GenomeNet

Database: UniProt
Entry: Q9DHD6
LinkDB: Q9DHD6
Original site: Q9DHD6 
ID   POLG_HCVJP              Reviewed;        3033 AA.
AC   Q9DHD6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   18-SEP-2019, entry version 146.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Core protein p21;
DE     AltName: Full=Capsid protein C;
DE     AltName: Full=p21;
DE   Contains:
DE     RecName: Full=Core protein p19;
DE   Contains:
DE     RecName: Full=Envelope glycoprotein E1;
DE     AltName: Full=gp32;
DE     AltName: Full=gp35;
DE   Contains:
DE     RecName: Full=Envelope glycoprotein E2;
DE     AltName: Full=NS1;
DE     AltName: Full=gp68;
DE     AltName: Full=gp70;
DE   Contains:
DE     RecName: Full=p7;
DE   Contains:
DE     RecName: Full=Protease NS2-3;
DE              Short=p23;
DE              EC=3.4.22.-;
DE   Contains:
DE     RecName: Full=Serine protease NS3;
DE              EC=3.4.21.98;
DE              EC=3.6.1.15;
DE              EC=3.6.4.13;
DE     AltName: Full=Hepacivirin;
DE     AltName: Full=NS3P;
DE     AltName: Full=p70;
DE   Contains:
DE     RecName: Full=Non-structural protein 4A;
DE              Short=NS4A;
DE     AltName: Full=p8;
DE   Contains:
DE     RecName: Full=Non-structural protein 4B;
DE              Short=NS4B;
DE     AltName: Full=p27;
DE   Contains:
DE     RecName: Full=Non-structural protein 5A;
DE              Short=NS5A;
DE     AltName: Full=p56;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE     AltName: Full=NS5B;
DE     AltName: Full=p68;
OS   Hepatitis C virus genotype 2b (isolate JPUT971017) (HCV).
OC   Viruses; Riboviria; Flaviviridae; Hepacivirus.
OX   NCBI_TaxID=356412;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11402859; DOI=10.1007/s007050170142;
RA   Murakami K., Abe M., Kageyama T., Kamoshita N., Nomoto A.;
RT   "Down-regulation of translation driven by hepatitis C virus internal
RT   ribosomal entry site by the 3' untranslated region of RNA.";
RL   Arch. Virol. 146:729-741(2001).
RN   [2]
RP   REVIEW.
RX   PubMed=10718937; DOI=10.1046/j.1365-2893.2000.00201.x;
RA   McLauchlan J.;
RT   "Properties of the hepatitis C virus core protein: a structural
RT   protein that modulates cellular processes.";
RL   J. Viral Hepat. 7:2-14(2000).
RN   [3]
RP   REVIEW, AND SUBCELLULAR LOCATION.
RX   PubMed=14752815; DOI=10.1002/hep.20032;
RA   Penin F., Dubuisson J., Rey F.A., Moradpour D., Pawlotsky J.-M.;
RT   "Structural biology of hepatitis C virus.";
RL   Hepatology 39:5-19(2004).
RN   [4]
RP   INTERACTION WITH HNRNPA1 AND SEPT6.
RX   PubMed=17229681; DOI=10.1128/jvi.01311-06;
RA   Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.;
RT   "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6,
RT   facilitate hepatitis C virus replication.";
RL   J. Virol. 81:3852-3865(2007).
CC   -!- FUNCTION: Core protein packages viral RNA to form a viral
CC       nucleocapsid, and promotes virion budding. Modulates viral
CC       translation initiation by interacting with HCV IRES and 40S
CC       ribosomal subunit. Also regulates many host cellular functions
CC       such as signaling pathways and apoptosis. Prevents the
CC       establishment of cellular antiviral state by blocking the
CC       interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling
CC       pathways and by inducing human STAT1 degradation. Thought to play
CC       a role in virus-mediated cell transformation leading to
CC       hepatocellular carcinomas. Interacts with, and activates STAT3
CC       leading to cellular transformation. May repress the promoter of
CC       p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the
CC       cytoplasm. Also represses cell cycle negative regulating factor
CC       CDKN1A, thereby interrupting an important check point of normal
CC       cell cycle regulation. Targets transcription factors involved in
CC       the regulation of inflammatory responses and in the immune
CC       response: suppresses NK-kappaB activation, and activates AP-1.
CC       Could mediate apoptotic pathways through association with TNF-type
CC       receptors TNFRSF1A and LTBR, although its effect on death
CC       receptor-induced apoptosis remains controversial. Enhances TRAIL
CC       mediated apoptosis, suggesting that it might play a role in
CC       immune-mediated liver cell injury. Seric core protein is able to
CC       bind C1QR1 at the T-cell surface, resulting in down-regulation of
CC       T-lymphocytes proliferation. May transactivate human MYC, Rous
CC       sarcoma virus LTR, and SV40 promoters. May suppress the human FOS
CC       and HIV-1 LTR activity. Alters lipid metabolism by interacting
CC       with hepatocellular proteins involved in lipid accumulation and
CC       storage. Core protein induces up-regulation of FAS promoter
CC       activity, and thereby probably contributes to the increased
CC       triglyceride accumulation in hepatocytes (steatosis) (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: E1 and E2 glycoproteins form a heterodimer that is
CC       involved in virus attachment to the host cell, virion
CC       internalization through clathrin-dependent endocytosis and fusion
CC       with host membrane. E1/E2 heterodimer binds to human LDLR, CD81
CC       and SCARB1/SR-BI receptors, but this binding is not sufficient for
CC       infection, some additional liver specific cofactors may be needed.
CC       The fusion function may possibly be carried by E1. E2 inhibits
CC       human EIF2AK2/PKR activation, preventing the establishment of an
CC       antiviral state. E2 is a viral ligand for CD209/DC-SIGN and
CC       CLEC4M/DC-SIGNR, which are respectively found on dendritic cells
CC       (DCs), and on liver sinusoidal endothelial cells and macrophage-
CC       like cells of lymph node sinuses. These interactions allow capture
CC       of circulating HCV particles by these cells and subsequent
CC       transmission to permissive cells. DCs act as sentinels in various
CC       tissues where they entrap pathogens and convey them to local
CC       lymphoid tissue or lymph node for establishment of immunity.
CC       Capture of circulating HCV particles by these SIGN+ cells may
CC       facilitate virus infection of proximal hepatocytes and lymphocyte
CC       subpopulations and may be essential for the establishment of
CC       persistent infection (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: P7 seems to be a heptameric ion channel protein
CC       (viroporin) and is inhibited by the antiviral drug amantadine.
CC       Also inhibited by long-alkyl-chain iminosugar derivatives.
CC       Essential for infectivity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Protease NS2-3 is a cysteine protease responsible for
CC       the autocatalytic cleavage of NS2-NS3. Seems to undergo self-
CC       inactivation following maturation (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: NS3 displays three enzymatic activities: serine
CC       protease, NTPase and RNA helicase. NS3 serine protease, in
CC       association with NS4A, is responsible for the cleavages of NS3-
CC       NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also
CC       prevents phosphorylation of human IRF3, thus preventing the
CC       establishment of dsRNA induced antiviral state. NS3 RNA helicase
CC       binds to RNA and unwinds dsRNA in the 3' to 5' direction, and
CC       likely RNA stable secondary structure in the template strand.
CC       Cleaves and inhibits the host antiviral protein MAVS (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: NS4B induces a specific membrane alteration that serves
CC       as a scaffold for the virus replication complex. This membrane
CC       alteration gives rise to the so-called ER-derived membranous web
CC       that contains the replication complex (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: NS5A is a component of the replication complex involved
CC       in RNA-binding. Its interaction with Human VAPB may target the
CC       viral replication complex to vesicles. Down-regulates viral IRES
CC       translation initiation. Mediates interferon resistance, presumably
CC       by interacting with and inhibiting human EIF2AK2/PKR. Seems to
CC       inhibit apoptosis by interacting with BIN1 and FKBP8. The
CC       hyperphosphorylated form of NS5A is an inhibitor of viral
CC       replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: NS5B is an RNA-dependent RNA polymerase that plays an
CC       essential role in the virus replication. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of four peptide bonds in the viral precursor
CC         polyprotein, commonly with Asp or Glu in the P6 position, Cys or
CC         Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per NS3 protease domain. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per NS5A N-terminal domain. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activity of auto-protease NS2-3 is dependent
CC       on zinc ions and completely inhibited by EDTA. Serine protease NS3
CC       is also activated by zinc ions (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Core protein is a homomultimer that binds the C-terminal
CC       part of E1 and interacts with numerous cellular proteins.
CC       Interaction with human STAT1 SH2 domain seems to result in
CC       decreased STAT1 phosphorylation, leading to decreased IFN-
CC       stimulated gene transcription. In addition to blocking the
CC       formation of phosphorylated STAT1, the core protein also promotes
CC       ubiquitin-mediated proteasome-dependent degradation of STAT1.
CC       Interacts with, and constitutively activates human STAT3.
CC       Associates with human LTBR and TNFRSF1A receptors and possibly
CC       induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK,
CC       C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins.
CC       Interacts with human CREB3 nuclear transcription protein,
CC       triggering cell transformation. May interact with human p53. Also
CC       binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). E1
CC       and E2 glycoproteins form a heterodimer that binds to human LDLR,
CC       CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human
CC       EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR.
CC       p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing
CC       a pair of composite active sites at the dimerization interface.
CC       NS2 seems to interact with all other non-structural (NS) proteins.
CC       NS4A interacts with NS3 serine protease and stabilizes its
CC       folding. NS3-NS4A complex is essential for the activation of the
CC       latter and allows membrane anchorage of NS3. NS3 interacts with
CC       human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form
CC       homodimers and seem to interact with all other non-structural (NS)
CC       proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2,
CC       BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B
CC       is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Core protein p21: Host endoplasmic reticulum
CC       membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000250}. Host mitochondrion membrane {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}. Host lipid droplet
CC       {ECO:0000250}. Note=The C-terminal transmembrane domain of core
CC       protein p21 contains an ER signal leading the nascent polyprotein
CC       to the ER membrane. Only a minor proportion of core protein is
CC       present in the nucleus and an unknown proportion is secreted.
CC   -!- SUBCELLULAR LOCATION: Core protein p19: Virion {ECO:0000250}. Host
CC       cytoplasm {ECO:0000250}. Host nucleus {ECO:0000250}. Secreted
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Envelope glycoprotein E1: Virion membrane
CC       {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC       Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Note=The C-terminal
CC       transmembrane domain acts as a signal sequence and forms a hairpin
CC       structure before cleavage by host signal peptidase. After
CC       cleavage, the membrane sequence is retained at the C-terminus of
CC       the protein, serving as ER membrane anchor. A reorientation of the
CC       second hydrophobic stretch occurs after cleavage producing a
CC       single reoriented transmembrane domain. These events explain the
CC       final topology of the protein. ER retention of E1 is leaky and, in
CC       overexpression conditions, only a small fraction reaches the
CC       plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Envelope glycoprotein E2: Virion membrane
CC       {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC       Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Note=The C-terminal
CC       transmembrane domain acts as a signal sequence and forms a hairpin
CC       structure before cleavage by host signal peptidase. After
CC       cleavage, the membrane sequence is retained at the C-terminus of
CC       the protein, serving as ER membrane anchor. A reorientation of the
CC       second hydrophobic stretch occurs after cleavage producing a
CC       single reoriented transmembrane domain. These events explain the
CC       final topology of the protein. ER retention of E2 is leaky and, in
CC       overexpression conditions, only a small fraction reaches the
CC       plasma membrane.
CC   -!- SUBCELLULAR LOCATION: p7: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
CC       cell membrane {ECO:0000250}. Note=The C-terminus of p7 membrane
CC       domain acts as a signal sequence. After cleavage by host signal
CC       peptidase, the membrane sequence is retained at the C-terminus of
CC       the protein, serving as ER membrane anchor. Only a fraction
CC       localizes to the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Protease NS2-3: Host endoplasmic reticulum
CC       membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Note=NS3 is associated to the ER membrane through
CC       its binding to NS4A.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
CC       reticulum membrane {ECO:0000305}; Single-pass type I membrane
CC       protein {ECO:0000305}. Note=Host membrane insertion occurs after
CC       processing by the NS3 protease.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
CC       reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Non-structural protein 5A: Host endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Host cytoplasm, host perinuclear region
CC       {ECO:0000250}. Host mitochondrion {ECO:0000250}. Note=Host
CC       membrane insertion occurs after processing by the NS3 protease.
CC   -!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host
CC       endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Note=Host membrane insertion
CC       occurs after processing by the NS3 protease.
CC   -!- DOMAIN: The transmembrane regions of envelope E1 and E2
CC       glycoproteins are involved in heterodimer formation, ER
CC       localization, and assembly of these proteins. Envelope E2
CC       glycoprotein contain a highly variable region called hypervariable
CC       region 1 (HVR1). E2 also contains two segments involved in CD81-
CC       binding. HVR1 is implicated in the SCARB1-mediated cell entry.
CC       CD81-binding regions may be involved in sensitivity and/or
CC       resistance to IFN-alpha therapy (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus of NS5A acts as membrane anchor. The
CC       central part of NS5A seems to be intrinsically disordered and
CC       interacts with NS5B and host PKR (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The SH3-binding domain of NS5A is involved in the
CC       interaction with human Bin1, GRB2 and Src-family kinases.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal one-third of serine protease NS3 contains
CC       the protease activity. This region contains a zinc atom that does
CC       not belong to the active site, but may play a structural rather
CC       than a catalytic role. This region is essential for the activity
CC       of protease NS2-3, maybe by contributing to the folding of the
CC       latter. The helicase activity is located in the C-terminus of NS3
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       The structural proteins, core, E1, E2 and p7 are produced by
CC       proteolytic processing by host signal peptidases. The core protein
CC       is synthesized as a 21 kDa precursor which is retained in the ER
CC       membrane through the hydrophobic signal peptide. Cleavage by the
CC       signal peptidase releases the 19 kDa mature core protein. The
CC       other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are
CC       cleaved by the viral proteases (By similarity). {ECO:0000250}.
CC   -!- PTM: Envelope E1 and E2 glycoproteins are highly N-glycosylated.
CC       {ECO:0000250}.
CC   -!- PTM: Core protein is phosphorylated by host PKC and PKA.
CC       {ECO:0000250}.
CC   -!- PTM: NS5A is phosphorylated in a basal form termed p56. p58 is a
CC       hyperphosphorylated form of p56. p56 and p58 coexist in the cell
CC       in roughly equivalent amounts. Hyperphosphorylation is dependent
CC       on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1,
CC       MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for
CC       NS5A phosphorylation (By similarity). {ECO:0000250}.
CC   -!- PTM: NS4B is palmitoylated. This modification may play a role in
CC       its polymerization or in protein-protein interactions (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: The N-terminus of a fraction of NS4B molecules seems to be
CC       relocated post-translationally from the cytoplasm to the ER lumen,
CC       with a 5th transmembrane segment. The C-terminus of NS2 may be
CC       lumenal with a fourth transmembrane segment (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Core protein is ubiquitinated; mediated by UBE3A and leading
CC       to core protein subsequent proteasomal degradation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Cell culture adaptation of the virus leads to
CC       mutations in NS5A, reducing its inhibitory effect on replication.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Core protein exerts viral interference on hepatitis
CC       B virus when HCV and HBV coinfect the same cell, by suppressing
CC       HBV gene expression, RNA encapsidation and budding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The core gene probably also codes for alternative reading
CC       frame proteins (ARFPs). Many functions depicted for the core
CC       protein might belong to the ARFPs. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Virus Pathogen Resource;
CC       URL="http://www.viprbrc.org/brc/home.spg?decorator=flavi_hcv";
DR   EMBL; AB030907; BAB08107.1; -; Genomic_RNA.
DR   SMR; Q9DHD6; -.
DR   DrugCentral; Q9DHD6; -.
DR   PRIDE; Q9DHD6; -.
DR   euHCVdb; AB030907; -.
DR   Proteomes; UP000008098; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1280.150; -; 1.
DR   Gene3D; 2.20.25.210; -; 1.
DR   Gene3D; 2.20.25.220; -; 1.
DR   Gene3D; 2.30.30.710; -; 1.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR002521; HCV_core_C.
DR   InterPro; IPR002522; HCV_core_N.
DR   InterPro; IPR002519; HCV_env.
DR   InterPro; IPR002531; HCV_NS1.
DR   InterPro; IPR002518; HCV_NS2.
DR   InterPro; IPR042205; HCV_NS2_C.
DR   InterPro; IPR042209; HCV_NS2_N.
DR   InterPro; IPR000745; HCV_NS4a.
DR   InterPro; IPR001490; HCV_NS4b.
DR   InterPro; IPR002868; HCV_NS5a.
DR   InterPro; IPR013193; HCV_NS5a_1B_dom.
DR   InterPro; IPR038568; HCV_NS5A_1B_sf.
DR   InterPro; IPR024350; HCV_NS5a_C.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR013192; NS5A_1a.
DR   InterPro; IPR038170; NS5A_1a_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR004109; Peptidase_S29_NS3.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF01543; HCV_capsid; 1.
DR   Pfam; PF01542; HCV_core; 1.
DR   Pfam; PF01539; HCV_env; 1.
DR   Pfam; PF01560; HCV_NS1; 1.
DR   Pfam; PF01538; HCV_NS2; 1.
DR   Pfam; PF01006; HCV_NS4a; 1.
DR   Pfam; PF01001; HCV_NS4b; 1.
DR   Pfam; PF01506; HCV_NS5a; 1.
DR   Pfam; PF08300; HCV_NS5a_1a; 1.
DR   Pfam; PF08301; HCV_NS5a_1b; 1.
DR   Pfam; PF12941; HCV_NS5a_C; 1.
DR   Pfam; PF02907; Peptidase_S29; 1.
DR   Pfam; PF00998; RdRP_3; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51693; HCV_NS2_PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51822; HV_PV_NS3_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activation of host autophagy by virus; Apoptosis;
KW   ATP-binding; Capsid protein;
KW   Clathrin-mediated endocytosis of virus by host; Complete proteome;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane;
KW   G1/S host cell cycle checkpoint dysregulation by virus; Glycoprotein;
KW   Helicase; Host cell membrane; Host cytoplasm;
KW   Host endoplasmic reticulum; Host lipid droplet; Host membrane;
KW   Host mitochondrion; Host nucleus; Host-virus interaction; Hydrolase;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host MAVS by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Inhibition of host STAT1 by virus; Inhibition of host TRAFs by virus;
KW   Interferon antiviral system evasion; Ion channel; Ion transport;
KW   Lipoprotein; Membrane; Metal-binding;
KW   Modulation of host cell cycle by virus; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Oncogene; Palmitate;
KW   Phosphoprotein; Protease; Ribonucleoprotein; RNA-binding;
KW   RNA-directed RNA polymerase; Secreted; Serine protease; SH3-binding;
KW   Thiol protease; Transcription; Transcription regulation; Transferase;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral immunoevasion; Viral ion channel; Viral nucleoprotein;
KW   Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW   Virus endocytosis by host; Virus entry into host cell; Zinc.
FT   INIT_MET      1      1       Removed; by host. {ECO:0000250}.
FT   CHAIN         2    191       Core protein p21. {ECO:0000255}.
FT                                /FTId=PRO_0000045628.
FT   CHAIN         2    177       Core protein p19. {ECO:0000250}.
FT                                /FTId=PRO_0000045629.
FT   PROPEP      178    191       ER anchor for the core protein, removed
FT                                in mature form by host signal peptidase.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000045630.
FT   CHAIN       192    383       Envelope glycoprotein E1. {ECO:0000255}.
FT                                /FTId=PRO_0000045631.
FT   CHAIN       384    750       Envelope glycoprotein E2. {ECO:0000255}.
FT                                /FTId=PRO_0000045632.
FT   CHAIN       751    813       p7. {ECO:0000250}.
FT                                /FTId=PRO_0000045633.
FT   CHAIN       814   1030       Protease NS2-3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01030}.
FT                                /FTId=PRO_0000045634.
FT   CHAIN      1031   1661       Serine protease NS3. {ECO:0000255}.
FT                                /FTId=PRO_0000045635.
FT   CHAIN      1662   1715       Non-structural protein 4A. {ECO:0000255}.
FT                                /FTId=PRO_0000045636.
FT   CHAIN      1716   1976       Non-structural protein 4B. {ECO:0000255}.
FT                                /FTId=PRO_0000045637.
FT   CHAIN      1977   2442       Non-structural protein 5A. {ECO:0000255}.
FT                                /FTId=PRO_0000045638.
FT   CHAIN      2443   3033       RNA-directed RNA polymerase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000045639.
FT   TOPO_DOM      2    168       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    169    189       Helical. {ECO:0000255}.
FT   TOPO_DOM    190    358       Lumenal. {ECO:0000255}.
FT   TRANSMEM    359    379       Helical. {ECO:0000255}.
FT   TOPO_DOM    380    729       Lumenal. {ECO:0000255}.
FT   TRANSMEM    730    750       Helical. {ECO:0000255}.
FT   TOPO_DOM    751    761       Lumenal. {ECO:0000255}.
FT   TRANSMEM    762    782       Helical. {ECO:0000255}.
FT   TOPO_DOM    783    786       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    787    807       Helical. {ECO:0000255}.
FT   TOPO_DOM    808    817       Lumenal. {ECO:0000255}.
FT   TRANSMEM    818    838       Helical. {ECO:0000255}.
FT   TOPO_DOM    839    885       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    886    906       Helical. {ECO:0000255}.
FT   TOPO_DOM    907    932       Lumenal. {ECO:0000255}.
FT   TRANSMEM    933    953       Helical. {ECO:0000255}.
FT   TOPO_DOM    954   1661       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1662   1682       Helical. {ECO:0000255}.
FT   TOPO_DOM   1683   1809       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1810   1830       Helical. {ECO:0000255}.
FT   TOPO_DOM   1831   1832       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1833   1853       Helical. {ECO:0000255}.
FT   TOPO_DOM   1854   1854       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1855   1875       Helical. {ECO:0000255}.
FT   TOPO_DOM   1876   1885       Lumenal. {ECO:0000255}.
FT   TRANSMEM   1886   1906       Helical. {ECO:0000255}.
FT   TOPO_DOM   1907   1976       Cytoplasmic. {ECO:0000255}.
FT   INTRAMEM   1977   2006       {ECO:0000250}.
FT   TOPO_DOM   2007   3012       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   3013   3033       Helical. {ECO:0000250}.
FT   DOMAIN      907   1030       Peptidase C18. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01030}.
FT   DOMAIN     1031   1212       Peptidase S29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   DOMAIN     1221   1373       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     2656   2774       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1234   1241       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        2     59       Interaction with DDX3X. {ECO:0000250}.
FT   REGION        2     23       Interaction with STAT1. {ECO:0000250}.
FT   REGION      122    173       Interaction with APOA2. {ECO:0000250}.
FT   REGION      150    159       Mitochondrial targeting signal.
FT                                {ECO:0000250}.
FT   REGION      164    167       Important for lipid droplets
FT                                localization. {ECO:0000250}.
FT   REGION      265    296       Fusion peptide. {ECO:0000255}.
FT   REGION      385    411       HVR1. {ECO:0000250}.
FT   REGION      484    496       CD81-binding 1. {ECO:0000255}.
FT   REGION      524    555       CD81-binding 2. {ECO:0000255}.
FT   REGION      664    675       PKR/eIF2-alpha phosphorylation homology
FT                                domain (PePHD). {ECO:0000250}.
FT   REGION     1683   1694       NS3-binding (by NS4A). {ECO:0000255}.
FT   REGION     2124   2332       Transcriptional activation.
FT                                {ECO:0000255}.
FT   REGION     2124   2212       FKBP8-binding. {ECO:0000255}.
FT   REGION     2204   2250       Basal phosphorylation. {ECO:0000250}.
FT   REGION     2214   2275       PKR-binding. {ECO:0000255}.
FT   REGION     2249   2306       NS4B-binding. {ECO:0000255}.
FT   REGION     2351   2442       Basal phosphorylation. {ECO:0000250}.
FT   MOTIF         5     13       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF        38     43       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF        58     64       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF        66     71       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF      1320   1323       DECH box. {ECO:0000250}.
FT   MOTIF      2322   2325       SH3-binding. {ECO:0000255}.
FT   MOTIF      2327   2335       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS   1436   1439       Poly-Val.
FT   COMPBIAS   2282   2327       Pro-rich.
FT   COMPBIAS   2328   2333       Poly-Arg.
FT   COMPBIAS   3013   3021       Poly-Leu.
FT   ACT_SITE    956    956       For protease NS2-3 activity; shared with
FT                                dimeric partner. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01030}.
FT   ACT_SITE    976    976       For protease NS2-3 activity; shared with
FT                                dimeric partner. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01030}.
FT   ACT_SITE    997    997       For protease NS2-3 activity; shared with
FT                                dimeric partner. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01030}.
FT   ACT_SITE   1087   1087       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   ACT_SITE   1111   1111       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   ACT_SITE   1169   1169       Charge relay system; for serine protease
FT                                NS3 activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   METAL      1127   1127       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   METAL      1129   1129       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   METAL      1175   1175       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   METAL      1179   1179       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01166}.
FT   METAL      2015   2015       Zinc. {ECO:0000250}.
FT   METAL      2033   2033       Zinc. {ECO:0000250}.
FT   METAL      2035   2035       Zinc. {ECO:0000250}.
FT   METAL      2056   2056       Zinc. {ECO:0000250}.
FT   SITE        177    178       Cleavage; by host signal peptidase.
FT                                {ECO:0000250}.
FT   SITE       ?191   ?192       Cleavage; by host signal peptidase.
FT                                {ECO:0000255}.
FT   SITE        383    384       Cleavage; by host signal peptidase.
FT                                {ECO:0000255}.
FT   SITE        750    751       Cleavage; by host signal peptidase.
FT                                {ECO:0000250}.
FT   SITE        813    814       Cleavage; by host signal peptidase.
FT                                {ECO:0000250}.
FT   SITE       1030   1031       Cleavage; by protease NS2-3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01030}.
FT   SITE       1661   1662       Cleavage; by serine protease NS3.
FT                                {ECO:0000255}.
FT   SITE       1715   1716       Cleavage; by serine protease NS3.
FT                                {ECO:0000255}.
FT   SITE       1976   1977       Cleavage; by serine protease NS3.
FT                                {ECO:0000255}.
FT   SITE       2442   2443       Cleavage; by serine protease NS3.
FT                                {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylserine; by host. {ECO:0000250}.
FT   MOD_RES      53     53       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES      99     99       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES     116    116       Phosphoserine; by host PKA.
FT                                {ECO:0000250}.
FT   MOD_RES    2198   2198       Phosphoserine; by host; in p56.
FT                                {ECO:0000250}.
FT   MOD_RES    2201   2201       Phosphoserine; by host; in p58.
FT                                {ECO:0000250}.
FT   MOD_RES    2205   2205       Phosphoserine; by host; in p58.
FT                                {ECO:0000250}.
FT   MOD_RES    2208   2208       Phosphoserine; by host; in p58.
FT                                {ECO:0000250}.
FT   LIPID      1972   1972       S-palmitoyl cysteine; by host.
FT                                {ECO:0000250}.
FT   LIPID      1976   1976       S-palmitoyl cysteine; by host.
FT                                {ECO:0000250}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    209    209       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    299    299       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    305    305       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    423    423       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    448    448       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    477    477       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    534    534       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    542    542       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    558    558       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    649    649       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   DISULFID   2118   2166       {ECO:0000250}.
SQ   SEQUENCE   3033 AA;  329985 MW;  6B183FED090872B4 CRC64;
     MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
     RRQPIPKDRR STGKSWGKPG YPWPLYGNEG CGWAGWLLSP RGSRPTWGPS DPRHRSRNLG
     RVIDTITCGF ADLMGYIPVV GAPVGGVARA LAHGVRVLED GINYATRNLP GCSFSIFLLA
     LLSCVTVPVS SVEIRNISTS YYATNDCSNN SITWQLTNAV LHLPGCVPCE NDNGTLRCWI
     QVTPNVAVKH RGALTHNLRA HVDVIVMAAT VCSALYVGDV CGAVMIVSQA LIVSPERHNF
     TQECNCSIYQ GHITGQRMAW DMMLNWSPTL TMILAYAARV PELVLEIVFG GHWGVVFGLA
     YFSMQGAWAK VIAILLLVAG VDATTYSTGA TVGRTVGSFA GLFKLGAQQN VQLINTNGSW
     HINRTALNCN DSLHTGFMAA LFYANKFNSS GCPERLSSCR GLDDFRIGWG TLEYETNVTN
     VEDMRPYCWH YPPKPCGIVP AQSVCGPVYC FTPSPVVVGT TDRQGVPTYN WGDNETDVFL
     LNSTRPPRGA WFGCTWMNGT GFTKTCGAPP CRIRKDFNST LDLLCPTDCF RKHPDATYVK
     CGAGPWLTPR CLIDYPYRLW HYPCTVNFTI FKVRMYVGGV EHRFSAACNF TRGDRCRLED
     RDRGQQSPLL HSTTEWAVLP CSFSDLPALS TGLLHLHQNI VDVQYLYGLS PAVTKYIVKW
     EWVVLLFLLL ADARICACLW MLIILGQAEA ALEKLIILHS ASAASANGPL WFFIFFTAAW
     YLKGRVVPAA TYSVLGLWSF LLLVLALPQQ AYALDAAEQG ELGLVILMII SIFTLTPAYK
     ILLSRSVWWL SYMLVLAEAQ VQQWVPPLEA RGGRDGIIWV AVILHPHLVF EVTKWLLAIL
     GSAYLLKASL LRVPYFVRAH ALLRVCTLVR HLAGARYIQM LLITMGRWTG TYIYDHLSPL
     STWAAQGLRD LAVAVEPVVF SPMEKKVIVW GAETVACGDI LHGLPVSARL GREVLLGPAD
     GYTSKGWKLL APITAYTQQT RGLLGAIVVS LTGRDKNEQA GQVQVLSSVT QSFLGTSISG
     VLWTVYHGAG NKTLASPRGP VTQMYTSAEG DLVGWPSPPG TKSLDPCTCG AVDLYLVTRN
     ADVIPVRRKD DRRGALLSPR PLSTLKGSSG GPVLCPRGHA VGLFRAAVCA RGVAKSIDFI
     PVESLDIARR TPSFSDNSTP PAVPQTYQVG YLHAPTGSGK STKVPAAYTS QGYKVLVLNP
     SVAATLGFGA YMSKAHGINP NIRTGVRTVT TGDSITYSTY GKFLADGGCS AGAYDIIICD
     ECHSVDATTI LGIGTVLDQA ETAGVRLVVL ATATPPGTVT TPHANIEEVA LGHEGEIPFY
     GKAIPLASIK GGRHLIFCHS KKKCDELAAA LRGMGVNAVA YYRGLDVSVI PTQGDVVVVA
     TDALMTGYTG DFDSVIDCNV AVTQIVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRL
     GTYRYVSSGE RPSGMFDSVV LCECYDAGAA WYELTPAETT VRLRAYFNTP GLPVCQDHLE
     FWEAVFTGLT HIDAHFLSQT KQGGDNFAYL TAYQATVCAR AKAPPPSWDV MWKCLTRLKP
     TLTGPTPLLY RLGAVTNEIT LTHPVTKYIA TCMQADLEVM TSTWVLAGGV LAAVAAYCLA
     TGCISIIGRI HLNDQVVVAP DKEILYEAFD EMEECASKAA LIEEGQRMAE MLKSKILGLL
     QQATKQAQDI QPAMQSSWPK IEQFWARHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
     LTSPLPTSTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK ILVDVLAGYG
     AGISGALVAF KIMSGEKPSV EDVVNLLPAI LSPGALVVGV ICAAILRRHV GQGEGAVQWM
     NRLIAFASRG NHVAPTHYVA ESDASLRVTQ VLSSLTITSL LRRLHAWITE DCPVPCSGSW
     LRDIWEWVCS ILTDFKNWLS AKLLPKMPGL PFISCQKGYR GVWAGTGVMT TRCSCGANIS
     GHVRLGTMKI TGPKTCLNMW QGTFPINCYT EGPCVPKPPP NYKTAIWRVA ASEYVEVTQH
     GSFSYVTGLT SDNLKVPCQV PAPEFFSWVD GVQIHRFAPT PGPFFRDEVT FTVGLNSLVV
     GSQLPCDPEP DTEVLASMLT DPSHITAETA ARRLARGSPP SQASSSASQL SAPSLKATCT
     THKTAYDCDM VDANLFMGGD VTRIESDSKV IVLDSLDSMT EVEDDREPSV PSEYLTRRRK
     FPPALPPWAR PDYNPPVIET WKRPDYEPPT VLGCALPPTP QAPVPPPRRR RARVLTQDNV
     EGVLREMADK VLSPLQDTND SGHSTGADTG GDSVQQPSGE TAASDAGSLS SMPPLEGEPG
     DPDLEFEPAR SAPPSEGECE VIDSDSKSWS TVSDQEDSVI CCSMSYSWTG ALITPCGPEE
     EKLPISPLSN SLMRFHNKVY STTSRSASLR AKKVTFDRVQ VLDAHYDSVL QDVKRAASKV
     SARLLSVEEA CALTPPHSAK SRYGFGAKEV RSLSRGAVNH IRSVWEDLLE DQHTPIDTTA
     MAKNEVFCID PAKGGKKPAR LIVYPDLGVR VCEKMALYDI AQKLPKAIMG PSYGFQYSPA
     ERVDFLLKAW GSKKDPMGFS YDTRCFDSTV TERDIRTEES IYQACSLPQE ARTVIHSITE
     RLYVGGPMTN SKGQSCGYRR CRASGVFTTS MGNTMTCYIK ALAACKAAGI VDPTMLVCGD
     DLVVISESQG NEEDERNLRA FTEAMTRYSA PPGDLPRPEY DLELITSCSS NVSVALDSRG
     RRRYFLTRDP TTPITRAAWE TVRHSPVNSW LGNIIQYAPT IWVRMVIMTH FFSILLAQDT
     LNQNLNFEMY GAVYSVNPLD LPAIIERLHG LDAFSLHTYS PHELSRVAAT LRKLGAPPLR
     AWKSRARAVR ASLIIQGGRA ATCGRYLFNW AVKTKLKLTP LPEASRLDLS GWFTVGAGGG
     DIFHSVSHAR PRLLLLCLLL LSVGVGIFLL PAR
//
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