171 1171 C->A: Reduced protease NS2-3 and serine
protease NS3 activities.
{ECO:0000269|PubMed:8392606}.
MUTAGEN 1175 1175 H->A: No effect on polyprotein
processing. Reduces zinc-binding by
serine protease NS3.
{ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1185 1185 C->A: No effect on polyprotein
processing. No effect on zinc-binding by
serine protease NS3.
{ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1199 1199 E->Q: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 1202 1202 E->Q: No effect on polyprotein
processing. {ECO:0000269|PubMed:8392606}.
MUTAGEN 1227 1227 H->A: No effect on polyprotein
processing. No effect on zinc-binding by
serine protease NS3.
{ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 1229 1229 H->A: No effect on polyprotein
processing. No effect on zinc-binding by
serine protease NS3.
{ECO:0000269|PubMed:8392606,
ECO:0000269|PubMed:9060645}.
MUTAGEN 2194 2194 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2197 2197 S->A: Loss of NS5A hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2200 2200 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2201 2201 S->A: Loss of NS5A hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2202 2202 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2204 2204 S->A: Loss of NS5A hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2207 2207 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2210 2210 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
MUTAGEN 2221 2221 S->A: No effect on NS5A
hyperphosphorylation.
{ECO:0000269|PubMed:7769656}.
HELIX 786 801 {ECO:0000244|PDB:2K8J}.
STRAND 1030 1035 {ECO:0000244|PDB:3P8N}.
HELIX 1039 1048 {ECO:0000244|PDB:3P8N}.
STRAND 1057 1063 {ECO:0000244|PDB:3P8N}.
STRAND 1068 1074 {ECO:0000244|PDB:3P8N}.
STRAND 1077 1080 {ECO:0000244|PDB:3P8N}.
HELIX 1082 1085 {ECO:0000244|PDB:3P8N}.
STRAND 1090 1092 {ECO:0000244|PDB:3P8N}.
STRAND 1095 1097 {ECO:0000244|PDB:3P8N}.
STRAND 1100 1103 {ECO:0000244|PDB:3P8N}.
TURN 1104 1107 {ECO:0000244|PDB:3P8N}.
STRAND 1108 1112 {ECO:0000244|PDB:3P8N}.
STRAND 1128 1133 {ECO:0000244|PDB:3P8N}.
STRAND 1139 1144 {ECO:0000244|PDB:3P8N}.
STRAND 1146 1157 {ECO:0000244|PDB:3P8N}.
HELIX 1158 1161 {ECO:0000244|PDB:3P8N}.
STRAND 1168 1170 {ECO:0000244|PDB:3P8N}.
STRAND 1176 1186 {ECO:0000244|PDB:3P8N}.
STRAND 1189 1197 {ECO:0000244|PDB:3P8N}.
HELIX 1198 1206 {ECO:0000244|PDB:3P8N}.
STRAND 1680 1689 {ECO:0000244|PDB:3P8N}.
SEQUENCE 3010 AA; 327021 MW; AA993794F46DB185 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG MGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTIPAS AYEVRNVSGI YHVTNDCSNS SIVYEAADMI MHTPGCVPCV RESNFSRCWV
ALTPTLAARN SSIPTTTIRR HVDLLVGAAA LCSAMYVGDL CGSVFLVSQL FTFSPRRYET
VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG AHWGVLAGLA
YYSMVGNWAK VLIVMLLFAG VDGHTHVTGG RVASSTQSLV SWLSQGPSQK IQLVNTNGSW
HINRTALNCN DSLQTGFIAA LFYAHRFNAS GCPERMASCR PIDEFAQGWG PITHDMPESS
DQRPYCWHYA PRPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGAPTYSWG ENETDVLLLS
NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLV CPTDCFRKHP EATYTKCGSG
PWLTPRCMVD YPYRLWHYPC TVNFTVFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS
ELSPLLLSTT EWQILPCSFT TLPALSTGLI HLHRNIVDVQ YLYGIGSAVV SFAIKWEYIL
LLFLLLADAR VCACLWMMLL IAQAEATLEN LVVLNAASVA GAHGLLSFLV FFCAAWYIKG
RLVPGAAYAL YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA
RLIWWLQYFI TRAEAHLQVW VPPLNVRGGR DAIILLTCAV HPELIFDITK LLLAILGPLM
VLQAGITRVP YFVRAQGLIR ACMLVRKVAG GHYVQMAFMK LAALTGTYVY DHLTPLRDWA
HAGLRDLAVA VEPVVFSDME TKLITWGADT AACGDIISGL PVSARRGKEI LLGPADSFGE
QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVDGEVQ VLSTATQSFL ATCVNGVCWT
VYHGAGSKTL AGPKGPITQM YTNVDQDLVG WPAPPGARSM TPCTCGSSDL YLVTRHADVV
PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPSGHVVGIF RAAVCTRGVA KAVDFIPVES
METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGIEPNIRT GVRTITTGGP ITYSTYCKFL ADGGCSGGAY DIIICDECHS
TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSITVPHP NIEEVALSNT GEIPFYGKAI
PIEAIKGGRH LIFCHSKKKC DELAAKLTGL GLNAVAYYRG LDVSVIPTSG DVVVVATDAL
MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRAQRRGR TGRGRSGIYR
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
VFTGLTHIDA HFLSQTKQAG DNLPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEVTLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
VIVGRIILSG RPAVIPDREV LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT
KQAEAAAPVV ESKWRALEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
LTTQNTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLKDV
WDWICTVLSD FKTWLQSKLL PRLPGLPFLS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK
NGSMRIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPVCKPL LREEVVFQVG LNQYLVGSQL
PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTHHD
SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFDPIR AVEDEREISV PAEILRKPRK
FPPALPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPSTK APPIPPPRRK RTVVLTESTV
SSALAELATK TFGSSGSSAV DSGTATGPPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
SDGSWSTVSG EAGEDVVCCS MSYTWTGALI TPCAAEESKL PINPLSNSLL RHHSMVYSTT
SRSASLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAR LLSIEEACKL TPPHSAKSKF
GYGAKDVRSL SSRAVNHIRS VWEDLLEDTE TPIDTTIMAK NEVFCVQPEK GGRKPARLIV
FPDLGVRVCE KMALYDVVST LPQAVMGPSY GFQYSPGQRV EFLVNTWKSK KCPMGFSYDT
RCFDSTVTEN DIRTEESIYQ CCDLAPEARQ AIRSLTERLY VGGPLTNSKG QNCGYRRCRA
SGVLTTSCGN TLTCYLKATA ACRAAKLQDC TMLVNGDDLV VICESAGTQE DAAALRAFTE
AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETVR
HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ
IIERLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRAKL LSQGGRAATC
GKYLFNWAVK TKLKLTPIPA ASQLDLSGWF VAGYNGGDIY HSLSRARPRW FMLCLLLLSV
GVGIYLLPNR


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