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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_HCV1               Reviewed;        3011 AA.
P26664; Q9IFE5;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 181.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Core protein p21;
AltName: Full=Capsid protein C;
AltName: Full=p21;
Contains:
RecName: Full=Core protein p19;
Contains:
RecName: Full=Envelope glycoprotein E1;
AltName: Full=gp32;
AltName: Full=gp35;
Contains:
RecName: Full=Envelope glycoprotein E2;
AltName: Full=NS1;
AltName: Full=gp68;
AltName: Full=gp70;
Contains:
RecName: Full=p7;
Contains:
RecName: Full=Protease NS2-3;
Short=p23;
EC=3.4.22.-;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.98;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Hepacivirin;
AltName: Full=NS3P;
AltName: Full=p70;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
AltName: Full=p8;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 5A;
Short=NS5A;
AltName: Full=p56;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=NS5B;
AltName: Full=p68;
Hepatitis C virus genotype 1a (isolate 1) (HCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=11104;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1848704; DOI=10.1073/pnas.88.6.2451;
Choo Q.-L., Richman K.H., Han J.H., Berger K., Lee C., Dong C.,
Gallegos C., Coit D., Medina-Selby A., Barr P.J., Weiner A.J.,
Bradley D.W., Kuo G., Houghton M.;
"Genetic organization and diversity of the hepatitis C virus.";
Proc. Natl. Acad. Sci. U.S.A. 88:2451-2455(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone pHCV-1/SF;
PubMed=11369872;
Lanford R.E., Lee H., Chavez D., Guerra B., Brasky K.M.;
"Infectious cDNA clone of the hepatitis C virus genotype 1 prototype
sequence.";
J. Gen. Virol. 82:1291-1297(2001).
[3]
PROTEIN SEQUENCE OF 2-16, AND SUBCELLULAR LOCATION OF CORE PROTEIN.
PubMed=7491770; DOI=10.1006/viro.1995.0018;
Lo S.-Y., Masiarz F., Hwang S.B., Lai M.M.C., Ou J.-H.;
"Differential subcellular localization of hepatitis C virus core gene
products.";
Virology 213:455-461(1995).
[4]
FUNCTION OF CORE PROTEIN.
PubMed=8533458; DOI=10.1016/0168-1702(95)00034-N;
Ray R.B., Lagging L.M., Meyer K., Steele R., Ray R.;
"Transcriptional regulation of cellular and viral promoters by the
hepatitis C virus core protein.";
Virus Res. 37:209-220(1995).
[5]
INTERACTION OF CORE PROTEIN WITH E1 PROTEIN.
PubMed=8764026;
Lo S.-Y., Selby M.J., Ou J.-H.;
"Interaction between hepatitis C virus core protein and E1 envelope
protein.";
J. Virol. 70:5177-5182(1996).
[6]
FUNCTION OF CORE PROTEIN.
PubMed=8955036; DOI=10.1006/viro.1996.0644;
Ray R.B., Meyer K., Ray R.;
"Suppression of apoptotic cell death by hepatitis C virus core
protein.";
Virology 226:176-182(1996).
[7]
FUNCTION OF CORE PROTEIN.
PubMed=9110985; DOI=10.1074/jbc.272.17.10983;
Ray R.B., Steele R., Meyer K., Ray R.;
"Transcriptional repression of p53 promoter by hepatitis C virus core
protein.";
J. Biol. Chem. 272:10983-10986(1997).
[8]
INTERACTION OF NS5A WITH HUMAN EIF2AK2/PKR.
PubMed=9143277; DOI=10.1006/viro.1997.8493;
Gale M.J. Jr., Korth M.J., Tang N.M., Tan S.-L., Hopkins D.A.,
Dever T.E., Polyak S.J., Gretch D.R., Katze M.G.;
"Evidence that hepatitis C virus resistance to interferon is mediated
through repression of the PKR protein kinase by the nonstructural 5A
protein.";
Virology 230:217-227(1997).
[9]
FUNCTION OF CORE PROTEIN.
PubMed=9524287; DOI=10.1016/S0378-1119(98)00030-4;
Ray R.B., Steele R., Meyer K., Ray R.;
"Hepatitis C virus core protein represses p21WAF1/Cip1/Sid1 promoter
activity.";
Gene 208:331-336(1998).
[10]
FUNCTION OF CORE PROTEIN.
PubMed=9811706;
Shrivastava A., Manna S.K., Ray R., Aggarwal B.B.;
"Ectopic expression of hepatitis C virus core protein differentially
regulates nuclear transcription factors.";
J. Virol. 72:9722-9728(1998).
[11]
INTERACTION OF E2 WITH HUMAN EIF2AK2/PKR.
PubMed=10390359; DOI=10.1126/science.285.5424.107;
Taylor D.R., Shi S.T., Romano P.R., Barber G.N., Lai M.M.C.;
"Inhibition of the interferon-inducible protein kinase PKR by HCV E2
protein.";
Science 285:107-110(1999).
[12]
FUNCTION OF E2.
PubMed=11152499; DOI=10.1128/JVI.75.3.1265-1273.2001;
Taylor D.R., Tian B., Romano P.R., Hinnebusch A.G., Lai M.M.C.,
Mathews M.B.;
"Hepatitis C virus envelope protein E2 does not inhibit PKR by simple
competition with autophosphorylation sites in the RNA-binding
domain.";
J. Virol. 75:1265-1273(2001).
[13]
TOPOLOGY OF NS2 PROTEIN.
PubMed=12082096; DOI=10.1074/jbc.M202304200;
Yamaga A.K., Ou J.-H.;
"Membrane topology of the hepatitis C virus NS2 protein.";
J. Biol. Chem. 277:33228-33234(2002).
[14]
INTERACTION OF NS5A WITH HUMAN SRC-FAMILY KINASES, AND MUTAGENESIS OF
2001-PRO--PRO-2004; 2315-PRO--PRO-2318 AND 2322-PRO--PRO-2326.
PubMed=14993658; DOI=10.1099/vir.0.19691-0;
Macdonald A., Crowder K., Street A., McCormick C., Harris M.;
"The hepatitis C virus NS5A protein binds to members of the Src family
of tyrosine kinases and regulates kinase activity.";
J. Gen. Virol. 85:721-729(2004).
[15]
SUBCELLULAR LOCATION OF CORE PROTEIN.
PubMed=15254168; DOI=10.1128/JVI.78.15.7958-7968.2004;
Schwer B., Ren S., Pietschmann T., Kartenbeck J., Kaehlcke K.,
Bartenschlager R., Yen T.S.B., Ott M.;
"Targeting of hepatitis C virus core protein to mitochondria through a
novel C-terminal localization motif.";
J. Virol. 78:7958-7968(2004).
[16]
FUNCTION OF NS5A.
PubMed=15784895; DOI=10.1099/vir.0.80728-0;
Kalliampakou K.I., Kalamvoki M., Mavromara P.;
"Hepatitis C virus (HCV) NS5A protein downregulates HCV IRES-dependent
translation.";
J. Gen. Virol. 86:1015-1025(2005).
[17]
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).
[18]
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).
[19]
INTERACTION WITH HNRNPA1 AND SEPT6.
PubMed=17229681; DOI=10.1128/JVI.01311-06;
Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.;
"An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6,
facilitate hepatitis C virus replication.";
J. Virol. 81:3852-3865(2007).
-!- FUNCTION: Core protein packages viral RNA to form a viral
nucleocapsid, and promotes virion budding. Modulates viral
translation initiation by interacting with HCV IRES and 40S
ribosomal subunit. Also regulates many host cellular functions
such as signaling pathways and apoptosis. Prevents the
establishment of cellular antiviral state by blocking the
interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling
pathways and by inducing human STAT1 degradation. Thought to play
a role in virus-mediated cell transformation leading to
hepatocellular carcinomas. Interacts with, and activates STAT3
leading to cellular transformation. May repress the promoter of
p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the
cytoplasm. Also represses cell cycle negative regulating factor
CDKN1A, thereby interrupting an important check point of normal
cell cycle regulation. Targets transcription factors involved in
the regulation of inflammatory responses and in the immune
response: suppresses NK-kappaB activation, and activates AP-1.
Could mediate apoptotic pathways through association with TNF-type
receptors TNFRSF1A and LTBR, although its effect on death
receptor-induced apoptosis remains controversial. Enhances TRAIL
mediated apoptosis, suggesting that it might play a role in
immune-mediated liver cell injury. Seric core protein is able to
bind C1QR1 at the T-cell surface, resulting in down-regulation of
T-lymphocytes proliferation. May transactivate human MYC, Rous
sarcoma virus LTR, and SV40 promoters. May suppress the human FOS
and HIV-1 LTR activity. Alters lipid metabolism by interacting
with hepatocellular proteins involved in lipid accumulation and
storage. Core protein induces up-regulation of FAS promoter
activity, and thereby probably contributes to the increased
triglyceride accumulation in hepatocytes (steatosis) (By
similarity). {ECO:0000250}.
-!- FUNCTION: E1 and E2 glycoproteins form a heterodimer that is
involved in virus attachment to the host cell, virion
internalization through clathrin-dependent endocytosis and fusion
with host membrane. E1/E2 heterodimer binds to human LDLR, CD81
and SCARB1/SR-BI receptors, but this binding is not sufficient for
infection, some additional liver specific cofactors may be needed.
The fusion function may possibly be carried by E1. E2 inhibits
human EIF2AK2/PKR activation, preventing the establishment of an
antiviral state. E2 is a viral ligand for CD209/DC-SIGN and
CLEC4M/DC-SIGNR, which are respectively found on dendritic cells
(DCs), and on liver sinusoidal endothelial cells and macrophage-
like cells of lymph node sinuses. These interactions allow capture
of circulating HCV particles by these cells and subsequent
transmission to permissive cells. DCs act as sentinels in various
tissues where they entrap pathogens and convey them to local
lymphoid tissue or lymph node for establishment of immunity.
Capture of circulating HCV particles by these SIGN+ cells may
facilitate virus infection of proximal hepatocytes and lymphocyte
subpopulations and may be essential for the establishment of
persistent infection.
-!- 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.
-!- FUNCTION: NS3 displays three enzymatic activities: serine
protease, NTPase and RNA helicase. NS3 serine protease, in
association with NS4A, is responsible for the cleavages of NS3-
NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also
prevents phosphorylation of human IRF3, thus preventing the
establishment of dsRNA induced antiviral state. NS3 RNA helicase
binds to RNA and unwinds dsRNA in the 3' to 5' direction, and
likely RNA stable secondary structure in the template strand.
Cleaves and inhibits the host antiviral protein MAVS (By
similarity). {ECO:0000250}.
-!- FUNCTION: NS4B induces a specific membrane alteration that serves
as a scaffold for the virus replication complex. This membrane
alteration gives rise to the so-called ER-derived membranous web
that contains the replication complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: NS5A is a component of the replication complex involved
in RNA-binding. Its interaction with Human VAPB may target the
viral replication complex to vesicles. Down-regulates viral IRES
translation initiation. Mediates interferon resistance, presumably
by interacting with and inhibiting human EIF2AK2/PKR. Seems to
inhibit apoptosis by interacting with BIN1 and FKBP8. The
hyperphosphorylated form of NS5A is an inhibitor of viral
replication (By similarity). {ECO:0000250}.
-!- FUNCTION: NS5B is an RNA-dependent RNA polymerase that plays an
essential role in the virus replication. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolysis of four peptide bonds in the viral
precursor polyprotein, commonly with Asp or Glu in the P6
position, Cys or Thr in P1 and Ser or Ala in P1'.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
-!- ENZYME REGULATION: Activity of auto-protease NS2-3 is dependent on
zinc ions and completely inhibited by EDTA. Serine protease NS3 is
also activated by zinc ions (By similarity). {ECO:0000250}.
-!- SUBUNIT: Core protein is a homomultimer that binds the C-terminal
part of E1 and interacts with numerous cellular proteins.
Interaction with human STAT1 SH2 domain seems to result in
decreased STAT1 phosphorylation, leading to decreased IFN-
stimulated gene transcription. In addition to blocking the
formation of phosphorylated STAT1, the core protein also promotes
ubiquitin-mediated proteasome-dependent degradation of STAT1.
Interacts with, and constitutively activates human STAT3.
Associates with human LTBR and TNFRSF1A receptors and possibly
induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK,
C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins.
Interacts with human CREB3 nuclear transcription protein,
triggering cell transformation. May interact with human p53. Also
binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1
and E2 glycoproteins form a heterodimer that binds to human LDLR,
CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human
EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR.
p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing
a pair of composite active sites at the dimerization interface.
NS2 seems to interact with all other non-structural (NS) proteins.
NS4A interacts with NS3 serine protease and stabilizes its
folding. NS3-NS4A complex is essential for the activation of the
latter and allows membrane anchorage of NS3. NS3 interacts with
human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form
homodimers and seem to interact with all other non-structural (NS)
proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2,
BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B
is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6
(By similarity). {ECO:0000250}.
-!- INTERACTION:
Q91XE4:Acy3 (xeno); NbExp=6; IntAct=EBI-6941357, EBI-7378963;
O00571:DDX3X (xeno); NbExp=3; IntAct=EBI-9209740, EBI-353779;
P42224:STAT1 (xeno); NbExp=5; IntAct=EBI-6941357, EBI-1057697;
-!- 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. Host cytoplasm.
Host nucleus. Secreted.
-!- 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.
-!- 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=P26664-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=F protein; Synonyms=Frameshifted protein;
IsoId=P0C044-1; 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.
-!- DOMAIN: The N-terminal one-third of serine protease NS3 contains
the protease activity. This region contains a zinc atom that does
not belong to the active site, but may play a structural rather
than a catalytic role. This region is essential for the activity
of protease NS2-3, maybe by contributing to the folding of the
latter. The helicase activity is located in the C-terminus of NS3
(By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The structural proteins, core, E1, E2 and p7 are produced by
proteolytic processing by host signal peptidases. The core protein
is synthesized as a 21 kDa precursor which is retained in the ER
membrane through the hydrophobic signal peptide. Cleavage by the
signal peptidase releases the 19 kDa mature core protein. The
other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are
cleaved by the viral proteases (By similarity). {ECO:0000250}.
-!- PTM: Envelope E1 and E2 glycoproteins are highly N-glycosylated.
{ECO:0000250}.
-!- PTM: Core protein is phosphorylated by host PKC and PKA.
{ECO:0000250}.
-!- PTM: NS5A is phosphorylated in a basal form termed p56. p58 is a
hyperphosphorylated form of p56. p56 and p58 coexist in the cell
in roughly equivalent amounts. Hyperphosphorylation is dependent
on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1,
MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for
NS5A phosphorylation (By similarity). {ECO:0000250}.
-!- PTM: NS4B is palmitoylated. This modification may play a role in
its polymerization or in protein-protein interactions (By
similarity). {ECO:0000250}.
-!- PTM: The N-terminus of a fraction of NS4B molecules seems to be
relocated post-translationally from the cytoplasm to the ER lumen,
with a 5th transmembrane segment. The C-terminus of NS2 may be
lumenal with a fourth transmembrane segment (By similarity).
{ECO:0000250}.
-!- PTM: Core protein is ubiquitinated; mediated by UBE3A and leading
to core protein subsequent proteasomal degradation. {ECO:0000250}.
-!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
mutations in NS5A, reducing its inhibitory effect on replication.
{ECO:0000250}.
-!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
B virus when HCV and HBV coinfect the same cell, by suppressing
HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
{ECO:0000305}.
-!- CAUTION: The core gene probably also codes for alternative reading
frame proteins (ARFPs). Many functions depicted for the core
protein might belong to the ARFPs. {ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
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EMBL; M62321; AAA45676.1; -; Genomic_RNA.
EMBL; AF271632; AAF81759.1; -; Genomic_RNA.
PIR; A39166; GNWVC3.
PDB; 1RTL; X-ray; 2.75 A; A/B=1027-1207.
PDB; 2A4G; X-ray; 2.50 A; A/C=1027-1207.
PDB; 2GVF; X-ray; 2.50 A; A/C=1027-1207, B/D=1680-1696.
PDB; 3EYD; X-ray; 2.30 A; A/C=1027-1207, B/D=1680-1696.
PDB; 3HKW; X-ray; 1.55 A; A/B/C=2421-2990.
PDB; 3KN2; X-ray; 2.30 A; A/C=1027-1207.
PDB; 3QGH; X-ray; 2.14 A; A=2421-2990.
PDB; 3QGI; X-ray; 1.80 A; A=2421-2990.
PDB; 3RC4; X-ray; 1.50 A; A=1030-1208.
PDB; 3RC5; X-ray; 1.60 A; A=1030-1208.
PDBsum; 1RTL; -.
PDBsum; 2A4G; -.
PDBsum; 2GVF; -.
PDBsum; 3EYD; -.
PDBsum; 3HKW; -.
PDBsum; 3KN2; -.
PDBsum; 3QGH; -.
PDBsum; 3QGI; -.
PDBsum; 3RC4; -.
PDBsum; 3RC5; -.
ProteinModelPortal; P26664; -.
SMR; P26664; -.
IntAct; P26664; 4.
MINT; MINT-97561; -.
BindingDB; P26664; -.
ChEMBL; CHEMBL4620; -.
DrugBank; DB05868; Ciluprevir.
DrugBank; DB06038; ITMN-191.
DrugBank; DB06058; XTL-6865.
MEROPS; C18.001; -.
euHCVdb; AF271632; -.
euHCVdb; M62321; -.
OrthoDB; VOG0900004E; -.
SABIO-RK; P26664; -.
EvolutionaryTrace; P26664; -.
PMAP-CutDB; P26664; -.
Proteomes; UP000007410; Genome.
Proteomes; UP000008855; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044186; C:host cell lipid particle; IEA:UniProtKB-SubCell.
GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR004109; Peptidase_S29.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF01543; HCV_capsid; 1.
Pfam; PF01542; HCV_core; 1.
Pfam; PF01539; HCV_env; 1.
Pfam; PF01560; HCV_NS1; 1.
Pfam; PF01538; HCV_NS2; 1.
Pfam; PF01006; HCV_NS4a; 1.
Pfam; PF01001; HCV_NS4b; 1.
Pfam; PF01506; HCV_NS5a; 1.
Pfam; PF08300; HCV_NS5a_1a; 1.
Pfam; PF08301; HCV_NS5a_1b; 1.
Pfam; PF12941; HCV_NS5a_C; 1.
Pfam; PF02907; Peptidase_S29; 1.
Pfam; PF00998; RdRP_3; 1.
ProDom; PD001388; HCV_env; 1.
SMART; SM00487; DEXDc; 1.
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;
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; 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:0000269|PubMed:7491770}.
CHAIN 2 191 Core protein p21. {ECO:0000255}.
/FTId=PRO_0000037517.
CHAIN 2 177 Core protein p19. {ECO:0000250}.
/FTId=PRO_0000037518.
PROPEP 178 191 ER anchor for the core protein, removed
in mature form by host signal peptidase.
{ECO:0000250}.
/FTId=PRO_0000037519.
CHAIN 192 383 Envelope glycoprotein E1. {ECO:0000255}.
/FTId=PRO_0000037520.
CHAIN 384 746 Envelope glycoprotein E2. {ECO:0000255}.
/FTId=PRO_0000037521.
CHAIN 747 809 p7. {ECO:0000250}.
/FTId=PRO_0000037522.
CHAIN 810 1026 Protease NS2-3. {ECO:0000255|PROSITE-
ProRule:PRU01030}.
/FTId=PRO_0000037523.
CHAIN 1027 1657 Serine protease NS3. {ECO:0000255}.
/FTId=PRO_0000037524.
CHAIN 1658 1711 Non-structural protein 4A. {ECO:0000255}.
/FTId=PRO_0000037525.
CHAIN 1712 1972 Non-structural protein 4B. {ECO:0000255}.
/FTId=PRO_0000037526.
CHAIN 1973 2420 Non-structural protein 5A. {ECO:0000255}.
/FTId=PRO_0000037527.
CHAIN 2421 3011 RNA-directed RNA polymerase.
{ECO:0000255}.
/FTId=PRO_0000037528.
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:0000255}.
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:0000305}.
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. {ECO:0000250}.
MOTIF 5 13 Nuclear localization signal.
{ECO:0000255}.
MOTIF 38 43 Nuclear localization signal.
{ECO:0000255}.
MOTIF 58 64 Nuclear localization signal.
{ECO:0000255}.
MOTIF 66 71 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1316 1319 DECH box.
MOTIF 2322 2325 SH3-binding. {ECO:0000255}.
MOTIF 2327 2335 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 796 803 Poly-Leu.
COMPBIAS 1432 1435 Poly-Val.
COMPBIAS 2286 2327 Pro-rich.
COMPBIAS 2996 2999 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 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: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 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 9 11 KKN -> RKT (in infectious clone pHCV-1/
SF).
VARIANT 399 399 F -> S (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 402 402 L -> F (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 929 929 I -> A (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 1703 1703 R -> Q (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 2021 2021 V -> G (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 2349 2350 TR -> IK (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 2378 2378 P -> R (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 2413 2413 N -> S (in strain: Isolate infectious
clone pHCV-1/SF).
VARIANT 2992 2992 I -> F (in strain: Isolate infectious
clone pHCV-1/SF).
MUTAGEN 2001 2004 PQLP->AQLA: No effect on binding to Src-
family kinases.
{ECO:0000269|PubMed:14993658}.
MUTAGEN 2315 2318 PLPP->ALAA: No effect on binding to Src-
family kinases.
{ECO:0000269|PubMed:14993658}.
MUTAGEN 2322 2326 PPVPP->APVAA: Complete loss of binding to
GRB2 and Src-family kinases.
{ECO:0000269|PubMed:14993658}.
STRAND 1032 1035 {ECO:0000244|PDB:3RC4}.
HELIX 1039 1048 {ECO:0000244|PDB:3RC4}.
STRAND 1057 1063 {ECO:0000244|PDB:3RC4}.
STRAND 1068 1074 {ECO:0000244|PDB:3RC4}.
STRAND 1077 1080 {ECO:0000244|PDB:3RC4}.
HELIX 1082 1085 {ECO:0000244|PDB:3RC4}.
STRAND 1090 1092 {ECO:0000244|PDB:3EYD}.
STRAND 1095 1097 {ECO:0000244|PDB:3EYD}.
STRAND 1100 1103 {ECO:0000244|PDB:3RC4}.
TURN 1104 1107 {ECO:0000244|PDB:3RC4}.
STRAND 1108 1112 {ECO:0000244|PDB:3RC4}.
STRAND 1129 1133 {ECO:0000244|PDB:3RC4}.
STRAND 1139 1144 {ECO:0000244|PDB:3RC4}.
STRAND 1146 1157 {ECO:0000244|PDB:3RC4}.
HELIX 1158 1160 {ECO:0000244|PDB:3RC4}.
TURN 1161 1163 {ECO:0000244|PDB:3RC4}.
STRAND 1168 1170 {ECO:0000244|PDB:3RC4}.
TURN 1172 1174 {ECO:0000244|PDB:2GVF}.
STRAND 1176 1186 {ECO:0000244|PDB:3RC4}.
STRAND 1189 1197 {ECO:0000244|PDB:3RC4}.
HELIX 1198 1205 {ECO:0000244|PDB:3RC4}.
STRAND 1680 1689 {ECO:0000244|PDB:3EYD}.
STRAND 2422 2426 {ECO:0000244|PDB:3HKW}.
HELIX 2445 2450 {ECO:0000244|PDB:3HKW}.
HELIX 2454 2456 {ECO:0000244|PDB:3HKW}.
STRAND 2457 2459 {ECO:0000244|PDB:3HKW}.
HELIX 2462 2464 {ECO:0000244|PDB:3HKW}.
HELIX 2465 2472 {ECO:0000244|PDB:3HKW}.
HELIX 2482 2495 {ECO:0000244|PDB:3HKW}.
HELIX 2505 2510 {ECO:0000244|PDB:3HKW}.
HELIX 2525 2529 {ECO:0000244|PDB:3HKW}.
HELIX 2533 2548 {ECO:0000244|PDB:3HKW}.
STRAND 2550 2552 {ECO:0000244|PDB:3HKW}.
STRAND 2556 2560 {ECO:0000244|PDB:3HKW}.
STRAND 2564 2566 {ECO:0000244|PDB:3HKW}.
STRAND 2579 2582 {ECO:0000244|PDB:3HKW}.
HELIX 2585 2607 {ECO:0000244|PDB:3HKW}.
HELIX 2608 2610 {ECO:0000244|PDB:3HKW}.
HELIX 2612 2614 {ECO:0000244|PDB:3HKW}.
HELIX 2617 2630 {ECO:0000244|PDB:3HKW}.
STRAND 2631 2639 {ECO:0000244|PDB:3HKW}.
HELIX 2644 2647 {ECO:0000244|PDB:3HKW}.
HELIX 2650 2660 {ECO:0000244|PDB:3HKW}.
HELIX 2667 2679 {ECO:0000244|PDB:3HKW}.
TURN 2680 2682 {ECO:0000244|PDB:3HKW}.
STRAND 2684 2687 {ECO:0000244|PDB:3HKW}.
STRAND 2693 2697 {ECO:0000244|PDB:3HKW}.
HELIX 2707 2725 {ECO:0000244|PDB:3HKW}.
STRAND 2729 2736 {ECO:0000244|PDB:3HKW}.
STRAND 2739 2745 {ECO:0000244|PDB:3HKW}.
HELIX 2749 2765 {ECO:0000244|PDB:3HKW}.
STRAND 2770 2772 {ECO:0000244|PDB:3HKW}.
STRAND 2777 2779 {ECO:0000244|PDB:3HKW}.
HELIX 2780 2782 {ECO:0000244|PDB:3HKW}.
STRAND 2788 2794 {ECO:0000244|PDB:3HKW}.
STRAND 2800 2806 {ECO:0000244|PDB:3HKW}.
HELIX 2809 2820 {ECO:0000244|PDB:3HKW}.
HELIX 2827 2835 {ECO:0000244|PDB:3HKW}.
HELIX 2839 2843 {ECO:0000244|PDB:3HKW}.
HELIX 2845 2855 {ECO:0000244|PDB:3HKW}.
STRAND 2863 2867 {ECO:0000244|PDB:3HKW}.
STRAND 2870 2874 {ECO:0000244|PDB:3HKW}.
HELIX 2876 2878 {ECO:0000244|PDB:3HKW}.
HELIX 2879 2887 {ECO:0000244|PDB:3HKW}.
HELIX 2889 2892 {ECO:0000244|PDB:3HKW}.
HELIX 2899 2912 {ECO:0000244|PDB:3HKW}.
HELIX 2917 2933 {ECO:0000244|PDB:3HKW}.
HELIX 2936 2945 {ECO:0000244|PDB:3HKW}.
HELIX 2947 2949 {ECO:0000244|PDB:3HKW}.
HELIX 2960 2964 {ECO:0000244|PDB:3HKW}.
TURN 2968 2971 {ECO:0000244|PDB:3HKW}.
STRAND 2972 2975 {ECO:0000244|PDB:3QGI}.
SEQUENCE 3011 AA; 327202 MW; 65F8C9447FCE5AF9 CRC64;
MSTNPKPQKK NKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTVPAS AYQVRNSTGL YHVTNDCPNS SIVYEAADAI LHTPGCVPCV REGNASRCWV
AMTPTVATRD GKLPATQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRRHWT
TQGCNCSIYP GHITGHRMAW DMMMNWSPTT ALVMAQLLRI PQAILDMIAG AHWGVLAGIA
YFSMVGNWAK VLVVLLLFAG VDAETHVTGG SAGHTVSGFV SLLAPGAKQN VQLINTNGSW
HLNSTALNCN DSLNTGWLAG LFYHHKFNSS GCPERLASCR PLTDFDQGWG PISYANGSGP
DQRPYCWHYP PKPCGIVPAK SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ENDTDVFVLN
NTRPPLGNWF GCTWMNSTGF TKVCGAPPCV IGGAGNNTLH CPTDCFRKHP DATYSRCGSG
PWITPRCLVD YPYRLWHYPC TINYTIFKIR MYVGGVEHRL EAACNWTRGE RCDLEDRDRS
ELSPLLLTTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGVGSSIA SWAIKWEYVV
LLFLLLADAR VCSCLWMMLL ISQAEAALEN LVILNAASLA GTHGLVSFLV FFCFAWYLKG
KWVPGAVYTF YGMWPLLLLL LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIS
WCLWWLQYFL TRVEAQLHVW IPPLNVRGGR DAVILLMCAV HPTLVFDITK LLLAVFGPLW
ILQASLLKVP YFVRVQGLLR FCALARKMIG GHYVQMVIIK LGALTGTYVY NHLTPLRDWA
HNGLRDLAVA VEPVVFSQME TKLITWGADT AACGDIINGL PVSARRGREI LLGPADGMVS
KGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ IVSTAAQTFL ATCINGVCWT
VYHGAGTRTI ASPKGPVIQM YTNVDQDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPAGHAVGIF RAAVCTRGVA KAVDFIPVEN
LETTMRSPVF TDNSSPPVVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGIDPNIRT GVRTITTGSP ITYSTYGKFL ADGGCSGGAY DIIICDECHS
TDATSILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEVALSTT GEIPFYGKAI
PLEVIKGGRH LIFCHSKKKC DELAAKLVAL GINAVAYYRG LDVSVIPTSG DVVVVATDAL
MTGYTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETITLPQD AVSRTQRRGR TGRGKPGIYR
FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV CQDHLEFWEG
VFTGLTHIDA HFLSQTKQSG ENLPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEITLTHP VTKYIMTCMS ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV
VIVGRVVLSG KPAIIPDREV LYREFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS
RQAEVIAPAV QTNWQKLETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP
LTTSQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAAIG SVGLGKVLID ILAGYGAGVA
GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTAILSS LTVTQLLRRL HQWISSECTT PCSGSWLRDI
WDWICEVLSD FKTWLKAKLM PQLPGIPFVS CQRGYKGVWR VDGIMHTRCH CGAEITGHVK
NGTMRIVGPR TCRNMWSGTF PINAYTTGPC TPLPAPNYTF ALWRVSAEEY VEIRQVGDFH
YVTGMTTDNL KCPCQVPSPE FFTELDGVRL HRFAPPCKPL LREEVSFRVG LHEYPVGSQL
PCEPEPDVAV LTSMLTDPSH ITAEAAGRRL ARGSPPSVAS SSASQLSAPS LKATCTANHD
SPDAELIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLV AEEDEREISV PAEILRKSRR
FAQALPVWAR PDYNPPLVET WKKPDYEPPV VHGCPLPPPK SPPVPPPRKK RTVVLTESTL
STALAELATR SFGSSSTSGI TGDNTTTSSE PAPSGCPPDS DAESYSSMPP LEGEPGDPDL
SDGSWSTVSS EANAEDVVCC SMSYSWTGAL VTPCAAEEQK LPINALSNSL LRHHNLVYST
TSRSACQRQK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA NLLSVEEACS LTPPHSAKSK
FGYGAKDVRC HARKAVTHIN SVWKDLLEDN VTPIDTTIMA KNEVFCVQPE KGGRKPARLI
VFPDLGVRVC EKMALYDVVT KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGFSYD
TRCFDSTVTE SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR
ASGVLTTSCG NTLTCYIKAR AACRAAGLQD CTMLVCGDDL VVICESAGVQ EDAASLRAFT
EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR VYYLTRDPTT PLARAAWETA
RHTPVNSWLG NIIMFAPTLW ARMILMTHFF SVLIARDQLE QALDCEIYGA CYSIEPLDLP
PIIQRLHGLS AFSLHSYSPG EINRVAACLR KLGVPPLRAW RHRARSVRAR LLARGGRAAI
CGKYLFNWAV RTKLKLTPIA AAGQLDLSGW FTAGYSGGDI YHSVSHARPR WIWFCLLLLA
AGVGIYLLPN R


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