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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_HCVBK              Reviewed;        3010 AA.
P26663;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 196.
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 BK) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=11105;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1847440;
Takamizawa A., Mori C., Fuke I., Manabe S., Murakami S., Fujita J.,
Onishi E., Andoh T., Yoshida I., Okayama H.;
"Structure and organization of the hepatitis C virus genome isolated
from human carriers.";
J. Virol. 65:1105-1113(1991).
[2]
PROTEIN SEQUENCE OF 1487-1500.
PubMed=8647104; DOI=10.1111/j.1432-1033.1996.0611p.x;
Borowski P., Heiland M., Oehlmann K., Becker B., Korneteky L.;
"Non-structural protein 3 of hepatitis C virus inhibits
phosphorylation mediated by cAMP-dependent protein kinase.";
Eur. J. Biochem. 237:611-618(1996).
[3]
SUBCELLULAR LOCATION, AND RNA-BINDING ACTIVITY OF CORE PROTEIN.
PubMed=8189501;
Santolini E., Migliaccio G., La Monica N.;
"Biosynthesis and biochemical properties of the hepatitis C virus core
protein.";
J. Virol. 68:3631-3641(1994).
[4]
CHARACTERIZATION OF PROTEASE NS2-3.
PubMed=9261354;
Pieroni L., Santolini E., Fipaldini C., Pacini L., Migliaccio G.,
La Monica N.;
"In vitro study of the NS2-3 protease of hepatitis C virus.";
J. Virol. 71:6373-6380(1997).
[5]
FUNCTION OF NS5A.
PubMed=9710605; DOI=10.1128/MCB.18.9.5208;
Gale M.J. Jr., Blakely C.M., Kwieciszewski B., Tan S.-L., Dossett M.,
Tang N.M., Korth M.J., Polyak S.J., Gretch D.R., Katze M.G.;
"Control of PKR protein kinase by hepatitis C virus nonstructural 5A
protein: molecular mechanisms of kinase regulation.";
Mol. Cell. Biol. 18:5208-5218(1998).
[6]
INTERACTION OF NS5A WITH HUMAN GRB2, AND MUTAGENESIS OF PRO-2322;
PRO-2323 AND PRO-2326.
PubMed=10318918; DOI=10.1073/pnas.96.10.5533;
Tan S.-L., Nakao H., He Y., Vijaysri S., Neddermann P., Jacobs B.L.,
Mayer B.J., Katze M.G.;
"NS5A, a nonstructural protein of hepatitis C virus, binds growth
factor receptor-bound protein 2 adaptor protein in a Src homology 3
domain/ligand-dependent manner and perturbs mitogenic signaling.";
Proc. Natl. Acad. Sci. U.S.A. 96:5533-5538(1999).
[7]
MUTAGENESIS OF SER-2194.
PubMed=11118372; DOI=10.1006/viro.2000.0662;
Katze M.G., Kwieciszewski B., Goodlett D.R., Blakely C.M.,
Neddermann P., Tan S.-L., Aebersold R.;
"Ser(2194) is a highly conserved major phosphorylation site of the
hepatitis C virus nonstructural protein NS5A.";
Virology 278:501-513(2000).
[8]
CHARACTERIZATION OF PROTEASE NS2-3.
PubMed=11591719; DOI=10.1074/jbc.M108266200;
Thibeault D., Maurice R., Pilote L., Lamarre D., Pause A.;
"In vitro characterization of a purified NS2/3 protease variant of
hepatitis C virus.";
J. Biol. Chem. 276:46678-46684(2001).
[9]
INTERACTION OF NS5A WITH HUMAN PIK3R1.
PubMed=12186904; DOI=10.1128/JVI.76.18.9207-9217.2002;
He Y., Nakao H., Tan S.-L., Polyak S.J., Neddermann P., Vijaysri S.,
Jacobs B.L., Katze M.G.;
"Subversion of cell signaling pathways by hepatitis C virus
nonstructural 5A protein via interaction with Grb2 and P85
phosphatidylinositol 3-kinase.";
J. Virol. 76:9207-9217(2002).
[10]
DOMAINS CD81-BINDING AND HVR2.
PubMed=12660945; DOI=10.1086/368221;
Hofmann W.P., Sarrazin C., Kronenberger B., Schonberger B., Bruch K.,
Zeuzem S.;
"Mutations within the CD81-binding sites and hypervariable region 2 of
the envelope 2 protein: correlation with treatment response in
hepatitis C virus-infected patients.";
J. Infect. Dis. 187:982-987(2003).
[11]
PHOSPHORYLATION OF NS5A.
PubMed=15016873; DOI=10.1128/JVI.78.7.3502-3513.2004;
Coito C., Diamond D.L., Neddermann P., Korth M.J., Katze M.G.;
"High-throughput screening of the yeast kinome: identification of
human serine/threonine protein kinases that phosphorylate the
hepatitis C virus NS5A protein.";
J. Virol. 78:3502-3513(2004).
[12]
DOMAINS ISDR AND V3 REGIONS.
PubMed=15258967; DOI=10.1002/jmv.20144;
Vuillermoz I., Khattab E., Sablon E., Ottevaere I., Durantel D.,
Vieux C., Trepo C., Zoulim F.;
"Genetic variability of hepatitis C virus in chronically infected
patients with viral breakthrough during interferon-ribavirin
therapy.";
J. Med. Virol. 74:41-53(2004).
[13]
INTERACTION OF NS5A WITH CELLULAR PROTEINS.
PubMed=15607035; DOI=10.5483/BMBRep.2004.37.6.741;
Ahn J., Chung K.-S., Kim D.-U., Won M., Kim L., Kim K.-S., Nam M.,
Choi S.-J., Kim H.-C., Yoon M., Chae S.-K., Hoe K.-L.;
"Systematic identification of hepatocellular proteins interacting with
NS5A of the hepatitis C virus.";
J. Biochem. Mol. Biol. 37:741-748(2004).
[14]
INTERACTION OF NS5A WITH HUMAN BIN1, AND FUNCTION OF NS5A.
PubMed=16530520; DOI=10.1053/j.gastro.2005.12.030;
Nanda S.K., Herion D., Liang T.J.;
"The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is
important for apoptosis and infectivity.";
Gastroenterology 130:794-809(2006).
[15]
SUBCELLULAR LOCATION OF CORE PROTEIN, AND FUNCTION OF CORE PROTEIN.
PubMed=17188392; DOI=10.1016/j.jhep.2006.10.019;
Jackel-Cram C., Babiuk L.A., Liu Q.;
"Up-regulation of fatty acid synthase promoter by hepatitis C virus
core protein: genotype-3a core has a stronger effect than genotype-1b
core.";
J. Hepatol. 46:999-1008(2007).
[16]
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).
[17]
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).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1027-1215.
PubMed=8861916; DOI=10.1016/S0092-8674(00)81350-1;
Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N.,
Moomaw E.W., Adachi T., Hostomska Z.;
"The crystal structure of hepatitis C virus NS3 proteinase reveals a
trypsin-like fold and a structural zinc binding site.";
Cell 87:331-342(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1027-1206 AND 1678-1691.
PubMed=9568891; DOI=10.1002/pro.5560070402;
Yan Y., Li Y., Munshi S., Sardana V., Cole J.L., Sardana M.,
Steinkuehler C., Tomei L., de Francesco R., Kuo L.C., Chen Z.;
"Complex of NS3 protease and NS4A peptide of BK strain hepatitis C
virus: a 2.2-A resolution structure in a hexagonal crystal form.";
Protein Sci. 7:837-847(1998).
[21]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1216-1650.
PubMed=9614113; DOI=10.1074/jbc.273.24.15045;
Cho H.-S., Ha N.-C., Kang L.-W., Chung K.M., Back S.H., Jang S.K.,
Oh B.-H.;
"Crystal structure of RNA helicase from genotype 1b hepatitis C virus.
A feasible mechanism of unwinding duplex RNA.";
J. Biol. Chem. 273:15045-15052(1998).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1013-1657.
PubMed=10574797; DOI=10.1016/S0969-2126(00)80025-8;
Yao N., Reichert P., Taremi S.S., Prosise W.W., Weber P.C.;
"Molecular views of viral polyprotein processing revealed by the
crystal structure of the hepatitis C virus bifunctional protease-
helicase.";
Structure 7:1353-1363(1999).
[23]
STRUCTURE BY NMR OF 1027-1206.
PubMed=10366511; DOI=10.1006/jmbi.1999.2745;
Barbato G., Cicero D.O., Nardi M.C., Steinkuehler C., Cortese R.,
De Francesco R., Bazzo R.;
"The solution structure of the N-terminal proteinase domain of the
hepatitis C virus (HCV) NS3 protein provides new insights into its
activation and catalytic mechanism.";
J. Mol. Biol. 289:371-384(1999).
[24]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2420-2950.
PubMed=10557268; DOI=10.1073/pnas.96.23.13034;
Bressanelli S., Tomei L., Roussel A., Incitti I., Vitale R.L.,
Mathieu M., De Francesco R., Rey F.A.;
"Crystal structure of the RNA-dependent RNA polymerase of hepatitis C
virus.";
Proc. Natl. Acad. Sci. U.S.A. 96:13034-13039(1999).
[25]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2414-2989.
PubMed=10504728; DOI=10.1038/13305;
Lesburg C.A., Cable M.B., Ferrari E., Hong Z., Mannarino A.F.,
Weber P.C.;
"Crystal structure of the RNA-dependent RNA polymerase from hepatitis
C virus reveals a fully encircled active site.";
Nat. Struct. Biol. 6:937-943(1999).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2420-2999.
PubMed=10574802; DOI=10.1016/S0969-2126(00)80031-3;
Ago H., Adachi T., Yoshida A., Yamamoto M., Habuka N., Yatsunami K.,
Miyano M.;
"Crystal structure of the RNA-dependent RNA polymerase of hepatitis C
virus.";
Structure 7:1417-1426(1999).
[27]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2420-2955.
PubMed=11884572; DOI=10.1128/JVI.76.7.3482-3492.2002;
Bressanelli S., Tomei L., Rey F.A., De Francesco R.;
"Structural analysis of the hepatitis C virus RNA polymerase in
complex with ribonucleotides.";
J. Virol. 76:3482-3492(2002).
[28]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2420-2989 IN COMPLEX WITH A
NON-NUCLEOSIDE INHIBITOR.
PubMed=12509436; DOI=10.1074/jbc.M209397200;
Wang M., Ng K.K.-S., Cherney M.M., Chan L., Yannopoulos C.G.,
Bedard J., Morin N., Nguyen-Ba N., Alaoui-Ismaili M.H., Bethell R.C.,
James M.N.G.;
"Non-nucleoside analogue inhibitors bind to an allosteric site on HCV
NS5B polymerase. Crystal structures and mechanism of inhibition.";
J. Biol. Chem. 278:9489-9495(2003).
[29]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2420-2995 IN COMPLEX WITH AN
INHIBITOR.
PubMed=12805457; DOI=10.1128/JVI.77.13.7575-7581.2003;
Love R.A., Parge H.E., Yu X., Hickey M.J., Diehl W., Gao J.,
Wriggers H., Ekker A., Wang L., Thomson J.A., Dragovich P.S.,
Fuhrman S.A.;
"Crystallographic identification of a noncompetitive inhibitor binding
site on the hepatitis C virus NS5B RNA polymerase enzyme.";
J. Virol. 77:7575-7581(2003).
-!- FUNCTION: Core protein packages viral RNA to form a viral
nucleocapsid, and promotes virion budding. Modulates viral
translation initiation by interacting with HCV IRES and 40S
ribosomal subunit. Also regulates many host cellular functions
such as signaling pathways and apoptosis. Prevents the
establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling
pathways and by inducing human STAT1 degradation. Thought to play
a role in virus-mediated cell transformation leading to
hepatocellular carcinomas. Interacts with, and activates STAT3
leading to cellular transformation. May repress the promoter of
p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the
cytoplasm. Also represses cell cycle negative regulating factor
CDKN1A, thereby interrupting an important check point of normal
cell cycle regulation. Targets transcription factors involved in
the regulation of inflammatory responses and in the immune
response: suppresses NK-kappaB activation, and activates AP-1.
Could mediate apoptotic pathways through association with TNF-type
receptors TNFRSF1A and LTBR, although its effect on death
receptor-induced apoptosis remains controversial. Enhances TRAIL
mediated apoptosis, suggesting that it might play a role in
immune-mediated liver cell injury. Seric core protein is able to
bind C1QR1 at the T-cell surface, resulting in down-regulation of
T-lymphocytes proliferation. May transactivate human MYC, Rous
sarcoma virus LTR, and SV40 promoters. May suppress the human FOS
and HIV-1 LTR activity. Alters lipid metabolism by interacting
with hepatocellular proteins involved in lipid accumulation and
storage. Core protein induces up-regulation of FAS promoter
activity, and thereby probably contributes to the increased
triglyceride accumulation in hepatocytes (steatosis) (By
similarity). {ECO:0000250}.
-!- FUNCTION: E1 and E2 glycoproteins form a heterodimer that is
involved in virus attachment to the host cell, virion
internalization through clathrin-dependent endocytosis and fusion
with host membrane. E1/E2 heterodimer binds to human LDLR, CD81
and SCARB1/SR-BI receptors, but this binding is not sufficient for
infection, some additional liver specific cofactors may be needed.
The fusion function may possibly be carried by E1. E2 inhibits
human EIF2AK2/PKR activation, preventing the establishment of an
antiviral state. E2 is a viral ligand for CD209/DC-SIGN and
CLEC4M/DC-SIGNR, which are respectively found on dendritic cells
(DCs), and on liver sinusoidal endothelial cells and macrophage-
like cells of lymph node sinuses. These interactions allow capture
of circulating HCV particles by these cells and subsequent
transmission to permissive cells. DCs act as sentinels in various
tissues where they entrap pathogens and convey them to local
lymphoid tissue or lymph node for establishment of immunity.
Capture of circulating HCV particles by these SIGN+ cells may
facilitate virus infection of proximal hepatocytes and lymphocyte
subpopulations and may be essential for the establishment of
persistent infection (By similarity). {ECO:0000250}.
-!- FUNCTION: P7 seems to be a heptameric ion channel protein
(viroporin) and is inhibited by the antiviral drug amantadine.
Also inhibited by long-alkyl-chain iminosugar derivatives.
Essential for infectivity (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease NS2-3 is a cysteine protease responsible for
the autocatalytic cleavage of NS2-NS3. Seems to undergo self-
inactivation following maturation (By similarity). {ECO:0000250}.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase. NS3 serine protease, in
association with NS4A, is responsible for the cleavages of NS3-
NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also
prevents phosphorylation of human IRF3, thus preventing the
establishment of dsRNA induced antiviral state. NS3 RNA helicase
binds to RNA and unwinds dsRNA in the 3' to 5' direction, and
likely RNA stable secondary structure in the template strand.
Cleaves and inhibits the host antiviral protein MAVS (By
similarity). {ECO:0000250}.
-!- FUNCTION: NS4B induces a specific membrane alteration that serves
as a scaffold for the virus replication complex. This membrane
alteration gives rise to the so-called ER-derived membranous web
that contains the replication complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: NS5A is a component of the replication complex involved
in RNA-binding. Its interaction with Human VAPB may target the
viral replication complex to vesicles. Down-regulates viral IRES
translation initiation. Mediates interferon resistance, presumably
by interacting with and inhibiting human EIF2AK2/PKR. Seems to
inhibit apoptosis by interacting with BIN1 and FKBP8. The
hyperphosphorylated form of NS5A is an inhibitor of viral
replication (By similarity). {ECO:0000250}.
-!- FUNCTION: NS5B is an RNA-dependent RNA polymerase that plays an
essential role in the virus replication. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of four peptide bonds in the viral
precursor polyprotein, commonly with Asp or Glu in the P6
position, Cys or Thr in P1 and Ser or Ala in P1'.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
-!- ENZYME REGULATION: Activity of auto-protease NS2-3 is dependent on
zinc ions and completely inhibited by EDTA, 1,10-phenanthroline,
iodocetamide and N-ethylmaleimide. According to PubMed:9261354,
completely inhibited by the serine protease inhibitors TLCK and
TPCK. According to PubMed:8189501, almost completely inhibited by
TPCK and slightly inhibited by TLCK. Not inhibited by antipain,
aprotinin, E64, PMSF and pepstatin. Also inhibited by NS2-3 and
NS4A derived peptides. 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 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:
Q9WMX2:- (xeno); NbExp=5; IntAct=EBI-6874437, EBI-6863741;
P52480:Pkm (xeno); NbExp=3; IntAct=EBI-6857429, EBI-647785;
Q62245:Sos1 (xeno); NbExp=2; IntAct=EBI-6857429, EBI-1693;
P04637:TP53 (xeno); NbExp=9; IntAct=EBI-6838571, EBI-366083;
-!- SUBCELLULAR LOCATION: Core protein p21: Host endoplasmic reticulum
membrane; Single-pass membrane protein. Host mitochondrion
membrane; Single-pass type I membrane protein. Host lipid droplet.
Note=The C-terminal transmembrane domain of core protein p21
contains an ER signal leading the nascent polyprotein to the ER
membrane. Only a minor proportion of core protein is present in
the nucleus and an unknown proportion is secreted.
-!- SUBCELLULAR LOCATION: Core protein p19: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Secreted
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E1 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Note=The C-terminal
transmembrane domain acts as a signal sequence and forms a hairpin
structure before cleavage by host signal peptidase. After
cleavage, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. A reorientation of the
second hydrophobic stretch occurs after cleavage producing a
single reoriented transmembrane domain. These events explain the
final topology of the protein. ER retention of E2 is leaky and, in
overexpression conditions, only a small fraction reaches the
plasma membrane.
-!- SUBCELLULAR LOCATION: p7: Host endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
cell membrane {ECO:0000250}. Note=The C-terminus of p7 membrane
domain acts as a signal sequence. After cleavage by host signal
peptidase, the membrane sequence is retained at the C-terminus of
the protein, serving as ER membrane anchor. Only a fraction
localizes to the plasma membrane.
-!- SUBCELLULAR LOCATION: Protease NS2-3: Host endoplasmic reticulum
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=NS3 is associated to the ER membrane through
its binding to NS4A.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000305}; Single-pass type I membrane
protein {ECO:0000305}. Note=Host membrane insertion occurs after
processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5A: Host endoplasmic
reticulum membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Host cytoplasm, host perinuclear region
{ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Host
membrane insertion occurs after processing by the NS3 protease.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host
endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Note=Host membrane insertion
occurs after processing by the NS3 protease.
-!- DOMAIN: The transmembrane regions of envelope E1 and E2
glycoproteins are involved in heterodimer formation, ER
localization, and assembly of these proteins. Envelope E2
glycoprotein contain 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 (By
similarity). 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:0000250}.
-!- DOMAIN: The SH3-binding domain of NS5A is involved in the
interaction with human Bin1, GRB2 and Src-family kinases.
-!- 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.
-!- 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. {ECO:0000269|PubMed:15016873}.
-!- PTM: NS4B is palmitoylated. This modification may play a role in
its polymerization or in protein-protein interactions (By
similarity). {ECO:0000250}.
-!- PTM: The N-terminus of a fraction of NS4B molecules seems to be
relocated post-translationally from the cytoplasm to the ER lumen,
with a 5th transmembrane segment. The C-terminus of NS2 may be
lumenal with a fourth transmembrane segment (By similarity).
{ECO:0000250}.
-!- PTM: Core protein is ubiquitinated; mediated by UBE3A and leading
to core protein subsequent proteasomal degradation. {ECO:0000250}.
-!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
mutations in NS5A, reducing its inhibitory effect on replication.
{ECO:0000250}.
-!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
B virus when HCV and HBV coinfect the same cell, by suppressing
HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
{ECO:0000305}.
-!- CAUTION: The core gene probably also codes for alternative reading
frame proteins (ARFPs). Many functions depicted for the core
protein might belong to the ARFPs. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M58335; AAA72945.1; -; Genomic_RNA.
PIR; A38465; GNWVTC.
PDB; 1A1Q; X-ray; 2.40 A; A/B/C=1027-1215.
PDB; 1BT7; NMR; -; A=1027-1206.
PDB; 1C2P; X-ray; 1.90 A; A/B=2422-2989.
PDB; 1CSJ; X-ray; 2.80 A; A/B=2420-2950.
PDB; 1CU1; X-ray; 2.50 A; A/B=1029-1657.
PDB; 1GX5; X-ray; 1.70 A; A=2420-2955.
PDB; 1GX6; X-ray; 1.85 A; A=2420-2950.
PDB; 1JXP; X-ray; 2.20 A; A/B=1027-1206, C/D=1678-1691.
PDB; 1NHU; X-ray; 2.00 A; A/B=2420-2989.
PDB; 1NHV; X-ray; 2.90 A; A/B=2420-2989.
PDB; 1NS3; X-ray; 2.80 A; A/B=1029-1206, C/D=1678-1689.
PDB; 1OS5; X-ray; 2.20 A; A=2420-2989.
PDB; 1QUV; X-ray; 2.50 A; A=2420-2989.
PDB; 2AWZ; X-ray; 2.15 A; A/B=2420-2989.
PDB; 2AX0; X-ray; 2.00 A; A/B=2420-2989.
PDB; 2AX1; X-ray; 2.10 A; A/B=2420-2989.
PDB; 2BRK; X-ray; 2.30 A; A=2420-2955.
PDB; 2BRL; X-ray; 2.40 A; A=2420-2955.
PDB; 2DXS; X-ray; 2.20 A; A/B=2420-2963.
PDB; 2GIQ; X-ray; 1.65 A; A/B=2421-2981.
PDB; 2GIR; X-ray; 1.90 A; A/B=2421-2981.
PDB; 2HAI; X-ray; 1.58 A; A=2420-2988.
PDB; 2HWH; X-ray; 2.30 A; A/B=2422-2989.
PDB; 2HWI; X-ray; 2.00 A; A/B=2422-2989.
PDB; 2I1R; X-ray; 2.20 A; A/B=2422-2989.
PDB; 2JC0; X-ray; 2.20 A; A/B=2420-2989.
PDB; 2JC1; X-ray; 2.00 A; A/B=2420-2989.
PDB; 2O5D; X-ray; 2.20 A; A/B=2422-2989.
PDB; 2WCX; X-ray; 2.00 A; A=2420-2955.
PDB; 2WHO; X-ray; 2.00 A; A/B=2420-2955.
PDB; 2WRM; X-ray; 1.95 A; A=2420-2955.
PDB; 2XWY; X-ray; 2.53 A; A=2420-2955.
PDB; 2ZKU; X-ray; 1.95 A; A/B/C/D=2420-2989.
PDB; 3BR9; X-ray; 2.30 A; A/B=2420-2989.
PDB; 3BSA; X-ray; 2.30 A; A/B=2420-2989.
PDB; 3BSC; X-ray; 2.65 A; A/B=2420-2989.
PDB; 3CDE; X-ray; 2.10 A; A/B=2420-2989.
PDB; 3CIZ; X-ray; 1.87 A; A/B=2421-2989.
PDB; 3CJ0; X-ray; 1.90 A; A/B=2421-2989.
PDB; 3CJ2; X-ray; 1.75 A; A/B=2421-2989.
PDB; 3CJ3; X-ray; 1.87 A; A/B=2421-2989.
PDB; 3CJ4; X-ray; 2.07 A; A/B=2421-2989.
PDB; 3CJ5; X-ray; 1.92 A; A/B=2421-2989.
PDB; 3CO9; X-ray; 2.10 A; A/B=2420-2989.
PDB; 3CVK; X-ray; 2.31 A; A/B=2420-2989.
PDB; 3CWJ; X-ray; 2.40 A; A/B=2420-2989.
PDB; 3D28; X-ray; 2.30 A; A/B=2420-2989.
PDB; 3D5M; X-ray; 2.20 A; A/B=2420-2989.
PDB; 3E51; X-ray; 1.90 A; A/B=2420-2989.
PDB; 3FQK; X-ray; 2.20 A; A/B=2421-2989.
PDB; 3FRZ; X-ray; 1.86 A; A=2420-2989.
PDB; 3G86; X-ray; 2.20 A; A/B=2421-2989.
PDB; 3GYN; X-ray; 2.15 A; A/B=2420-2989.
PDB; 3H2L; X-ray; 1.90 A; A/B=2420-2989.
PDB; 3H59; X-ray; 2.10 A; A/B=2421-2989.
PDB; 3H5S; X-ray; 2.00 A; A/B=2421-2989.
PDB; 3H5U; X-ray; 1.95 A; A/B=2421-2989.
PDB; 3H98; X-ray; 1.90 A; A/B=2421-2989.
PDB; 3IGV; X-ray; 2.60 A; A/B=2420-2989.
PDB; 3MF5; X-ray; 2.00 A; A/B=2421-2989.
PDB; 3RVB; X-ray; 2.20 A; A=1186-1657.
PDB; 3UA7; X-ray; 1.50 A; E/F=2321-2331.
PDB; 3UDL; X-ray; 2.17 A; A/B/C/D=2420-2989.
PDB; 3VQS; X-ray; 1.90 A; A/B/C/D=2420-2989.
PDB; 4A92; X-ray; 2.73 A; A/B=1029-1657, A/B=1678-1690.
PDB; 4B6E; X-ray; 2.46 A; A/B=1029-1657.
PDB; 4B6F; X-ray; 2.89 A; A/B=1029-1657.
PDB; 4B71; X-ray; 2.50 A; A/B=1029-1657.
PDB; 4B73; X-ray; 2.50 A; A/B=1029-1657.
PDB; 4B74; X-ray; 2.18 A; A/B=1029-1657.
PDB; 4B75; X-ray; 2.53 A; A/B=1029-1655.
PDB; 4B76; X-ray; 2.14 A; A/B=1029-1657.
PDB; 4DGV; X-ray; 1.80 A; A=412-423.
PDB; 4DGY; X-ray; 1.80 A; A=412-423.
PDB; 4EO6; X-ray; 1.79 A; A/B=2422-2989.
PDB; 4EO8; X-ray; 1.80 A; A/B=2422-2989.
PDB; 4IH5; X-ray; 1.90 A; A/B=2421-2989.
PDB; 4IH6; X-ray; 2.20 A; A/B=2421-2989.
PDB; 4IH7; X-ray; 2.30 A; A/B=2421-2989.
PDB; 4K8B; X-ray; 2.80 A; C/D=1678-1689.
PDB; 4KAI; X-ray; 2.30 A; A/B=2420-2989.
PDB; 4KB7; X-ray; 1.85 A; A/B=2420-2989.
PDB; 4KBI; X-ray; 2.06 A; A/B=2420-2989.
PDB; 4KE5; X-ray; 2.11 A; A/B=2420-2989.
PDB; 4MIA; X-ray; 2.80 A; A/B=2421-2989.
PDB; 4MIB; X-ray; 2.30 A; A/B=2421-2989.
PDB; 4MK7; X-ray; 2.80 A; A/B=2421-2989.
PDB; 4MK8; X-ray; 2.09 A; A/B=2421-2989.
PDB; 4MK9; X-ray; 2.05 A; A/B=2421-2989.
PDB; 4MKA; X-ray; 2.05 A; A/B=2421-2989.
PDB; 4MKB; X-ray; 1.90 A; A/B=2421-2989.
PDB; 4TN2; X-ray; 2.70 A; A=2422-2989.
PDB; 4WXP; X-ray; 2.08 A; A=1206-1656.
PDB; 5FPS; X-ray; 2.68 A; A/B=1029-1657.
PDB; 5FPT; X-ray; 2.72 A; A/B=1029-1657.
PDB; 5FPY; X-ray; 2.52 A; A/B=1029-1657.
PDB; 5KZP; X-ray; 2.26 A; A/B/C/D=412-423.
PDB; 5W2E; X-ray; 2.80 A; A/B=2422-2989.
PDB; 8OHM; X-ray; 2.30 A; A=1216-1650.
PDBsum; 1A1Q; -.
PDBsum; 1BT7; -.
PDBsum; 1C2P; -.
PDBsum; 1CSJ; -.
PDBsum; 1CU1; -.
PDBsum; 1GX5; -.
PDBsum; 1GX6; -.
PDBsum; 1JXP; -.
PDBsum; 1NHU; -.
PDBsum; 1NHV; -.
PDBsum; 1NS3; -.
PDBsum; 1OS5; -.
PDBsum; 1QUV; -.
PDBsum; 2AWZ; -.
PDBsum; 2AX0; -.
PDBsum; 2AX1; -.
PDBsum; 2BRK; -.
PDBsum; 2BRL; -.
PDBsum; 2DXS; -.
PDBsum; 2GIQ; -.
PDBsum; 2GIR; -.
PDBsum; 2HAI; -.
PDBsum; 2HWH; -.
PDBsum; 2HWI; -.
PDBsum; 2I1R; -.
PDBsum; 2JC0; -.
PDBsum; 2JC1; -.
PDBsum; 2O5D; -.
PDBsum; 2WCX; -.
PDBsum; 2WHO; -.
PDBsum; 2WRM; -.
PDBsum; 2XWY; -.
PDBsum; 2ZKU; -.
PDBsum; 3BR9; -.
PDBsum; 3BSA; -.
PDBsum; 3BSC; -.
PDBsum; 3CDE; -.
PDBsum; 3CIZ; -.
PDBsum; 3CJ0; -.
PDBsum; 3CJ2; -.
PDBsum; 3CJ3; -.
PDBsum; 3CJ4; -.
PDBsum; 3CJ5; -.
PDBsum; 3CO9; -.
PDBsum; 3CVK; -.
PDBsum; 3CWJ; -.
PDBsum; 3D28; -.
PDBsum; 3D5M; -.
PDBsum; 3E51; -.
PDBsum; 3FQK; -.
PDBsum; 3FRZ; -.
PDBsum; 3G86; -.
PDBsum; 3GYN; -.
PDBsum; 3H2L; -.
PDBsum; 3H59; -.
PDBsum; 3H5S; -.
PDBsum; 3H5U; -.
PDBsum; 3H98; -.
PDBsum; 3IGV; -.
PDBsum; 3MF5; -.
PDBsum; 3RVB; -.
PDBsum; 3UA7; -.
PDBsum; 3UDL; -.
PDBsum; 3VQS; -.
PDBsum; 4A92; -.
PDBsum; 4B6E; -.
PDBsum; 4B6F; -.
PDBsum; 4B71; -.
PDBsum; 4B73; -.
PDBsum; 4B74; -.
PDBsum; 4B75; -.
PDBsum; 4B76; -.
PDBsum; 4DGV; -.
PDBsum; 4DGY; -.
PDBsum; 4EO6; -.
PDBsum; 4EO8; -.
PDBsum; 4IH5; -.
PDBsum; 4IH6; -.
PDBsum; 4IH7; -.
PDBsum; 4K8B; -.
PDBsum; 4KAI; -.
PDBsum; 4KB7; -.
PDBsum; 4KBI; -.
PDBsum; 4KE5; -.
PDBsum; 4MIA; -.
PDBsum; 4MIB; -.
PDBsum; 4MK7; -.
PDBsum; 4MK8; -.
PDBsum; 4MK9; -.
PDBsum; 4MKA; -.
PDBsum; 4MKB; -.
PDBsum; 4TN2; -.
PDBsum; 4WXP; -.
PDBsum; 5FPS; -.
PDBsum; 5FPT; -.
PDBsum; 5FPY; -.
PDBsum; 5KZP; -.
PDBsum; 5W2E; -.
PDBsum; 8OHM; -.
ProteinModelPortal; P26663; -.
SMR; P26663; -.
IntAct; P26663; 6.
MINT; MINT-6548567; -.
BindingDB; P26663; -.
ChEMBL; CHEMBL6040; -.
DrugBank; DB07570; 3-CYCLOHEXYL-1-(2-MORPHOLIN-4-YL-2-OXOETHYL)-2-PHENYL-1H-INDOLE-6-CARBOXYLIC ACID.
DrugBank; DB08279; 3-{ISOPROPYL[(TRANS-4-METHYLCYCLOHEXYL)CARBONYL]AMINO}-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID.
DrugBank; DB08578; 4-[(5-bromopyridin-2-yl)amino]-4-oxobutanoic acid.
DrugBank; DB08580; 4-bromo-2-{[(2R)-2-(2-chlorobenzyl)pyrrolidin-1-yl]carbonyl}aniline.
DrugBank; DB07238; 5-cyclopropyl-2-(4-fluorophenyl)-6-[(2-hydroxyethyl)(methylsulfonyl)amino]-N-methyl-1-benzofuran-3-carboxamide.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB04005; Uridine 5'-Triphosphate.
iPTMnet; P26663; -.
euHCVdb; M58335; -.
OrthoDB; VOG09000032; -.
BRENDA; 2.7.7.48; 2642.
BRENDA; 3.4.21.98; 2642.
BRENDA; 3.6.4.13; 2642.
EvolutionaryTrace; P26663; -.
Proteomes; UP000007413; 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; IMP: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; IMP: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: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:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:AgBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:AgBase.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
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.
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;
Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane;
G1/S host cell cycle checkpoint dysregulation by virus; Glycoprotein;
Helicase; Host cell membrane; Host cytoplasm;
Host endoplasmic reticulum; Host lipid droplet; Host membrane;
Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host TRAFs by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Lipoprotein; Membrane; Metal-binding;
Modulation of host cell cycle by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Oncogene; Palmitate;
Phosphoprotein; Protease; Ribonucleoprotein; RNA-binding;
RNA-directed RNA polymerase; Secreted; Serine protease; SH3-binding;
Thiol protease; Transcription; Transcription regulation; Transferase;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral ion channel; Viral nucleoprotein;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 191 Core protein p21. {ECO:0000255}.
/FTId=PRO_0000037529.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000037530.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000037531.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000037532.
CHAIN 384 746 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000037533.
CHAIN 747 809 p7. {ECO:0000250}.
/FTId=PRO_0000037534.
CHAIN 810 1026 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000037535.
CHAIN 1027 1657 Serine protease NS3.
/FTId=PRO_0000037536.
CHAIN 1658 1711 Non-structural protein 4A.
/FTId=PRO_0000037537.
CHAIN 1712 1972 Non-structural protein 4B.
/FTId=PRO_0000037538.
CHAIN 1973 2419 Non-structural protein 5A.
/FTId=PRO_0000037539.
CHAIN 2420 3010 RNA-directed RNA polymerase.
/FTId=PRO_0000037540.
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. {ECO:0000250}.
REGION 122 173 Interaction with APOA2. {ECO:0000250}.
REGION 148 236 Interaction with FKBP8.
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.
REGION 475 481 HVR2.
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. {ECO:0000250}.
REGION 2210 2275 PKR-binding. {ECO:0000255}.
REGION 2210 2249 ISDR.
REGION 2249 2306 NS4B-binding. {ECO:0000255}.
REGION 2351 2419 Basal phosphorylation. {ECO:0000250}.
REGION 2354 2377 V3.
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 2995 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:0000305|PubMed:15016873}.
MOD_RES 2197 2197 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2201 2201 Phosphoserine; by host; in p58.
{ECO:0000250}.
MOD_RES 2204 2204 Phosphoserine; by host; in p58.
{ECO:0000250}.
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 540 540 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}.
MUTAGEN 2194 2194 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:11118372}.
MUTAGEN 2322 2322 P->A: Complete loss of binding to GRB2.
{ECO:0000269|PubMed:10318918}.
MUTAGEN 2323 2323 P->A: Complete loss of binding to GRB2.
{ECO:0000269|PubMed:10318918}.
MUTAGEN 2326 2326 P->A: Complete loss of binding to GRB2.
{ECO:0000269|PubMed:10318918}.
STRAND 413 416 {ECO:0000244|PDB:4DGY}.
STRAND 419 422 {ECO:0000244|PDB:4DGY}.
STRAND 1031 1035 {ECO:0000244|PDB:4B76}.
HELIX 1039 1048 {ECO:0000244|PDB:4B76}.
STRAND 1057 1063 {ECO:0000244|PDB:4B76}.
STRAND 1068 1074 {ECO:0000244|PDB:4B76}.
STRAND 1077 1080 {ECO:0000244|PDB:4B76}.
HELIX 1082 1085 {ECO:0000244|PDB:4B76}.
STRAND 1090 1092 {ECO:0000244|PDB:1JXP}.
STRAND 1095 1097 {ECO:0000244|PDB:1JXP}.
STRAND 1100 1103 {ECO:0000244|PDB:4B76}.
TURN 1104 1107 {ECO:0000244|PDB:4B76}.
STRAND 1108 1112 {ECO:0000244|PDB:4B76}.
STRAND 1128 1133 {ECO:0000244|PDB:4B76}.
STRAND 1135 1137 {ECO:0000244|PDB:1BT7}.
STRAND 1139 1144 {ECO:0000244|PDB:4B76}.
STRAND 1146 1157 {ECO:0000244|PDB:4B76}.
HELIX 1158 1161 {ECO:0000244|PDB:4B76}.
STRAND 1168 1170 {ECO:0000244|PDB:4B76}.
TURN 1172 1174 {ECO:0000244|PDB:1JXP}.
STRAND 1176 1186 {ECO:0000244|PDB:4B76}.
STRAND 1189 1197 {ECO:0000244|PDB:4B76}.
HELIX 1198 1206 {ECO:0000244|PDB:4B76}.
STRAND 1224 1229 {ECO:0000244|PDB:4WXP}.
STRAND 1232 1235 {ECO:0000244|PDB:1CU1}.
TURN 1236 1238 {ECO:0000244|PDB:4WXP}.
HELIX 1239 1246 {ECO:0000244|PDB:4WXP}.
STRAND 1251 1256 {ECO:0000244|PDB:4WXP}.
HELIX 1258 1272 {ECO:0000244|PDB:4WXP}.
STRAND 1277 1279 {ECO:0000244|PDB:4WXP}.
STRAND 1290 1295 {ECO:0000244|PDB:4WXP}.
HELIX 1296 1301 {ECO:0000244|PDB:4WXP}.
STRAND 1307 1309 {ECO:0000244|PDB:4WXP}.
STRAND 1311 1315 {ECO:0000244|PDB:4WXP}.
TURN 1316 1319 {ECO:0000244|PDB:4WXP}.
HELIX 1323 1335 {ECO:0000244|PDB:4WXP}.
TURN 1336 1340 {ECO:0000244|PDB:4WXP}.
STRAND 1342 1350 {ECO:0000244|PDB:4WXP}.
STRAND 1362 1366 {ECO:0000244|PDB:4WXP}.
STRAND 1371 1375 {ECO:0000244|PDB:4WXP}.
STRAND 1378 1380 {ECO:0000244|PDB:4WXP}.
HELIX 1382 1384 {ECO:0000244|PDB:4WXP}.
STRAND 1386 1393 {ECO:0000244|PDB:4WXP}.
HELIX 1397 1409 {ECO:0000244|PDB:4WXP}.
STRAND 1414 1417 {ECO:0000244|PDB:4WXP}.
STRAND 1419 1421 {ECO:0000244|PDB:8OHM}.
HELIX 1423 1425 {ECO:0000244|PDB:4WXP}.
STRAND 1428 1430 {ECO:0000244|PDB:4WXP}.
STRAND 1432 1436 {ECO:0000244|PDB:4WXP}.
HELIX 1438 1441 {ECO:0000244|PDB:4WXP}.
TURN 1442 1444 {ECO:0000244|PDB:8OHM}.
STRAND 1448 1453 {ECO:0000244|PDB:4WXP}.
STRAND 1456 1463 {ECO:0000244|PDB:4WXP}.
STRAND 1467 1469 {ECO:0000244|PDB:4WXP}.
STRAND 1471 1478 {ECO:0000244|PDB:4WXP}.
HELIX 1481 1488 {ECO:0000244|PDB:4WXP}.
STRAND 1493 1495 {ECO:0000244|PDB:4WXP}.
STRAND 1497 1503 {ECO:0000244|PDB:4WXP}.
STRAND 1509 1511 {ECO:0000244|PDB:4B76}.
HELIX 1514 1526 {ECO:0000244|PDB:4WXP}.
HELIX 1532 1544 {ECO:0000244|PDB:4WXP}.
HELIX 1555 1563 {ECO:0000244|PDB:4WXP}.
HELIX 1570 1579 {ECO:0000244|PDB:4WXP}.
HELIX 1584 1596 {ECO:0000244|PDB:4WXP}.
HELIX 1606 1611 {ECO:0000244|PDB:4WXP}.
TURN 1612 1614 {ECO:0000244|PDB:4WXP}.
HELIX 1615 1617 {ECO:0000244|PDB:4WXP}.
STRAND 1625 1629 {ECO:0000244|PDB:4WXP}.
STRAND 1635 1637 {ECO:0000244|PDB:8OHM}.
HELIX 1640 1650 {ECO:0000244|PDB:4WXP}.
TURN 1653 1655 {ECO:0000244|PDB:4WXP}.
STRAND 1680 1688 {ECO:0000244|PDB:1JXP}.
STRAND 2421 2425 {ECO:0000244|PDB:2GIQ}.
HELIX 2446 2449 {ECO:0000244|PDB:2GIQ}.
HELIX 2453 2455 {ECO:0000244|PDB:2GIQ}.
STRAND 2456 2458 {ECO:0000244|PDB:2GIQ}.
HELIX 2461 2463 {ECO:0000244|PDB:2GIQ}.
HELIX 2464 2471 {ECO:0000244|PDB:2GIQ}.
HELIX 2481 2494 {ECO:0000244|PDB:2GIQ}.
HELIX 2504 2509 {ECO:0000244|PDB:2GIQ}.
TURN 2519 2521 {ECO:0000244|PDB:2WRM}.
HELIX 2524 2528 {ECO:0000244|PDB:2GIQ}.
HELIX 2532 2547 {ECO:0000244|PDB:2GIQ}.
STRAND 2549 2551 {ECO:0000244|PDB:2GIQ}.
STRAND 2555 2559 {ECO:0000244|PDB:2GIQ}.
STRAND 2563 2565 {ECO:0000244|PDB:2GIQ}.
TURN 2568 2571 {ECO:0000244|PDB:1GX5}.
STRAND 2578 2581 {ECO:0000244|PDB:2GIQ}.
HELIX 2584 2606 {ECO:0000244|PDB:2GIQ}.
HELIX 2607 2609 {ECO:0000244|PDB:2GIQ}.
HELIX 2611 2613 {ECO:0000244|PDB:2GIQ}.
HELIX 2616 2629 {ECO:0000244|PDB:2GIQ}.
STRAND 2630 2638 {ECO:0000244|PDB:2GIQ}.
HELIX 2643 2646 {ECO:0000244|PDB:2GIQ}.
HELIX 2649 2659 {ECO:0000244|PDB:2GIQ}.
HELIX 2666 2678 {ECO:0000244|PDB:2GIQ}.
TURN 2679 2681 {ECO:0000244|PDB:1GX6}.
STRAND 2683 2686 {ECO:0000244|PDB:2GIQ}.
STRAND 2688 2690 {ECO:0000244|PDB:1CSJ}.
STRAND 2692 2696 {ECO:0000244|PDB:2GIQ}.
STRAND 2701 2703 {ECO:0000244|PDB:2HWI}.
HELIX 2706 2724 {ECO:0000244|PDB:2GIQ}.
STRAND 2728 2735 {ECO:0000244|PDB:2GIQ}.
STRAND 2738 2744 {ECO:0000244|PDB:2GIQ}.
HELIX 2748 2764 {ECO:0000244|PDB:2GIQ}.
STRAND 2769 2771 {ECO:0000244|PDB:2GIQ}.
STRAND 2776 2778 {ECO:0000244|PDB:2GIQ}.
HELIX 2779 2781 {ECO:0000244|PDB:2GIQ}.
STRAND 2787 2793 {ECO:0000244|PDB:2GIQ}.
STRAND 2795 2797 {ECO:0000244|PDB:3CVK}.
STRAND 2799 2804 {ECO:0000244|PDB:2GIQ}.
HELIX 2808 2819 {ECO:0000244|PDB:2GIQ}.
HELIX 2826 2833 {ECO:0000244|PDB:2GIQ}.
TURN 2834 2836 {ECO:0000244|PDB:2GIQ}.
HELIX 2838 2842 {ECO:0000244|PDB:2GIQ}.
HELIX 2844 2854 {ECO:0000244|PDB:2GIQ}.
STRAND 2858 2860 {ECO:0000244|PDB:3BSA}.
STRAND 2862 2866 {ECO:0000244|PDB:2GIQ}.
STRAND 2869 2873 {ECO:0000244|PDB:2GIQ}.
HELIX 2875 2877 {ECO:0000244|PDB:2GIQ}.
HELIX 2878 2886 {ECO:0000244|PDB:2GIQ}.
HELIX 2888 2891 {ECO:0000244|PDB:2GIQ}.
HELIX 2898 2911 {ECO:0000244|PDB:2GIQ}.
HELIX 2916 2933 {ECO:0000244|PDB:2GIQ}.
HELIX 2935 2944 {ECO:0000244|PDB:2GIQ}.
HELIX 2946 2948 {ECO:0000244|PDB:2GIQ}.
STRAND 2949 2951 {ECO:0000244|PDB:2GIQ}.
HELIX 2959 2962 {ECO:0000244|PDB:2GIQ}.
TURN 2967 2970 {ECO:0000244|PDB:2GIQ}.
STRAND 2976 2978 {ECO:0000244|PDB:4KE5}.
STRAND 2980 2982 {ECO:0000244|PDB:4EO6}.
SEQUENCE 3010 AA; 327194 MW; F8422D5ECCFDFD9C CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRAPR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTTPAS AYEVHNVSGI YHVTNDCSNA SIVYEAADLI MHTPGCVPCV REGNSSRCWV
ALTPTLAARN VTIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHVT
LQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG AHWGVLAGLA
YYSMAGNWAK VLIVMLLFAG VDGDTHVTGG AQAKTTNRLV SMFASGPSQK IQLINTNGSW
HINRTALNCN DSLQTGFLAA LFYTHSFNSS GCPERMAQCR TIDKFDQGWG PITYAESSRS
DQRPYCWHYP PPQCTIVPAS EVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN
NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLT CPTDCFRKHP EATYTKCGSG
PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRP
ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGIGSAVV SFAIKWEYVL
LLFLLLADAR VCACLWMMLL IAQAEAALEN LVVLNSASVA GAHGILSFLV FFCAAWYIKG
RLVPGATYAL YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA
RLIWWLQYFT TRAEADLHVW IPPLNARGGR DAIILLMCAV HPELIFDITK LLIAILGPLM
VLQAGITRVP YFVRAQGLIH ACMLVRKVAG GHYVQMAFMK LGALTGTYIY NHLTPLRDWP
RAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL PVSARRGKEI LLGPADSLEG
RGLRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT
VYHGAGSKTL AAPKGPITQM YTNVDQDLVG WPKPPGARSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPVSY LKGSSGGPLL CPFGHAVGIF RAAVCTRGVA KAVDFVPVES
METTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGIDPNIRT GVRTITTGAP VTYSTYGKFL ADGGCSGGAY DIIICDECHS
TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEVALSNT GEIPFYGKAI
PIEAIRGGRH LIFCHSKKKC DELAAKLSGL GINAVAYYRG LDVSVIPTIG DVVVVATDAL
MTGYTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEVTLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
VIVGRIILSG RPAIVPDREL LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT
KQAEAAAPVV ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
LTTQSTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV
WDWICTVLTD FKTWLQSKLL PQLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK
NGSMRIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
YVTGMTTDNV KCPCQVPAPE FFSEVDGVRL HRYAPACRPL LREEVTFQVG LNQYLVGSQL
PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTHHV
SPDADLIEAN LLWRQEMGGN ITRVESENKV VVLDSFDPLR AEEDEREVSV PAEILRKSKK
FPAAMPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPIK APPIPPPRRK RTVVLTESSV
SSALAELATK TFGSSESSAV DSGTATALPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL RHHNMVYATT
SRSAGLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK LLSVEEACKL TPPHSAKSKF
GYGAKDVRNL SSKAVNHIHS VWKDLLEDTV TPIDTTIMAK NEVFCVQPEK GGRKPARLIV
FPDLGVRVCE KMALYDVVST LPQVVMGSSY GFQYSPGQRV EFLVNTWKSK KNPMGFSYDT
RCFDSTVTEN DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA
SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE DAASLRVFTE
AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETAR
HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ
IIERLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC
GKYLFNWAVK TKLKLTPIPA ASRLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV
GVGIYLLPNR


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