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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_HCVH               Reviewed;        3011 AA.
P27958; O36579; O36608; O36609; O36610;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 199.
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 1a (isolate H) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=11108;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND DOMAIN V3 REGION.
PubMed=1658800; DOI=10.1073/pnas.88.22.10292;
Inchauspe G., Zebedee S., Lee D.H.H., Sugitani M., Nasoff M.,
Prince A.M.;
"Genomic structure of the human prototype strain H of hepatitis C
virus: comparison with American and Japanese isolates.";
Proc. Natl. Acad. Sci. U.S.A. 88:10292-10296(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate H77;
PubMed=9228008; DOI=10.1126/science.277.5325.570;
Kolykhalov A.A., Agapov E.V., Blight K.J., Mihalik K., Feinstone S.M.,
Rice C.M.;
"Transmission of hepatitis C by intrahepatic inoculation with
transcribed RNA.";
Science 277:570-574(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate H77;
PubMed=9238047; DOI=10.1073/pnas.94.16.8738;
Yanagi M., Purcell R.H., Emerson S.U., Bukh J.;
"Transcripts from a single full-length cDNA clone of hepatitis C virus
are infectious when directly transfected into the liver of a
chimpanzee.";
Proc. Natl. Acad. Sci. U.S.A. 94:8738-8743(1997).
[4]
IDENTIFICATION OF THE CYSTEINE PROTEASE, AND MUTAGENESIS OF HIS-952;
CYS-993 AND SER-1165.
PubMed=8248148; DOI=10.1073/pnas.90.22.10583;
Grakoui A., McCourt D.W., Wychowski C., Feinstone S.M., Rice C.M.;
"A second hepatitis C virus-encoded proteinase.";
Proc. Natl. Acad. Sci. U.S.A. 90:10583-10587(1993).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=7679746;
Grakoui A., Wychowski C., Lin C., Feinstone S.M., Rice C.M.;
"Expression and identification of hepatitis C virus polyprotein
cleavage products.";
J. Virol. 67:1385-1395(1993).
[6]
SUBCELLULAR LOCATION OF NS5A, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=8982089; DOI=10.1016/S0378-1119(96)00555-0;
Ide Y., Zhang L., Chen M., Inchauspe G., Bahl C., Sasaguri Y.,
Padmanabhan R.;
"Characterization of the nuclear localization signal and subcellular
distribution of hepatitis C virus nonstructural protein NS5A.";
Gene 182:203-211(1996).
[7]
PHOSPHORYLATION AT SER-2321, AND MUTAGENESIS OF SER-2321.
PubMed=10488152; DOI=10.1074/jbc.274.39.28011;
Reed K.E., Rice C.M.;
"Identification of the major phosphorylation site of the hepatitis C
virus H strain NS5A protein as serine 2321.";
J. Biol. Chem. 274:28011-28018(1999).
[8]
INTERACTION OF NS5A WITH SRCAP, AND SUBCELLULAR LOCATION OF NS5A.
PubMed=10702287; DOI=10.1074/jbc.275.10.7184;
Ghosh A.K., Majumder M., Steele R., Yaciuk P., Chrivia J., Ray R.,
Ray R.B.;
"Hepatitis C virus NS5A protein modulates transcription through a
novel cellular transcription factor SRCAP.";
J. Biol. Chem. 275:7184-7188(2000).
[9]
SUBCELLULAR LOCATION OF E1 AND E2, AND ROLE OF TRANSMEMBRANE DOMAINS.
PubMed=10729138; DOI=10.1128/JVI.74.8.3623-3633.2000;
Cocquerel L., Wychowski C., Minner F., Penin F., Dubuisson J.;
"Charged residues in the transmembrane domains of hepatitis C virus
glycoproteins play a major role in the processing, subcellular
localization, and assembly of these envelope proteins.";
J. Virol. 74:3623-3633(2000).
[10]
INTERACTION OF CORE PROTEIN WITH HUMAN C1QR1.
PubMed=11086025; DOI=10.1172/JCI10323;
Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J.,
Hahn Y.S.;
"Interaction between complement receptor gC1qR and hepatitis C virus
core protein inhibits T-lymphocyte proliferation.";
J. Clin. Invest. 106:1239-1249(2000).
[11]
CHARACTERIZATION OF HVR1 REGION.
PubMed=11356980; DOI=10.1128/JVI.75.12.5703-5710.2001;
Penin F., Combet C., Germanidis G., Frainais P.-O., Deleage G.,
Pawlotsky J.-M.;
"Conservation of the conformation and positive charges of hepatitis C
virus E2 envelope glycoprotein hypervariable region 1 points to a role
in cell attachment.";
J. Virol. 75:5703-5710(2001).
[12]
TOPOLOGY OF NS5B.
PubMed=11557752; DOI=10.1074/jbc.M103358200;
Schmidt-Mende J., Bieck E., Huegle T., Penin F., Rice C.M., Blum H.E.,
Moradpour D.;
"Determinants for membrane association of the hepatitis C virus RNA-
dependent RNA polymerase.";
J. Biol. Chem. 276:44052-44063(2001).
[13]
TOPOLOGY OF ENVELOPE GLYCOPROTEINS E1 AND E2.
PubMed=12065403; DOI=10.1093/emboj/cdf295;
Cocquerel L., Op de Beeck A., Lambot M., Roussel J., Delgrange D.,
Pillez A., Wychowski C., Penin F., Dubuisson J.;
"Topological changes in the transmembrane domains of hepatitis C virus
envelope glycoproteins.";
EMBO J. 21:2893-2902(2002).
[14]
TOPOLOGY, AND SUBCELLULAR LOCATION OF P7.
PubMed=11907211; DOI=10.1128/JVI.76.8.3720-3730.2002;
Carrere-Kremer S., Montpellier-Pala C., Cocquerel L., Wychowski C.,
Penin F., Dubuisson J.;
"Subcellular localization and topology of the p7 polypeptide of
hepatitis C virus.";
J. Virol. 76:3720-3730(2002).
[15]
TOPOLOGY OF NS5A.
PubMed=11744739; DOI=10.1074/jbc.M111289200;
Brass V., Bieck E., Montserret R., Woelk B., Hellings J.A., Blum H.E.,
Penin F., Moradpour D.;
"An amino-terminal amphipathic alpha-helix mediates membrane
association of the hepatitis C virus nonstructural protein 5A.";
J. Biol. Chem. 277:8130-8139(2002).
[16]
REPLICATION COMPLEX.
PubMed=12021330; DOI=10.1128/JVI.76.12.5974-5984.2002;
Egger D., Woelk B., Gosert R., Bianchi L., Blum H.E., Moradpour D.,
Bienz K.;
"Expression of hepatitis C virus proteins induces distinct membrane
alterations including a candidate viral replication complex.";
J. Virol. 76:5974-5984(2002).
[17]
REPLICATION COMPLEX.
PubMed=12692249; DOI=10.1128/JVI.77.9.5487-5492.2003;
Gosert R., Egger D., Lohmann V., Bartenschlager R., Blum H.E.,
Bienz K., Moradpour D.;
"Identification of the hepatitis C virus RNA replication complex in
Huh-7 cells harboring subgenomic replicons.";
J. Virol. 77:5487-5492(2003).
[18]
INHIBITION OF P7 BY LONG-ALKYL-CHAIN IMINOSUGAR DERIVATIVES.
PubMed=12719519; DOI=10.1073/pnas.1031527100;
Pavlovic D., Neville D.C., Argaud O., Blumberg B., Dwek R.A.,
Fischer W.B., Zitzmann N.;
"The hepatitis C virus p7 protein forms an ion channel that is
inhibited by long-alkyl-chain iminosugar derivatives.";
Proc. Natl. Acad. Sci. U.S.A. 100:6104-6108(2003).
[19]
MUTAGENESIS OF LYS-779 AND ARG-781.
STRAIN=Isolate H77;
PubMed=14504405; DOI=10.1073/pnas.1834545100;
Sakai A., Claire M.S., Faulk K., Govindarajan S., Emerson S.U.,
Purcell R.H., Bukh J.;
"The p7 polypeptide of hepatitis C virus is critical for infectivity
and contains functionally important genotype-specific sequences.";
Proc. Natl. Acad. Sci. U.S.A. 100:11646-11651(2003).
[20]
INTERACTION BETWEEN NON-STRUCTURAL PROTEINS.
PubMed=12692242; DOI=10.1128/JVI.77.9.5401-5414.2003;
Dimitrova M., Imbert I., Kieny M.P., Schuster C.;
"Protein-protein interactions between hepatitis C virus nonstructural
proteins.";
J. Virol. 77:5401-5414(2003).
[21]
TOPOLOGY, AND SUBCELLULAR LOCATION OF NS4B.
STRAIN=Isolate H77;
PubMed=12692244; DOI=10.1128/JVI.77.9.5428-5438.2003;
Lundin M., Monne M., Widell A., Von Heijne G., Persson M.A.A.;
"Topology of the membrane-associated hepatitis C virus protein NS4B.";
J. Virol. 77:5428-5438(2003).
[22]
INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81.
PubMed=12970454; DOI=10.1128/JVI.77.19.10677-10683.2003;
Cocquerel L., Kuo C.-C., Dubuisson J., Levy S.;
"CD81-dependent binding of hepatitis C virus E1E2 heterodimers.";
J. Virol. 77:10677-10683(2003).
[23]
INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81; LDLR AND SCARB1.
PubMed=12615904; DOI=10.1084/jem.20021756;
Bartosch B., Dubuisson J., Cosset F.-L.;
"Infectious hepatitis C virus pseudo-particles containing functional
E1-E2 envelope protein complexes.";
J. Exp. Med. 197:633-642(2003).
[24]
INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81.
PubMed=12913001; DOI=10.1074/jbc.M305289200;
Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J.,
Pascale S., Scarselli E., Cortese R., Nicosia A., Cosset F.-L.;
"Cell entry of hepatitis C virus requires a set of co-receptors that
include the CD81 tetraspanin and the SR-B1 scavenger receptor.";
J. Biol. Chem. 278:41624-41630(2003).
[25]
CHARACTERIZATION OF E1 AND E2.
PubMed=14990718; DOI=10.1128/JVI.78.6.2994-3002.2004;
Op De Beeck A., Voisset C., Bartosch B., Ciczora Y., Cocquerel L.,
Keck Z., Foung S., Cosset F.-L., Dubuisson J.;
"Characterization of functional hepatitis C virus envelope
glycoproteins.";
J. Virol. 78:2994-3002(2004).
[26]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=15247249; DOI=10.1074/jbc.M406315200;
Carrere-Kremer S., Montpellier C., Lorenzo L., Brulin B.,
Cocquerel L., Belouzard S., Penin F., Dubuisson J.;
"Regulation of hepatitis C virus polyprotein processing by signal
peptidase involves structural determinants at the p7 sequence
junctions.";
J. Biol. Chem. 279:41384-41392(2004).
[27]
INTERACTION WITH HUMAN CD209/DC-SIGN AND CLEC4M/DC-SIGNR.
STRAIN=Isolate H77;
PubMed=15371595; DOI=10.1073/pnas.0405695101;
Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C.,
Olson W.C., Gardner J.P., Dragic T.;
"L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver
cells by hepatitis C virus.";
Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004).
[28]
CLEAVAGE BETWEEN E2 AND P7, TOPOLOGY OF P7, AND MUTAGENESIS OF
VAL-720.
PubMed=15722527; DOI=10.1099/vir.0.80737-0;
Isherwood B.J., Patel A.H.;
"Analysis of the processing and transmembrane topology of the E2p7
protein of hepatitis C virus.";
J. Gen. Virol. 86:667-676(2005).
[29]
INTERACTION OF NS3 PROTEASE WITH HUMAN MAVS.
PubMed=16301520; DOI=10.1073/pnas.0508531102;
Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.;
"Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral
signaling protein off the mitochondria to evade innate immunity.";
Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005).
[30]
PALMITOYLATION AT CYS-1968 AND CYS-1972 (NS4B) BY HOST, AND
MUTAGENESIS OF CYS-1968 AND CYS-1972.
STRAIN=Isolate H77;
PubMed=16731940; DOI=10.1128/JVI.00053-06;
Yu G.-Y., Lee K.-J., Gao L., Lai M.M.C.;
"Palmitoylation and polymerization or in protein-protein interactions
of hepatitis C virus NS4B protein.";
J. Virol. 80:6013-6023(2006).
[31]
FUNCTION OF E1 AND E2.
STRAIN=Isolate H77;
PubMed=16894197; DOI=10.1099/vir.0.81710-0;
Codran A., Royer C., Jaeck D., Bastien-Valle M., Baumert T.F.,
Kieny M.P., Pereira C.A., Martin J.P.;
"Entry of hepatitis C virus pseudotypes into primary human hepatocytes
by clathrin-dependent endocytosis.";
J. Gen. Virol. 87:2583-2593(2006).
[32]
CHARACTERIZATION OF THE FUSION PEPTIDE.
STRAIN=Isolate H77;
PubMed=16533059; DOI=10.1021/bi0523963;
Perez-Berna A.J., Moreno M.R., Guillen J., Bernabeu A., Villalain J.;
"The membrane-active regions of the hepatitis C virus E1 and E2
envelope glycoproteins.";
Biochemistry 45:3755-3768(2006).
[33]
TOPOLOGY OF NS4B.
STRAIN=Isolate H77;
PubMed=17030859; DOI=10.1099/vir.0.82211-0;
Lundin M., Lindstrom H., Groenwall C., Persson M.A.;
"Dual topology of the processed hepatitis C virus protein NS4B is
influenced by the NS5A protein.";
J. Gen. Virol. 87:3263-3272(2006).
[34]
INTERACTION OF NS5A WITH NS5B AND HOST PKR.
PubMed=16951545;
Liang Y., Kang C.B., Yoon H.S.;
"Molecular and structural characterization of the domain 2 of
hepatitis C virus non-structural protein 5A.";
Mol. Cells 22:13-20(2006).
[35]
SUBCELLULAR LOCATION OF NS5A.
PubMed=17192310; DOI=10.1128/JVI.01279-06;
Brass V., Pal Z., Sapay N., Deleage G., Blum H.E., Penin F.,
Moradpour D.;
"Conserved determinants for membrane association of nonstructural
protein 5A from hepatitis C virus and related viruses.";
J. Virol. 81:2745-2757(2007).
[36]
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).
[37]
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).
[38]
ENZYME REGULATION, PHOSPHORYLATION, AND INTERACTION WITH PKN2.
PubMed=15364941; DOI=10.1074/jbc.M408617200;
Kim S.J., Kim J.H., Kim Y.G., Lim H.S., Oh J.W.;
"Protein kinase C-related kinase 2 regulates hepatitis C virus RNA
polymerase function by phosphorylation.";
J. Biol. Chem. 279:50031-50041(2004).
[39]
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).
[40]
INTERACTION WITH ACY3.
PubMed=19486448; DOI=10.1111/j.1440-1746.2009.05846.x;
Chen Y.R., Chen T.Y., Zhang S.L., Lin S.M., Zhao Y.R., Ye F.,
Zhang X., Shi L., Dang S.S., Liu M.;
"Identification of a novel protein binding to hepatitis C virus core
protein.";
J. Gastroenterol. Hepatol. 24:1300-1304(2009).
[41]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1206-1656.
PubMed=9187654; DOI=10.1038/nsb0697-463;
Yao N., Hesson T., Cable M.B., Hong Z., Kwong A.D., Le H.V.,
Weber P.C.;
"Structure of the hepatitis C virus RNA helicase domain.";
Nat. Struct. Biol. 4:463-467(1997).
[42]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1027-1206 IN COMPLEX WITH
NS4A.
PubMed=8861917; DOI=10.1016/S0092-8674(00)81351-3;
Kim J.L., Morgenstern K.A., Lin C., Fox T., Dwyer M.D., Landro J.A.,
Chambers S.P., Markland W., Lepre C.A., O'Malley E.T., Harbeson S.L.,
Rice C.M., Murcko M.A., Caron P.R., Thomson J.A.;
"Crystal structure of the hepatitis C virus NS3 protease domain
complexed with a synthetic NS4A cofactor peptide.";
Cell 87:343-355(1996).
[43]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1192-1657.
PubMed=9493270; DOI=10.1016/S0969-2126(98)00010-0;
Kim J.L., Morgenstern K.A., Griffith J.P., Dwyer M.D., Thomson J.A.,
Murcko M.A., Lin C., Caron P.R.;
"Hepatitis C virus NS3 RNA helicase domain with a bound
oligonucleotide: the crystal structure provides insights into the mode
of unwinding.";
Structure 6:89-100(1998).
[44]
STRUCTURE BY NMR OF 1353-1507.
PubMed=11846566; DOI=10.1006/jmbi.2001.5146;
Liu D., Wang Y.-S., Gesell J.J., Wyss D.F.;
"Solution structure and backbone dynamics of an engineered arginine-
rich subdomain 2 of the hepatitis C virus NS3 RNA helicase.";
J. Mol. Biol. 314:543-561(2001).
[45]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1027-1207.
PubMed=12465917; DOI=10.1021/ol027014p;
Andrews D.M., Chaignot H., Coomber B.A., Good A.C., Hind S.L.,
Johnson M.R., Jones P.S., Mills G., Robinson J.E., Skarzynski T.,
Slater M.J., Somers D.O.;
"Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray crystal structure
data in the optimization of P3 and P4 substituents.";
Org. Lett. 4:4479-4482(2002).
[46]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 903-1026, AND MUTAGENESIS OF
HIS-952 AND CYS-993.
PubMed=16862121; DOI=10.1038/nature04975;
Lorenz I.C., Marcotrigiano J., Dentzer T.G., Rice C.M.;
"Structure of the catalytic domain of the hepatitis C virus NS2-3
protease.";
Nature 442:831-835(2006).
-!- 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 (By
similarity). Also inhibited by long-alkyl-chain iminosugar
derivatives. Essential for infectivity. {ECO:0000250,
ECO:0000269|PubMed:16894197}.
-!- 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 (By
similarity). Cleaves and inhibits the host antiviral protein MAVS.
{ECO:0000250, ECO:0000269|PubMed:16894197}.
-!- 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. NS4B polymerization or in
protein-protein interactions activity may contribute to its
function in membranous web formation.
{ECO:0000269|PubMed:16894197}.
-!- 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:0000269|PubMed:16894197}.
-!- CATALYTIC ACTIVITY: Hydrolysis of four peptide bonds in the viral
precursor polyprotein, commonly with Asp or Glu in the P6
position, Cys or Thr in P1 and Ser or Ala in P1'.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
-!- ENZYME REGULATION: Activity of auto-protease NS2-3 is dependent on
zinc ions and completely inhibited by EDTA. Serine protease NS3 is
also activated by zinc ions (By similarity). Activity is up-
regulated by PKN2-mediated phosphorylation. {ECO:0000250,
ECO:0000269|PubMed:15364941}.
-!- SUBUNIT: Core protein is a homomultimer that binds the C-terminal
part of E1 and interacts with numerous cellular proteins.
Interacts (via N-terminus finger domain) with human PKN2.
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).
Interacts with human ACY3. 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:
P26660:- (xeno); NbExp=4; IntAct=EBI-6377335, EBI-6875462;
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-8753518, EBI-6858513;
P12814:ACTN1 (xeno); NbExp=7; IntAct=EBI-6904388, EBI-351710;
Q96CW1:AP2M1 (xeno); NbExp=4; IntAct=EBI-6377335, EBI-297683;
P02649:APOE (xeno); NbExp=4; IntAct=EBI-6904269, EBI-1222467;
Q96P48:ARAP1 (xeno); NbExp=3; IntAct=EBI-8753518, EBI-710003;
Q99941:ATF6B (xeno); NbExp=5; IntAct=EBI-8763498, EBI-2841031;
Q13315:ATM (xeno); NbExp=3; IntAct=EBI-6904388, EBI-495465;
O00499:BIN1 (xeno); NbExp=11; IntAct=EBI-8753518, EBI-719094;
O00499-7:BIN1 (xeno); NbExp=2; IntAct=EBI-8753518, EBI-8870146;
Q07021:C1QBP (xeno); NbExp=4; IntAct=EBI-6377335, EBI-347528;
Q9H6F5:CCDC86 (xeno); NbExp=3; IntAct=EBI-8753518, EBI-721289;
P60033:CD81 (xeno); NbExp=11; IntAct=EBI-6904269, EBI-712921;
P38936:CDKN1A (xeno); NbExp=3; IntAct=EBI-6377335, EBI-375077;
O96017:CHEK2 (xeno); NbExp=3; IntAct=EBI-6904388, EBI-1180783;
Q9UHD4:CIDEB (xeno); NbExp=6; IntAct=EBI-6919131, EBI-7062247;
Q920L9:CNX (xeno); NbExp=2; IntAct=EBI-6904269, EBI-9209498;
P29762:CRABP1 (xeno); NbExp=3; IntAct=EBI-8753518, EBI-725950;
O00571:DDX3X (xeno); NbExp=11; IntAct=EBI-6377335, EBI-353779;
P17844:DDX5 (xeno); NbExp=12; IntAct=EBI-6904388, EBI-351962;
P19525:EIF2AK2 (xeno); NbExp=5; IntAct=EBI-8753518, EBI-640775;
Q9Z2B5:Eif2ak3 (xeno); NbExp=5; IntAct=EBI-6904269, EBI-1226344;
Q14240:EIF4A2 (xeno); NbExp=4; IntAct=EBI-6904388, EBI-73473;
Q8IUD2-3:ERC1 (xeno); NbExp=8; IntAct=EBI-3649474, EBI-9352449;
Q8IUD2-4:ERC1 (xeno); NbExp=3; IntAct=EBI-3649474, EBI-9352501;
P02675:FGB (xeno); NbExp=4; IntAct=EBI-6377335, EBI-1034445;
P06241:FYN (xeno); NbExp=4; IntAct=EBI-706378, EBI-515315;
P62993:GRB2 (xeno); NbExp=3; IntAct=EBI-706378, EBI-401755;
P08631:HCK (xeno); NbExp=5; IntAct=EBI-706378, EBI-346340;
P09651:HNRNPA1 (xeno); NbExp=4; IntAct=EBI-6904388, EBI-352662;
P07823:HSPA5 (xeno); NbExp=3; IntAct=EBI-6904259, EBI-371776;
Q14164:IKBKE (xeno); NbExp=2; IntAct=EBI-6919131, EBI-307369;
O00410:IPO5 (xeno); NbExp=5; IntAct=EBI-8753518, EBI-356424;
P06240:Lck (xeno); NbExp=3; IntAct=EBI-706378, EBI-1401;
P02788:LTF (xeno); NbExp=9; IntAct=EBI-6904269, EBI-1058602;
P24627:LTF (xeno); NbExp=3; IntAct=EBI-6904269, EBI-8076910;
P07948:LYN (xeno); NbExp=4; IntAct=EBI-706378, EBI-79452;
Q16644:MAPKAPK3 (xeno); NbExp=5; IntAct=EBI-6377335, EBI-1384657;
P19338:NCL (xeno); NbExp=4; IntAct=EBI-6904388, EBI-346967;
P42356:PI4KA (xeno); NbExp=7; IntAct=EBI-8753518, EBI-723050;
P29590:PML (xeno); NbExp=6; IntAct=EBI-6377335, EBI-295890;
P28062:PSMB8 (xeno); NbExp=4; IntAct=EBI-3649474, EBI-372294;
Q8WTV0:SCARB1 (xeno); NbExp=2; IntAct=EBI-6904269, EBI-78657;
Q14141:SEPT6 (xeno); NbExp=4; IntAct=EBI-6904388, EBI-745901;
P62314:SNRPD1 (xeno); NbExp=7; IntAct=EBI-3649474, EBI-372177;
P42224:STAT1 (xeno); NbExp=4; IntAct=EBI-8753518, EBI-1057697;
Q96BZ9:TBC1D20 (xeno); NbExp=11; IntAct=EBI-8753518, EBI-9254454;
Q9UHD2:TBK1 (xeno); NbExp=4; IntAct=EBI-3649474, EBI-356402;
Q86WV6:TMEM173 (xeno); NbExp=5; IntAct=EBI-8763498, EBI-2800345;
Q13625:TP53BP2 (xeno); NbExp=5; IntAct=EBI-6377335, EBI-77642;
P39429:Traf2 (xeno); NbExp=5; IntAct=EBI-8753518, EBI-520016;
Q9P0L0:VAPA (xeno); NbExp=5; IntAct=EBI-6904388, EBI-1059156;
P08670:VIM (xeno); NbExp=4; IntAct=EBI-6377335, EBI-353844;
-!- 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; Single-pass type I membrane
protein. 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; Single-pass type I membrane
protein. 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:0000269|PubMed:11907211}; Multi-pass membrane protein
{ECO:0000269|PubMed:11907211}. Host cell membrane
{ECO:0000269|PubMed:11907211}. 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:0000269|PubMed:12692244}; Multi-pass
membrane protein {ECO:0000269|PubMed:12692244}.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=The exact location of the ribosomal frameshift is
unknown. The F protein seems to be generated by a -2 ribosomal
frameshift located in the vicinity of codon 11 of the core
protein coding sequence. However, some F proteins may also be
generated by +1 ribosomal frameshift. Since the core gene
encodes alternative reading frame proteins (ARFPs), many
functions depicted for the core protein might belong to the
ARFPs.;
Name=Genome polyprotein;
IsoId=P27958-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=F protein; Synonyms=Frameshifted protein;
IsoId=P0C045-1; Sequence=External;
Note=Produced by ribosomal frameshifting.;
-!- 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 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) (By similarity).
{ECO:0000250}.
-!- DOMAIN: The SH3-binding domain of NS5A is involved in the
interaction with human Bin1, GRB2 and Src-family kinases.
{ECO:0000250}.
-!- DOMAIN: The N-terminal one-third of serine protease NS3 contains
the protease activity. This region contains a zinc atom that does
not belong to the active site, but may play a structural rather
than a catalytic role. This region is essential for the activity
of protease NS2-3, maybe by contributing to the folding of the
latter. The helicase activity is located in the C-terminus of NS3.
{ECO:0000269|PubMed:1658800}.
-!- 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.
-!- 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: 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}.
-!- PTM: NS4B is palmitoylated. This modification may play a role in
its polymerization or in protein-protein interactions.
{ECO:0000269|PubMed:16731940}.
-!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
mutations in NS5A, reducing its inhibitory effect on replication.
{ECO:0000250}.
-!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
B virus when HCV and HBV coinfect the same cell, by suppressing
HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
{ECO:0000305}.
-!- CAUTION: The core gene probably also codes for alternative reading
frame proteins (ARFPs). Many functions depicted for the core
protein might belong to the ARFPs. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
-----------------------------------------------------------------------
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EMBL; M67463; AAA45534.1; -; Genomic_RNA.
EMBL; AF009606; AAB66324.1; -; Genomic_RNA.
EMBL; AF011751; AAB67036.1; -; Genomic_RNA.
EMBL; AF011752; AAB67037.1; -; Genomic_RNA.
EMBL; AF011753; AAB67038.1; -; Genomic_RNA.
PIR; A36814; GNWVCH.
PDB; 1A1R; X-ray; 2.50 A; A/B=1027-1206.
PDB; 1A1V; X-ray; 2.20 A; A=1193-1657.
PDB; 1CWX; NMR; -; A=2-45.
PDB; 1HEI; X-ray; 2.10 A; A/B=1206-1656.
PDB; 1JR6; NMR; -; A=1353-1456, A=1478-1507.
PDB; 1N1L; X-ray; 2.60 A; A/B=1027-1206.
PDB; 1ONB; NMR; -; A=1353-1456, A=1478-1507.
PDB; 1R7C; NMR; -; A=1973-2003.
PDB; 1R7D; NMR; -; A=1973-2003.
PDB; 1R7E; NMR; -; A=1973-2003.
PDB; 1R7F; NMR; -; A=1973-2003.
PDB; 1R7G; NMR; -; A=1973-2003.
PDB; 1RGQ; X-ray; 2.90 A; A/B=1027-1207.
PDB; 2A4R; X-ray; 2.40 A; A/C=1027-1207, B/D=1680-1696.
PDB; 2F9V; X-ray; 2.60 A; A/C=1027-1207, B/D=1678-1696.
PDB; 2HD0; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I/J/K/L=903-1026.
PDB; 2JXF; NMR; -; A=1751-1780.
PDB; 2KDR; NMR; -; X=1938-1965.
PDB; 2N1P; NMR; -; A=2982-3011.
PDB; 2O8M; X-ray; 2.00 A; A/B=1027-1207, C/D=1678-1696.
PDB; 2OBO; X-ray; 2.60 A; A/C=1022-1207, B/D=1677-1695.
PDB; 2OBQ; X-ray; 2.50 A; A/C=1027-1207, B/D=1678-1696.
PDB; 2OC0; X-ray; 2.30 A; A/C=1027-1207, B/D=1680-1696.
PDB; 2OC1; X-ray; 2.70 A; A/C=1027-1207, B/D=1680-1696.
PDB; 2OC7; X-ray; 2.70 A; A/C=1027-1207, B/D=1680-1696.
PDB; 2OC8; X-ray; 2.66 A; A/C=1027-1207, B/D=1680-1696.
PDB; 2OIN; X-ray; 2.50 A; A/B=1027-1207, C/D=1678-1696.
PDB; 2P59; X-ray; 2.90 A; C/D=1678-1696.
PDB; 2QV1; X-ray; 2.40 A; C/D=1678-1696.
PDB; 2XI2; X-ray; 1.80 A; A/B/C=2421-2990.
PDB; 2XI3; X-ray; 1.70 A; A/B=2421-2990.
PDB; 2XNI; X-ray; 3.30 A; A/B=1027-1206.
PDB; 4CL1; X-ray; 3.50 A; A/B/C/D=2005-2174.
PDB; 4JZN; X-ray; 2.05 A; K=434-446.
PDB; 4JZO; X-ray; 2.22 A; I/J/K/L=434-446.
PDB; 4MWF; X-ray; 2.64 A; C/D=412-459, C/D=486-645.
PDB; 4N0Y; X-ray; 1.75 A; A=314-324.
PDB; 4Q0X; X-ray; 2.90 A; E=421-446.
PDB; 4XVJ; X-ray; 2.00 A; A=412-423.
PDB; 4Z0X; X-ray; 2.00 A; C=435-446.
PDB; 5EOC; X-ray; 1.98 A; P/Q=412-422.
PDB; 5ERW; X-ray; 2.90 A; C=434-446.
PDB; 5FGB; X-ray; 1.65 A; F/G=405-425.
PDB; 5FGC; X-ray; 1.90 A; A=405-425.
PDBsum; 1A1R; -.
PDBsum; 1A1V; -.
PDBsum; 1CWX; -.
PDBsum; 1HEI; -.
PDBsum; 1JR6; -.
PDBsum; 1N1L; -.
PDBsum; 1ONB; -.
PDBsum; 1R7C; -.
PDBsum; 1R7D; -.
PDBsum; 1R7E; -.
PDBsum; 1R7F; -.
PDBsum; 1R7G; -.
PDBsum; 1RGQ; -.
PDBsum; 2A4R; -.
PDBsum; 2F9V; -.
PDBsum; 2HD0; -.
PDBsum; 2JXF; -.
PDBsum; 2KDR; -.
PDBsum; 2N1P; -.
PDBsum; 2O8M; -.
PDBsum; 2OBO; -.
PDBsum; 2OBQ; -.
PDBsum; 2OC0; -.
PDBsum; 2OC1; -.
PDBsum; 2OC7; -.
PDBsum; 2OC8; -.
PDBsum; 2OIN; -.
PDBsum; 2P59; -.
PDBsum; 2QV1; -.
PDBsum; 2XI2; -.
PDBsum; 2XI3; -.
PDBsum; 2XNI; -.
PDBsum; 4CL1; -.
PDBsum; 4JZN; -.
PDBsum; 4JZO; -.
PDBsum; 4MWF; -.
PDBsum; 4N0Y; -.
PDBsum; 4Q0X; -.
PDBsum; 4XVJ; -.
PDBsum; 4Z0X; -.
PDBsum; 5EOC; -.
PDBsum; 5ERW; -.
PDBsum; 5FGB; -.
PDBsum; 5FGC; -.
DisProt; DP00588; -.
ProteinModelPortal; P27958; -.
SMR; P27958; -.
ELM; P27958; -.
IntAct; P27958; 234.
MINT; MINT-106294; -.
BindingDB; P27958; -.
ChEMBL; CHEMBL3638344; -.
DrugBank; DB08644; {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER.
iPTMnet; P27958; -.
euHCVdb; AF009606; -.
euHCVdb; AF011751; -.
euHCVdb; AF011752; -.
euHCVdb; AF011753; -.
euHCVdb; M67463; -.
OrthoDB; VOG0900004E; -.
BRENDA; 3.4.21.98; 2642.
BRENDA; 3.6.4.13; 2642.
Reactome; R-HSA-8854214; TBC/RABGAPs.
EvolutionaryTrace; P27958; -.
Proteomes; UP000000518; Genome.
Proteomes; UP000115192; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
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:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044177; C:host cell Golgi apparatus; IDA:AgBase.
GO; GO:0044186; C:host cell lipid particle; IDA:AgBase.
GO; GO:0033644; C:host cell membrane; IDA:AgBase.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0033647; C:host intracellular organelle; IMP:AgBase.
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:0016887; F:ATPase activity; IMP:AgBase.
GO; GO:0060590; F:ATPase regulator activity; IDA:AgBase.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:AgBase.
GO; GO:0019899; F:enzyme binding; IPI:AgBase.
GO; GO:0031072; F:heat shock protein binding; IPI:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:1990254; F:keratin filament binding; IPI:AgBase.
GO; GO:0019900; F:kinase binding; IDA:AgBase.
GO; GO:0042288; F:MHC class I protein binding; IPI:AgBase.
GO; GO:0002039; F:p53 binding; IPI:AgBase.
GO; GO:0008233; F:peptidase activity; IDA:AgBase.
GO; GO:0019903; F:protein phosphatase binding; IPI:AgBase.
GO; GO:0017137; F:Rab GTPase binding; IPI:AgBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IDA:AgBase.
GO; GO:0005124; F:scavenger receptor binding; IPI:AgBase.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:AgBase.
GO; GO:0008236; F:serine-type peptidase activity; IDA:AgBase.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0097677; F:STAT family protein binding; IPI:AgBase.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0035663; F:Toll-like receptor 2 binding; IMP:AgBase.
GO; GO:0008134; F:transcription factor binding; IPI:AgBase.
GO; GO:0031369; F:translation initiation factor binding; IPI:AgBase.
GO; GO:0008270; F:zinc ion binding; IDA:AgBase.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0071593; P:lymphocyte aggregation; IMP:AgBase.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0044833; P:modulation by virus of host protein transport; IMP:AgBase.
GO; GO:0019056; P:modulation by virus of host transcription; IMP:AgBase.
GO; GO:0033663; P:negative regulation by symbiont of host defense-related protein level; IMP:AgBase.
GO; GO:1990214; P:negative regulation by symbiont of host protein levels; IDA:AgBase.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IMP:AgBase.
GO; GO:0032780; P:negative regulation of ATPase activity; IDA:AgBase.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:AgBase.
GO; GO:0060548; P:negative regulation of cell death; IDA:AgBase.
GO; GO:0050689; P:negative regulation of defense response to virus by host; TAS:AgBase.
GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IDA:AgBase.
GO; GO:0060702; P:negative regulation of endoribonuclease activity; IMP:AgBase.
GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IMP:AgBase.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:AgBase.
GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; IMP:AgBase.
GO; GO:0033673; P:negative regulation of kinase activity; IMP:AgBase.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:AgBase.
GO; GO:0050709; P:negative regulation of protein secretion; IDA:AgBase.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:AgBase.
GO; GO:1900369; P:negative regulation of RNA interference; IDA:AgBase.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IDA:AgBase.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IDA:AgBase.
GO; GO:0034156; P:negative regulation of toll-like receptor 7 signaling pathway; IDA:AgBase.
GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; IDA:AgBase.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:AgBase.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:AgBase.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IMP:AgBase.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:1990219; P:positive regulation by symbiont of host protein levels; IDA:AgBase.
GO; GO:1990216; P:positive regulation by symbiont of host transcription; IDA:AgBase.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IDA:AgBase.
GO; GO:0030307; P:positive regulation of cell growth; IDA:AgBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:AgBase.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IDA:AgBase.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:AgBase.
GO; GO:0051047; P:positive regulation of secretion; IDA:AgBase.
GO; GO:0045727; P:positive regulation of translation; IMP:AgBase.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IDA:AgBase.
GO; GO:0048524; P:positive regulation of viral process; IDA:AgBase.
GO; GO:1990044; P:protein localization to lipid particle; IDA:AgBase.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IDA:AgBase.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:AgBase.
GO; GO:0046774; P:suppression by virus of host intracellular interferon activity; IMP:AgBase.
GO; GO:0039560; P:suppression by virus of host IRF9 activity; IMP:AgBase.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039546; P:suppression by virus of host MAVS activity by MAVS proteolysis; TAS:AgBase.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IDA:AgBase.
GO; GO:0039580; P:suppression by virus of host PKR activity; IDA:AgBase.
GO; GO:0039613; P:suppression by virus of host protein phosphorylation; IDA:AgBase.
GO; GO:0039565; P:suppression by virus of host STAT1 activity by positive regulation of STAT1 catabolic process; IDA:AgBase.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IDA:AgBase.
GO; GO:0039653; P:suppression by virus of host transcription; IDA:AgBase.
GO; GO:0039608; P:suppression by virus of host translation initiation factor activity by induction of host protein dephosphorylation; IDA:AgBase.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IDA:AgBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; IMP:AgBase.
GO; GO:0046762; P:viral budding from ER membrane; IDA:UniProtKB.
GO; GO:0019082; P:viral protein processing; TAS:AgBase.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR004109; Peptidase_S29.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF01543; HCV_capsid; 1.
Pfam; PF01542; HCV_core; 1.
Pfam; PF01539; HCV_env; 1.
Pfam; PF01560; HCV_NS1; 1.
Pfam; PF01538; HCV_NS2; 1.
Pfam; PF01006; HCV_NS4a; 1.
Pfam; PF01001; HCV_NS4b; 1.
Pfam; PF01506; HCV_NS5a; 1.
Pfam; PF08300; HCV_NS5a_1a; 1.
Pfam; PF08301; HCV_NS5a_1b; 1.
Pfam; PF12941; HCV_NS5a_C; 1.
Pfam; PF02907; Peptidase_S29; 1.
Pfam; PF00998; RdRP_3; 1.
ProDom; PD001388; HCV_env; 1.
SMART; SM00487; DEXDc; 1.
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; Reference proteome; Ribonucleoprotein;
Ribosomal frameshifting; 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_0000037566.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000037567.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000037568.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000037569.
CHAIN 384 746 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000037570.
CHAIN 747 809 p7.
/FTId=PRO_0000037571.
CHAIN 810 1026 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000037572.
CHAIN 1027 1657 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000037573.
CHAIN 1658 1711 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000037574.
CHAIN 1712 1972 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000037575.
CHAIN 1973 2420 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000037576.
CHAIN 2421 3011 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000037577.
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 2990 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2991 3011 Helical. {ECO:0000250}.
DOMAIN 899 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 2634 2752 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 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. {ECO:0000250}.
REGION 2210 2275 PKR-binding. {ECO:0000255}.
REGION 2249 2306 NS4B-binding. {ECO:0000255}.
REGION 2351 2420 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 2286 2327 Pro-rich.
COMPBIAS 2996 2999 Poly-Leu.
ACT_SITE 952 952 For protease NS2-3 activity; shared with
dimeric partner.
ACT_SITE 972 972 For protease NS2-3 activity; shared with
dimeric partner.
ACT_SITE 993 993 For protease NS2-3 activity; shared with
dimeric partner.
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.
SITE 809 810 Cleavage; by host signal peptidase.
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 2420 2421 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:0000250}.
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}.
MOD_RES 2321 2321 Phosphoserine; by host.
{ECO:0000269|PubMed:10488152}.
LIPID 1968 1968 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:16731940}.
LIPID 1972 1972 S-palmitoyl cysteine; by host; partial.
{ECO:0000269|PubMed:16731940}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 476 476 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}.
VARIANT 212 212 V -> I (in strain: Isolate H77).
VARIANT 297 297 H -> R (in strain: Isolate H77).
VARIANT 303 303 D -> S (in strain: Isolate H77).
VARIANT 321 321 N -> D (in strain: Isolate H77).
VARIANT 360 360 K -> A (in strain: Isolate H77).
VARIANT 391 391 N -> S (in strain: Isolate H77).
VARIANT 394 394 R -> H (in strain: Isolate H77).
VARIANT 431 431 E -> D (in strain: Isolate H77).
VARIANT 434 434 N -> T (in strain: Isolate H77).
VARIANT 444 444 Q -> R (in strain: Isolate H77).
VARIANT 457 457 A -> T (in strain: Isolate H77).
VARIANT 564 566 CGA -> RGV (in strain: Isolate H77).
VARIANT 589 589 Y -> H (in strain: Isolate H77).
VARIANT 602 602 R -> W (in strain: Isolate H77).
VARIANT 650 650 E -> G (in strain: Isolate H77).
VARIANT 773 773 C -> R (in strain: Isolate H77).
VARIANT 787 787 V -> A (in strain: Isolate H77).
VARIANT 790 790 L -> F (in strain: Isolate H77).
VARIANT 877 877 T -> M (in strain: Isolate H77).
VARIANT 883 883 A -> T (in strain: Isolate H77).
VARIANT 948 948 C -> Y (in strain: Isolate H77).
VARIANT 954 954 A -> T (in strain: Isolate H77).
VARIANT 1026 1026 L -> Q (in strain: Isolate H77).
VARIANT 1033 1033 A -> T (in strain: Isolate H77).
VARIANT 1049 1049 G -> S (in strain: Isolate H77).
VARIANT 1100 1100 T -> M (in strain: Isolate H77).
VARIANT 1121 1121 T -> A (in strain: Isolate H77).
VARIANT 1173 1173 T -> A (in strain: Isolate H77).
VARIANT 1202 1202 E -> G (in strain: Isolate H77).
VARIANT 1214 1214 S -> P (in strain: Isolate H77).
VARIANT 1247 1247 K -> Q (in strain: Isolate H77).
VARIANT 1303 1303 A -> G (in strain: Isolate H77).
VARIANT 1327 1327 S -> L (in strain: Isolate H77).
VARIANT 1556 1556 G -> E (in strain: Isolate H77).
VARIANT 1608 1608 R -> W (in strain: Isolate H77).
VARIANT 1742 1742 H -> Q (in strain: Isolate H77).
VARIANT 1839 1840 LD -> IG (in strain: Isolate H77).
VARIANT 1893 1893 A -> V (in strain: Isolate H77).
VARIANT 1898 1900 FAS -> CAA (in strain: Isolate H77).
VARIANT 1905 1905 R -> H (in strain: Isolate H77).
VARIANT 1940 1940 A -> V (in strain: Isolate H77).
VARIANT 2043 2043 T -> A (in strain: Isolate H77).
VARIANT 2053 2053 K -> R (in strain: Isolate H77).
VARIANT 2061 2061 F -> L (in strain: Isolate H77).
VARIANT 2102 2102 V -> I (in strain: Isolate H77).
VARIANT 2185 2185 A -> E (in strain: Isolate H77).
VARIANT 2283 2283 P -> R (in strain: Isolate H77).
VARIANT 2296 2296 L -> P (in strain: Isolate H77).
VARIANT 2341 2341 P -> S (in strain: Isolate H77).
VARIANT 2355 2355 S -> P (in strain: Isolate H77).
VARIANT 2400 2400 L -> F (in strain: Isolate H77).
VARIANT 2425 2425 S -> T (in strain: Isolate H77).
VARIANT 2469 2469 K -> Q (in strain: Isolate H77).
VARIANT 2512 2512 A -> T (in strain: Isolate H77).
VARIANT 2637 2637 L -> F (in strain: Isolate H77).
VARIANT 2703 2703 R -> G (in strain: Isolate H77).
VARIANT 2715 2715 R -> C (in strain: Isolate H77).
VARIANT 2755 2755 S -> N (in strain: Isolate H77).
VARIANT 2925 2925 W -> R (in strain: Isolate H77).
VARIANT 2933 2933 A -> S (in strain: Isolate H77).
VARIANT 2937 2937 K -> R (in strain: Isolate H77).
VARIANT 2960 2960 T -> A (in strain: Isolate H77).
MUTAGEN 720 720 V->L: Increases processing between E2 and
p7. {ECO:0000269|PubMed:15722527}.
MUTAGEN 779 779 K->I: Virus can no longer infect
chimpanzee.
{ECO:0000269|PubMed:14504405}.
MUTAGEN 781 781 R->S: Virus can no longer infect
chimpanzee.
{ECO:0000269|PubMed:14504405}.
MUTAGEN 952 952 H->A: Complete loss of NS2-NS3 cleavage.
{ECO:0000269|PubMed:16862121,
ECO:0000269|PubMed:8248148}.
MUTAGEN 993 993 C->A: Complete loss of NS2-NS3 cleavage.
{ECO:0000269|PubMed:16862121,
ECO:0000269|PubMed:8248148}.
MUTAGEN 1165 1165 S->A: Complete loss of NS3-NS4A, NS4A-
NS4B, NS4B-NS5A and NS5A-NS5B cleavages.
{ECO:0000269|PubMed:8248148}.
MUTAGEN 1968 1968 C->A: Strong decrease in NS4B
palmitoylation.
{ECO:0000269|PubMed:16731940}.
MUTAGEN 1972 1972 C->A: Slight decrease in NS4B
palmitoylation.
{ECO:0000269|PubMed:16731940}.
MUTAGEN 2321 2321 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:10488152}.
STRAND 10 12 {ECO:0000244|PDB:1CWX}.
STRAND 16 18 {ECO:0000244|PDB:1CWX}.
TURN 19 23 {ECO:0000244|PDB:1CWX}.
STRAND 30 35 {ECO:0000244|PDB:1CWX}.
TURN 36 38 {ECO:0000244|PDB:1CWX}.
STRAND 39 41 {ECO:0000244|PDB:1CWX}.
HELIX 316 323 {ECO:0000244|PDB:4N0Y}.
STRAND 412 414 {ECO:0000244|PDB:5EOC}.
STRAND 416 418 {ECO:0000244|PDB:5EOC}.
STRAND 420 422 {ECO:0000244|PDB:5EOC}.
STRAND 425 427 {ECO:0000244|PDB:4MWF}.
TURN 432 435 {ECO:0000244|PDB:4MWF}.
HELIX 436 442 {ECO:0000244|PDB:4Z0X}.
STRAND 496 498 {ECO:0000244|PDB:4MWF}.
HELIX 499 501 {ECO:0000244|PDB:4MWF}.
STRAND 502 504 {ECO:0000244|PDB:4MWF}.
STRAND 507 515 {ECO:0000244|PDB:4MWF}.
STRAND 532 534 {ECO:0000244|PDB:4MWF}.
STRAND 536 538 {ECO:0000244|PDB:4MWF}.
STRAND 550 556 {ECO:0000244|PDB:4MWF}.
STRAND 561 565 {ECO:0000244|PDB:4MWF}.
HELIX 568 571 {ECO:0000244|PDB:4MWF}.
TURN 574 577 {ECO:0000244|PDB:4MWF}.
STRAND 579 581 {ECO:0000244|PDB:4MWF}.
STRAND 602 604 {ECO:0000244|PDB:4MWF}.
STRAND 607 609 {ECO:0000244|PDB:4MWF}.
HELIX 614 617 {ECO:0000244|PDB:4MWF}.
HELIX 619 621 {ECO:0000244|PDB:4MWF}.
STRAND 625 633 {ECO:0000244|PDB:4MWF}.
STRAND 636 644 {ECO:0000244|PDB:4MWF}.
HELIX 911 923 {ECO:0000244|PDB:2HD0}.
TURN 924 927 {ECO:0000244|PDB:2HD0}.
HELIX 931 944 {ECO:0000244|PDB:2HD0}.
TURN 951 953 {ECO:0000244|PDB:2HD0}.
HELIX 956 958 {ECO:0000244|PDB:2HD0}.
HELIX 964 967 {ECO:0000244|PDB:2HD0}.
TURN 971 974 {ECO:0000244|PDB:2HD0}.
STRAND 975 977 {ECO:0000244|PDB:2HD0}.
STRAND 982 984 {ECO:0000244|PDB:2HD0}.
TURN 988 990 {ECO:0000244|PDB:2HD0}.
STRAND 1000 1008 {ECO:0000244|PDB:2HD0}.
STRAND 1010 1013 {ECO:0000244|PDB:2HD0}.
TURN 1016 1018 {ECO:0000244|PDB:2HD0}.
HELIX 1019 1021 {ECO:0000244|PDB:2HD0}.
STRAND 1032 1035 {ECO:0000244|PDB:2O8M}.
HELIX 1039 1048 {ECO:0000244|PDB:2O8M}.
STRAND 1057 1063 {ECO:0000244|PDB:2O8M}.
STRAND 1068 1074 {ECO:0000244|PDB:2O8M}.
STRAND 1077 1081 {ECO:0000244|PDB:2O8M}.
HELIX 1082 1085 {ECO:0000244|PDB:2O8M}.
STRAND 1090 1092 {ECO:0000244|PDB:2OC0}.
STRAND 1095 1097 {ECO:0000244|PDB:2OC0}.
STRAND 1100 1103 {ECO:0000244|PDB:2O8M}.
TURN 1104 1107 {ECO:0000244|PDB:2O8M}.
STRAND 1108 1112 {ECO:0000244|PDB:2O8M}.
STRAND 1128 1133 {ECO:0000244|PDB:2O8M}.
STRAND 1139 1144 {ECO:0000244|PDB:2O8M}.
STRAND 1146 1157 {ECO:0000244|PDB:2O8M}.
HELIX 1158 1160 {ECO:0000244|PDB:2O8M}.
TURN 1161 1163 {ECO:0000244|PDB:2O8M}.
STRAND 1168 1170 {ECO:0000244|PDB:2O8M}.
TURN 1172 1174 {ECO:0000244|PDB:2F9V}.
STRAND 1176 1186 {ECO:0000244|PDB:2O8M}.
STRAND 1189 1197 {ECO:0000244|PDB:2O8M}.
HELIX 1198 1206 {ECO:0000244|PDB:2O8M}.
STRAND 1224 1226 {ECO:0000244|PDB:1HEI}.
TURN 1236 1238 {ECO:0000244|PDB:1HEI}.
HELIX 1239 1246 {ECO:0000244|PDB:1HEI}.
STRAND 1251 1256 {ECO:0000244|PDB:1HEI}.
HELIX 1258 1271 {ECO:0000244|PDB:1HEI}.
STRAND 1277 1280 {ECO:0000244|PDB:1HEI}.
STRAND 1283 1285 {ECO:0000244|PDB:1HEI}.
STRAND 1290 1295 {ECO:0000244|PDB:1HEI}.
HELIX 1296 1301 {ECO:0000244|PDB:1HEI}.
HELIX 1304 1307 {ECO:0000244|PDB:1A1V}.
STRAND 1311 1316 {ECO:0000244|PDB:1HEI}.
TURN 1317 1319 {ECO:0000244|PDB:1HEI}.
HELIX 1323 1335 {ECO:0000244|PDB:1HEI}.
TURN 1336 1340 {ECO:0000244|PDB:1HEI}.
STRAND 1342 1347 {ECO:0000244|PDB:1HEI}.
STRAND 1362 1366 {ECO:0000244|PDB:1HEI}.
STRAND 1371 1375 {ECO:0000244|PDB:1HEI}.
STRAND 1378 1380 {ECO:0000244|PDB:1HEI}.
HELIX 1382 1385 {ECO:0000244|PDB:1HEI}.
STRAND 1386 1393 {ECO:0000244|PDB:1HEI}.
HELIX 1397 1409 {ECO:0000244|PDB:1HEI}.
STRAND 1414 1417 {ECO:0000244|PDB:1HEI}.
HELIX 1423 1425 {ECO:0000244|PDB:1A1V}.
STRAND 1428 1436 {ECO:0000244|PDB:1HEI}.
STRAND 1442 1444 {ECO:0000244|PDB:1HEI}.
STRAND 1449 1453 {ECO:0000244|PDB:1HEI}.
STRAND 1456 1463 {ECO:0000244|PDB:1HEI}.
STRAND 1467 1469 {ECO:0000244|PDB:1HEI}.
STRAND 1471 1478 {ECO:0000244|PDB:1HEI}.
HELIX 1481 1488 {ECO:0000244|PDB:1HEI}.
STRAND 1493 1495 {ECO:0000244|PDB:1HEI}.
STRAND 1497 1502 {ECO:0000244|PDB:1HEI}.
HELIX 1514 1527 {ECO:0000244|PDB:1HEI}.
HELIX 1532 1544 {ECO:0000244|PDB:1HEI}.
STRAND 1545 1548 {ECO:0000244|PDB:1HEI}.
HELIX 1555 1564 {ECO:0000244|PDB:1HEI}.
HELIX 1570 1578 {ECO:0000244|PDB:1HEI}.
HELIX 1584 1597 {ECO:0000244|PDB:1HEI}.
HELIX 1606 1611 {ECO:0000244|PDB:1HEI}.
TURN 1614 1618 {ECO:0000244|PDB:1HEI}.
STRAND 1627 1629 {ECO:0000244|PDB:1HEI}.
STRAND 1635 1637 {ECO:0000244|PDB:1HEI}.
HELIX 1640 1652 {ECO:0000244|PDB:1HEI}.
STRAND 1680 1687 {ECO:0000244|PDB:2O8M}.
HELIX 1753 1777 {ECO:0000244|PDB:2JXF}.
HELIX 1940 1964 {ECO:0000244|PDB:2KDR}.
HELIX 1976 1999 {ECO:0000244|PDB:1R7C}.
STRAND 2422 2426 {ECO:0000244|PDB:2XI3}.
HELIX 2445 2450 {ECO:0000244|PDB:2XI3}.
HELIX 2454 2456 {ECO:0000244|PDB:2XI3}.
STRAND 2457 2459 {ECO:0000244|PDB:2XI3}.
HELIX 2462 2464 {ECO:0000244|PDB:2XI3}.
HELIX 2465 2472 {ECO:0000244|PDB:2XI3}.
HELIX 2482 2495 {ECO:0000244|PDB:2XI3}.
HELIX 2505 2510 {ECO:0000244|PDB:2XI3}.
HELIX 2525 2529 {ECO:0000244|PDB:2XI3}.
HELIX 2533 2548 {ECO:0000244|PDB:2XI3}.
STRAND 2550 2552 {ECO:0000244|PDB:2XI3}.
STRAND 2556 2560 {ECO:0000244|PDB:2XI3}.
STRAND 2564 2566 {ECO:0000244|PDB:2XI3}.
HELIX 2569 2571 {ECO:0000244|PDB:2XI3}.
STRAND 2579 2582 {ECO:0000244|PDB:2XI3}.
HELIX 2585 2607 {ECO:0000244|PDB:2XI3}.
HELIX 2608 2610 {ECO:0000244|PDB:2XI3}.
HELIX 2612 2614 {ECO:0000244|PDB:2XI3}.
HELIX 2617 2629 {ECO:0000244|PDB:2XI3}.
STRAND 2631 2639 {ECO:0000244|PDB:2XI3}.
HELIX 2644 2647 {ECO:0000244|PDB:2XI3}.
HELIX 2650 2660 {ECO:0000244|PDB:2XI3}.
HELIX 2667 2679 {ECO:0000244|PDB:2XI3}.
TURN 2680 2682 {ECO:0000244|PDB:2XI3}.
STRAND 2684 2687 {ECO:0000244|PDB:2XI3}.
STRAND 2693 2697 {ECO:0000244|PDB:2XI3}.
HELIX 2707 2726 {ECO:0000244|PDB:2XI3}.
STRAND 2729 2736 {ECO:0000244|PDB:2XI3}.
STRAND 2739 2745 {ECO:0000244|PDB:2XI3}.
HELIX 2749 2765 {ECO:0000244|PDB:2XI3}.
STRAND 2770 2772 {ECO:0000244|PDB:2XI3}.
HELIX 2780 2782 {ECO:0000244|PDB:2XI3}.
STRAND 2788 2794 {ECO:0000244|PDB:2XI3}.
STRAND 2800 2806 {ECO:0000244|PDB:2XI3}.
HELIX 2809 2820 {ECO:0000244|PDB:2XI3}.
HELIX 2827 2835 {ECO:0000244|PDB:2XI3}.
HELIX 2839 2843 {ECO:0000244|PDB:2XI3}.
HELIX 2845 2855 {ECO:0000244|PDB:2XI3}.
STRAND 2863 2867 {ECO:0000244|PDB:2XI3}.
STRAND 2870 2874 {ECO:0000244|PDB:2XI3}.
HELIX 2876 2878 {ECO:0000244|PDB:2XI3}.
HELIX 2879 2887 {ECO:0000244|PDB:2XI3}.
HELIX 2889 2892 {ECO:0000244|PDB:2XI3}.
HELIX 2899 2912 {ECO:0000244|PDB:2XI3}.
HELIX 2917 2934 {ECO:0000244|PDB:2XI3}.
HELIX 2936 2945 {ECO:0000244|PDB:2XI3}.
HELIX 2947 2949 {ECO:0000244|PDB:2XI3}.
STRAND 2950 2952 {ECO:0000244|PDB:2XI3}.
HELIX 2960 2964 {ECO:0000244|PDB:2XI3}.
TURN 2968 2971 {ECO:0000244|PDB:2XI3}.
STRAND 2984 2986 {ECO:0000244|PDB:2N1P}.
HELIX 2994 3007 {ECO:0000244|PDB:2N1P}.
SEQUENCE 3011 AA; 327146 MW; 772CBB29CCD94753 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTVPAS AYQVRNSSGL YHVTNDCPNS SVVYEAADAI LHTPGCVPCV REGNASRCWV
AVTPTVATRD GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRHHWT
TQDCNCSIYP GHITGHRMAW NMMMNWSPTA ALVVAQLLRI PQAIMDMIAG AHWGVLAGIK
YFSMVGNWAK VLVVLLLFAG VDAETHVTGG NAGRTTAGLV GLLTPGAKQN IQLINTNGSW
HINSTALNCN ESLNTGWLAG LFYQHKFNSS GCPERLASCR RLTDFAQGWG PISYANGSGL
DERPYCWHYP PRPCGIVPAK SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ANDTDVFVLN
NTRPPLGNWF GCTWMNSTGF TKVCGAPPCV IGGVGNNTLL CPTDCFRKYP EATYSRCGSG
PRITPRCMVD YPYRLWHYPC TINYTIFKVR MYVGGVEHRL EAACNWTRGE RCDLEDRDRS
ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGVGSSIA SWAIKWEYVV
LLFLLLADAR VCSCLWMMLL ISQAEAALEN LVILNAASLA GTHGLVSFLV FFCFAWYLKG
RWVPGAVYAL YGMWPLLLLL LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIS
WCMWWLQYFL TRVEAQLHVW VPPLNVRGGR DAVILLTCVV HPALVFDITK LLLAIFGPLW
ILQASLLKVP YFVRVQGLLR ICALARKIAG GHYVQMAIIK LGALTGTCVY NHLAPLRDWA
HNGLRDLAVA VEPVVFSRME TKLITWGADT AACGDIINGL PVSARRGQEI LLGPADGMVS
KGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ IVSTATQTFL ATCINGVCWT
VYHGAGTRTI ASPKGPVIQT YTNVDQDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPTGHAVGLF RAAVCTRGVA KAVDFIPVEN
LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAKGYK VLVLNPSVAA
TLGFGAYMSK AHGVDPNIRT GVRTITTGSP ITYSTYGKFL ADAGCSGGAY DIIICDECHS
TDATSISGIG TVLDQAETAG ARLVVLATAT PPGSVTVSHP NIEEVALSTT GEIPFYGKAI
PLEVIKGGRH LIFCHSKKKC DELAAKLVAL GINAVAYYRG LDVSVIPTSG DVVVVSTDAL
MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR
FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV CQDHLGFWEG
VFTGLTHIDA HFLSQTKQSG ENFPYLVAYQ ATVCARAQAP PPSWDQMRKC LIRLKPTLHG
PTPLLYRLGA VQNEVTLTHP ITKYIMTCMS ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV
VIVGRIVLSG KPAIIPDREV LYQEFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS
RHAEVITPAV QTNWQKLEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP
LTTGQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAALD SVGLGKVLVD ILAGYGAGVA
GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALAVGVVFAS ILRRRVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTAILSS LTVTQLLRRL HQWISSECTT PCSGSWLRDI
WDWICEVLSD FKTWLKAKLM PQLPGIPFVS CQRGYRGVWR GDGIMHTRCH CGAEITGHVK
NGTMRIVGPR TCKNMWSGTF FINAYTTGPC TPLPAPNYKF ALWRVSAEEY VEIRRVGDFH
YVSGMTTDNL KCPCQIPSPE FFTELDGVRL HRFAPPCKPL LREEVSFRVG LHEYPVGSQL
PCEPEPDVAV LTSMLTDPSH ITAEAAGRRL ARGSPPSMAS SSASQLSAPS LKATCTANHD
SPDAELIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLV AEEDEREVSV PAEILRKSRR
FAPALPVWAR PDYNPLLVET WKKPDYEPPV VHGCPLPPPR SPPVPPPRKK RTVVLTESTL
PTALAELATK SFGSSSTSGI TGDNTTTSSE PAPSGCPPDS DVESYSSMPP LEGEPGDPDL
SDGSWSTVSS GADTEDVVCC SMSYSWTGAL VTPCAAEEQK LPINALSNSL LRHHNLVYST
TSRSACQRKK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA NLLSVEEACS LAPPHSAKSK
FGYGAKDVRC HARKAVAHIN SVWKDLLEDS VTPIDTTIMA KNEVFCVQPE KGGRKPARLI
VFPDLGVRVC EKMALYDVVS KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGLSYD
TRCFDSTVTE SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR
ASRVLTTSCG NTLTRYIKAR AACRAAGLQD CTMLVCGDDL VVICESAGVQ EDAASLRAFT
EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR VYYLTRDPTT PLARAAWETA
RHTPVNSWLG NIIMFAPTLW ARMILMTHFF SVLIARDQLE QALNCEIYGA CYSIEPLDLP
PIIQRLHGLS AFSLHSYSPG EINRVAACLR KLGVPPLRAW RHRAWSVRAR LLARGGKAAI
CGKYLFNWAV RTKLKLTPIT AAGRLDLSGW FTAGYSGGDI YHSVSHARPR WFWFCLLLLA
AGVGIYLLPN R


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