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UniProtKB - O39929 (POLG_HCVED)

Entry version 149 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 4a (isolate ED43) (HCV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity
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).By similarity
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).By similarity
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity).By similarity
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).By similarity
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).By similarity
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).By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Miscellaneous

Cell culture adaptation of the virus leads to mutations in NS5A, reducing its inhibitory effect on replication.By similarity
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.By similarity

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.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • 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'. EC:3.4.21.98

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei952For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei972For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei993For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei1083Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1107Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1123ZincPROSITE-ProRule annotation1
Metal bindingi1125ZincPROSITE-ProRule annotation1
Active sitei1165Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Metal bindingi1171ZincPROSITE-ProRule annotation1
Metal bindingi1175ZincPROSITE-ProRule annotation1
Metal bindingi2029ZincBy similarity1
Metal bindingi2031ZincBy similarity1
Metal bindingi2052ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1230 – 1237ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Multifunctional enzyme, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-binding, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel, Viral nucleoprotein
Biological processActivation of host autophagy by virus, Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, G1/S host cell cycle checkpoint dysregulation by virus, Host-virus interaction, 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 transport, Modulation of host cell cycle by virus, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPS protease database

More...MEROPSi		C18.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Core protein p21
Alternative name(s):
Capsid protein C
p21
Core protein p19
Envelope glycoprotein E1
Alternative name(s):
gp32
gp35
Envelope glycoprotein E2
Alternative name(s):
NS1
gp68
gp70
p7
Protease NS2-3 (EC:3.4.22.-)
Short name:
p23
Serine protease NS3 (EC:3.4.21.98, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Hepacivirin
NS3P
p70
Non-structural protein 4A
Short name:
NS4A
Alternative name(s):
p8
Non-structural protein 4B
Short name:
NS4B
Alternative name(s):
p27
Non-structural protein 5A
Short name:
NS5A
Alternative name(s):
p56
RNA-directed RNA polymerase (EC:2.7.7.48)
Alternative name(s):
NS5B
p68
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHepatitis C virus genotype 4a (isolate ED43) (HCV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri356418 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Hepacivirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007415 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Core protein p21 :
Core protein p19 :
Envelope glycoprotein E1 :
  • Virion membrane Curated; Single-pass type I membrane protein Curated
  • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
    • 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.
Envelope glycoprotein E2 :
  • Virion membrane Curated; Single-pass type I membrane protein Curated
  • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
    • 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.
p7 :
Protease NS2-3 :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
Non-structural protein 5A :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 168CytoplasmicSequence analysisAdd BLAST167
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 358LumenalSequence analysisAdd BLAST169
Transmembranei359 – 379HelicalSequence analysisAdd BLAST21
Topological domaini380 – 725LumenalSequence analysisAdd BLAST346
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 757LumenalSequence analysisAdd BLAST11
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 782CytoplasmicSequence analysis4
Transmembranei783 – 803HelicalSequence analysisAdd BLAST21
Topological domaini804 – 813LumenalSequence analysis10
Transmembranei814 – 834HelicalSequence analysisAdd BLAST21
Topological domaini835 – 881CytoplasmicSequence analysisAdd BLAST47
Transmembranei882 – 902HelicalSequence analysisAdd BLAST21
Topological domaini903 – 928LumenalSequence analysisAdd BLAST26
Transmembranei929 – 949HelicalSequence analysisAdd BLAST21
Topological domaini950 – 1657CytoplasmicSequence analysisAdd BLAST708
Transmembranei1658 – 1678HelicalSequence analysisAdd BLAST21
Topological domaini1679 – 1805CytoplasmicSequence analysisAdd BLAST127
Transmembranei1806 – 1826HelicalSequence analysisAdd BLAST21
Topological domaini1827 – 1828LumenalSequence analysis2
Transmembranei1829 – 1849HelicalSequence analysisAdd BLAST21
Topological domaini1850CytoplasmicSequence analysis1
Transmembranei1851 – 1871HelicalSequence analysisAdd BLAST21
Topological domaini1872 – 1881LumenalSequence analysis10
Transmembranei1882 – 1902HelicalSequence analysisAdd BLAST21
Topological domaini1903 – 1972CytoplasmicSequence analysisAdd BLAST70
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1973 – 2002By similarityAdd BLAST30
Topological domaini2003 – 2987CytoplasmicSequence analysisAdd BLAST985
Transmembranei2988 – 3008HelicalBy similarityAdd BLAST21

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host endoplasmic reticulum, Host lipid droplet, Host membrane, Host mitochondrion, Host nucleus, Membrane, Secreted, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Oncogene

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000455322 – 191Core protein p21Sequence analysisAdd BLAST190
ChainiPRO_00000455332 – 177Core protein p19By similarityAdd BLAST176
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000045534178 – 191ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityAdd BLAST14
ChainiPRO_0000045535192 – 383Envelope glycoprotein E1Sequence analysisAdd BLAST192
ChainiPRO_0000045536384 – 746Envelope glycoprotein E2Sequence analysisAdd BLAST363
ChainiPRO_0000045537747 – 809p7By similarityAdd BLAST63
ChainiPRO_0000045538810 – 1026Protease NS2-3PROSITE-ProRule annotationAdd BLAST217
ChainiPRO_00000455391027 – 1657Serine protease NS3Sequence analysisAdd BLAST631
ChainiPRO_00000455401658 – 1711Non-structural protein 4ASequence analysisAdd BLAST54
ChainiPRO_00000455411712 – 1972Non-structural protein 4BSequence analysisAdd BLAST261
ChainiPRO_00000455421973 – 2417Non-structural protein 5ASequence analysisAdd BLAST445
ChainiPRO_00000455432418 – 3008RNA-directed RNA polymeraseSequence analysisAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine; by hostBy similarity1
Modified residuei53Phosphoserine; by hostBy similarity1
Modified residuei99Phosphoserine; by hostBy similarity1
Modified residuei116Phosphoserine; by host PKABy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi196N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi209N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi305N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi417N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi423N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi430N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi476N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi533N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi541N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi557N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi576N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi623N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi645N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi1968S-palmitoyl cysteine; by hostBy similarity1
Lipidationi1972S-palmitoyl cysteine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi2114 ↔ 2162By similarity
Modified residuei2194Phosphoserine; by host; in p56By similarity1
Modified residuei2197Phosphoserine; by host; in p58By similarity1
Modified residuei2201Phosphoserine; by host; in p58By similarity1
Modified residuei2204Phosphoserine; by host; in p58By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity
Envelope E1 and E2 glycoproteins are highly N-glycosylated.By similarity
Core protein is phosphorylated by host PKC and PKA.By similarity
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).By similarity
NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions (By similarity).By similarity
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).By similarity
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei177 – 178Cleavage; by host signal peptidaseBy similarity2
Sitei191 – 192Cleavage; by host signal peptidaseSequence analysis2
Sitei383 – 384Cleavage; by host signal peptidaseSequence analysis2
Sitei746 – 747Cleavage; by host signal peptidaseBy similarity2
Sitei809 – 810Cleavage; by host signal peptidaseBy similarity2
Sitei1026 – 1027Cleavage; by protease NS2-3PROSITE-ProRule annotation2
Sitei1657 – 1658Cleavage; by serine protease NS3Sequence analysis2
Sitei1711 – 1712Cleavage; by serine protease NS3Sequence analysis2
Sitei1972 – 1973Cleavage; by serine protease NS3Sequence analysis2
Sitei2417 – 2418Cleavage; by serine protease NS3Sequence analysis2

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		O39929

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O39929

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O39929

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini903 – 1026Peptidase C18PROSITE-ProRule annotationAdd BLAST124
Domaini1027 – 1208Peptidase S29PROSITE-ProRule annotationAdd BLAST182
Domaini1217 – 1369Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini2631 – 2749RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 59Interaction with DDX3XBy similarityAdd BLAST58
Regioni2 – 23Interaction with STAT1By similarityAdd BLAST22
Regioni122 – 173Interaction with APOA2By similarityAdd BLAST52
Regioni150 – 159Mitochondrial targeting signalBy similarity10
Regioni164 – 167Important for lipid droplets localizationBy similarity4
Regioni265 – 296Fusion peptideSequence analysisAdd BLAST32
Regioni385 – 411HVR1By similarityAdd BLAST27
Regioni483 – 495CD81-binding 1Sequence analysisAdd BLAST13
Regioni523 – 554CD81-binding 2Sequence analysisAdd BLAST32
Regioni660 – 671PKR/eIF2-alpha phosphorylation homology domain (PePHD)By similarityAdd BLAST12
Regioni1679 – 1690NS3-binding (by NS4A)Sequence analysisAdd BLAST12
Regioni2120 – 2329Transcriptional activationSequence analysisAdd BLAST210
Regioni2120 – 2208FKBP8-bindingSequence analysisAdd BLAST89
Regioni2200 – 2246Basal phosphorylationBy similarityAdd BLAST47
Regioni2210 – 2272PKR-bindingSequence analysisAdd BLAST63
Regioni2245 – 2303NS4B-bindingSequence analysisAdd BLAST59
Regioni2348 – 2417Basal phosphorylationBy similarityAdd BLAST70

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi5 – 13Nuclear localization signalSequence analysis9
Motifi38 – 43Nuclear localization signalSequence analysis6
Motifi58 – 64Nuclear localization signalSequence analysis7
Motifi66 – 71Nuclear localization signalSequence analysis6
Motifi1316 – 1319DECH box; atypicalBy similarity4
Motifi2319 – 2322SH3-bindingSequence analysis4
Motifi2325 – 2333Nuclear localization signalSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi784 – 790Poly-Ala7
Compositional biasi798 – 803Poly-Leu6
Compositional biasi2274 – 2324Pro-richAdd BLAST51

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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 a highly variable region called hypervariable region 1 (HVR1). E2 also contains two segments involved in CD81-binding. HVR1 is implicated in the SCARB1-mediated cell entry. CD81-binding regions may be involved in sensitivity and/or resistance to IFN-alpha therapy (By similarity).By similarity
The N-terminus of NS5A act as membrane anchor. The central part of NS5A seems to be intrinsically disordered and interacts with NS5B and host PKR (By similarity).By similarity
The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases.By similarity
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).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

KEGG Orthology (KO)

More...KOi		K19358

Family and domain databases

Conserved Domains Database

More...CDDi		cd00079 HELICc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.20.25.210, 1 hit
2.20.25.220, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002521 HCV_core_C
IPR002522 HCV_core_N
IPR002519 HCV_env
IPR002531 HCV_NS1
IPR002518 HCV_NS2
IPR000745 HCV_NS4a
IPR001490 HCV_NS4b
IPR002868 HCV_NS5a
IPR013193 HCV_NS5a_1B_dom
IPR038568 HCV_NS5A_1B_sf
IPR024350 HCV_NS5a_C
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR013192 NS5A_1a
IPR038170 NS5A_1a_sf
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR004109 Peptidase_S29_NS3
IPR007094 RNA-dir_pol_PSvirus
IPR002166 RNA_pol_HCV

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01543 HCV_capsid, 1 hit
PF01542 HCV_core, 1 hit
PF01539 HCV_env, 1 hit
PF01560 HCV_NS1, 1 hit
PF01538 HCV_NS2, 1 hit
PF01006 HCV_NS4a, 1 hit
PF01001 HCV_NS4b, 1 hit
PF01506 HCV_NS5a, 1 hit
PF08300 HCV_NS5a_1a, 1 hit
PF08301 HCV_NS5a_1b, 1 hit
PF12941 HCV_NS5a_C, 1 hit
PF02907 Peptidase_S29, 1 hit
PF00998 RdRP_3, 1 hit

ProDom; a protein domain database

More...ProDomi		View protein in ProDom or Entries sharing at least one domain
PD001388 HCV_env, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487 DEXDc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51693 HCV_NS2_PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51822 HV_PV_NS3_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O39929-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPM DVKFPGGGQI VGGVYLLPRR GPRLGVRATR 
        60         70         80         90        100
KTSERSQPRG RRQPIPKARR PEGRSWAQPG YPWPLYGNEG CGWAGWLLSP 
       110        120        130        140        150
RGSRPSWGPN DPRGRSRNLG KVIDTLTCGF ADLMGYIPLV GAPVGSVARA 
       160        170        180        190        200
LAHGVRALED GINYATGNLP GCSFSIFLLA LLSCLTVPAS AVNYRNVSGI 
       210        220        230        240        250
YHVTNDCPNS SIVYEADHHI MHLPGCVPCV REGNQSRCWV ALTPTVAAPY 
       260        270        280        290        300
IGAPLESLRS HVDLMVGAAT VCSGLYIGDL CGGLFLVGQM FSFRPRRHWT 
       310        320        330        340        350
TQDCNCSIYT GHITGHRMAW DMMMNWSPTT TLVLAQVMRI PTTLVDLLSG 
       360        370        380        390        400
GHWGVLVGVA YFSMQANWAK VILVLFLFAG VDAETHVSGA AVGRSTAGLA 
       410        420        430        440        450
NLFSSGSKQN LQLINSNGSW HINRTALNCN DSLNTGFLAS LFYTHKFNSS 
       460        470        480        490        500
GCSERLACCK SLDSYGQGWG PLGVANISGS SDDRPYCWHY APRPCGIVPA 
       510        520        530        540        550
SSVCGPVYCF TPSPVVVGTT DHVGVPTYTW GENETDVFLL NSTRPPHGAW 
       560        570        580        590        600
FGCVWMNSTG FTKTCGAPPC EVNTNNGTWH CPTDCFRKHP ETTYAKCGSG 
       610        620        630        640        650
PWITPRCLID YPYRLWHFPC TANFSVFNIR TFVGGIEHRM QAACNWTRGE 
       660        670        680        690        700
VCGLEHRDRV ELSPLLLTTT AWQILPCSFT TLPALSTGLI HLHQNIVDVQ 
       710        720        730        740        750
YLYGVGSAVV SWALKWEYVV LAFLLLADAR VSAYLWMMFM VSQVEAALSN 
       760        770        780        790        800
LININAASAA GAQGFWYAIL FICIVWHVKG RFPAAAAYAA CGLWPCFLLL 
       810        820        830        840        850
LMLPERAYAY DQEVAGSLGG AIVVMLTILT LSPHYKLWLA RGLWWIQYFI 
       860        870        880        890        900
ARTEAVLHVY IPSFNVRGPR DSVIVLAVLV CPDLVFDITK YLLAILGPLH 
       910        920        930        940        950
ILQASLLRIP YFVRAQALVK ICSLLRGVVY GKYFQMVVLK SRGLTGTYIY 
       960        970        980        990       1000
DHLTPMSDWP PYGLRDLAVA LEPVVFTPME KKVIVWGADT AACGDIIRGL 
      1010       1020       1030       1040       1050
PVSARLGNEI LLGPADTETS KGWRLLAPIT AYAQQTRGLF STIVTSLTGR 
      1060       1070       1080       1090       1100
DTNENCGEVQ VLSTATQSFL GTAVNGVMWT VYHGAGAKTI SGPKGPVNQM 
      1110       1120       1130       1140       1150
YTNVDQDLVG WPAPPGVRSL APCTCGSADL YLVTRHADVI PVRRRGDTRG 
      1160       1170       1180       1190       1200
ALLSPRPISI LKGSSGGPLL CPMGHRAGIF RAAVCTRGVA KAVDFVPVES 
      1210       1220       1230       1240       1250
LETTMRSPVF TDNSTPPAVP QTYQVAHLHA PTGSGKSTKV PAAHAAQGYK 
      1260       1270       1280       1290       1300
VLVLNPSVAA TLGFGVYMSK AYGIDPNIRS GVRTITTGAP ITYSTYGKFL 
      1310       1320       1330       1340       1350
ADGGCSGGAY DIIICDECYS TDSTTILGIG TVLDQAETAG VRLTVLATAT 
      1360       1370       1380       1390       1400
PPGSVTTPHS NIEEVALPTT GEIPFYGKAI PLELIKGGRH LIFCHSKKKC 
      1410       1420       1430       1440       1450
DELARQLTSL GLNAVAYYRG LDVSVIPTSG DVVVCATDAL MTGFTGDFDS 
      1460       1470       1480       1490       1500
VIDCNTSVIQ TVDFSLDPTF SIEITTVPQD AVSRSQRRGR TGRGRLGTYR 
      1510       1520       1530       1540       1550
YVTPGERPSG MFDTAELCEC YDAGCAWYEL TPAETTTRLK AYFDTPGLPV 
      1560       1570       1580       1590       1600
CQDHLEFWES VFTGLTHIDG HFLSQTKQSG ENFPYLVAYQ ATVSAKVWLA 
      1610       1620       1630       1640       1650
PPSWDTMWKC LIRLKPTLHG PTPLLYRLGS VQNEVVLTHP ITKYIMACMS 
      1660       1670       1680       1690       1700
ADLEVVTSTW VLVGGVLAAL AAYCLSVGSV VIVGRVVLSG QPAVIPDREV 
      1710       1720       1730       1740       1750
LYQQFDEMEE CSKHLPLVEH GLQLAEQFKQ KALGLLNFAG KQAQEATPVI 
      1760       1770       1780       1790       1800
QSNFAKLEQF WANDMWNFIS GIQYLAGLST LPGNPAIASL MSFTAAVTSP 
      1810       1820       1830       1840       1850
LTTQQTLLFN ILGGWVASQI RDSDASTAFV VSGLAGAAVG SVGLGKILVD 
      1860       1870       1880       1890       1900
ILPGYGAGVR GAVVTFKIMS GEMPSTEDLV NLLPAILSPG ALVVEVVCPA 
      1910       1920       1930       1940       1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA ARRVTTILSS 
      1960       1970       1980       1990       2000
LTVTSLLRRL HKWINEDCST PCAESWLWEV WDWVLHVLSD FKTCLKAKFV 
      2010       2020       2030       2040       2050
PLMPGIPLLS WPRGYKGEWR GDGVMHTTCP CGADLAGHIK NGSMRITGPK 
      2060       2070       2080       2090       2100
TCSNTWHGTF PINAYTTGPG VPIPAPNYKF ALWRVSAEDY VEVRRVGDFH 
      2110       2120       2130       2140       2150
YVTGVTQDNI KFPCQVPAPE LFTEVDGIRI HRHAPKCKPL LRDEVSFSVG 
      2160       2170       2180       2190       2200
LNSFVVGSQL PCEPEPDVAV LTSMLTDPSH ITAESARRRL ARGSRPSLAS 
      2210       2220       2230       2240       2250
SSASQLSPRL LQATCTAPHD SPGTDLLEAN LLWGSTATRV ETDEKVIILD 
      2260       2270       2280       2290       2300
SFESCVAEQN DDREVSVAAE ILRPTKKFPP ALPIWARPDY NPPLTETWKQ 
      2310       2320       2330       2340       2350
QDYQAPTVHG CALPPAKQPP VPSPRRKRTV QLTESVVSTA LAELAAKTFG 
      2360       2370       2380       2390       2400
QSEPSSDRDT DLTTPTETTD SGPIVVDDAS DDGSYSSMPP LEGEPGDPDL 
      2410       2420       2430       2440       2450
TSDSWSTVSG SEDVVCCSMS YSWTGALVTP CAAEESKLPI SPLSNSLLRH 
      2460       2470       2480       2490       2500
HNMVYATTTR SAVTRQKKVT FDRLQVVDST YNEVLKEIKA RASRVKPRLL 
      2510       2520       2530       2540       2550
TTEEACDLTP PHSARSKFGY GKKDVRSHSR KAINHISSVW KDLLDDNNTP 
      2560       2570       2580       2590       2600
IPTTIMAKNE VFAVNPAKGG RKPARLIVYP DLGSRVCEKR ALHDVIKKTA 
      2610       2620       2630       2640       2650
LAVMGAAYGF QYSPAQRVEF LLTAWKSKND PMGFSYDTRC FDSTVTEKDI 
      2660       2670       2680       2690       2700
RVEEEVYQCC DLEPEARKVI TALTDRLYVG GPMHNSKGDL CGYRRCRATG 
      2710       2720       2730       2740       2750
VYTTSFGNTL TCYLKATAAI RAAALRDCTM LVCGDDLVVI AESDGVEEDN 
      2760       2770       2780       2790       2800
RALRAFTEAM TRYSAPPGDA PQPAYDLELI TSCSSNVSVA HDVTGKKVYY 
      2810       2820       2830       2840       2850
LTRDPETPLA RAVWETVRHT PVNSWLGNII VYAPTIWVRM ILMTHFFSIL 
      2860       2870       2880       2890       2900
QSQEALEKAL DFDMYGVTYS ITPLDLPAII QRLHGLSAFT LHGYSPHELN 
      2910       2920       2930       2940       2950
RVAGALRKLG VPPLRAWRHR ARAVRAKLIA QGGRAKICGI YLFNWAVKTK 
      2960       2970       2980       2990       3000
LKLTPLPAAA KLDLSGWFTV GAGGGDIYHS MSHARPRYLL LCLLILTVGV 

GIFLLPAR
Length:3,008
Mass (Da):327,599
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8E7FC932E27C406F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Y11604 Genomic RNA Translation: CAA72338.1

Protein sequence database of the Protein Information Resource

More...PIRi		PQ0804

NCBI Reference Sequences

More...RefSeqi		YP_001469632.1, NC_009825.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11027168

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:11027168

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11604 Genomic RNA Translation: CAA72338.1
PIRiPQ0804
RefSeqiYP_001469632.1, NC_009825.1

3D structure databases

SMRiO39929
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiO39929

Protein family/group databases

MEROPSiC18.001

Proteomic databases

PRIDEiO39929

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11027168
KEGGivg:11027168

Organism-specific databases

European Hepatitis C Virus Database

More...euHCVdbi		Y11604

Phylogenomic databases

KOiK19358

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di2.20.25.210, 1 hit
2.20.25.220, 1 hit
InterProiView protein in InterPro
IPR002521 HCV_core_C
IPR002522 HCV_core_N
IPR002519 HCV_env
IPR002531 HCV_NS1
IPR002518 HCV_NS2
IPR000745 HCV_NS4a
IPR001490 HCV_NS4b
IPR002868 HCV_NS5a
IPR013193 HCV_NS5a_1B_dom
IPR038568 HCV_NS5A_1B_sf
IPR024350 HCV_NS5a_C
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR013192 NS5A_1a
IPR038170 NS5A_1a_sf
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR004109 Peptidase_S29_NS3
IPR007094 RNA-dir_pol_PSvirus
IPR002166 RNA_pol_HCV
PfamiView protein in Pfam
PF01543 HCV_capsid, 1 hit
PF01542 HCV_core, 1 hit
PF01539 HCV_env, 1 hit
PF01560 HCV_NS1, 1 hit
PF01538 HCV_NS2, 1 hit
PF01006 HCV_NS4a, 1 hit
PF01001 HCV_NS4b, 1 hit
PF01506 HCV_NS5a, 1 hit
PF08300 HCV_NS5a_1a, 1 hit
PF08301 HCV_NS5a_1b, 1 hit
PF12941 HCV_NS5a_C, 1 hit
PF02907 Peptidase_S29, 1 hit
PF00998 RdRP_3, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001388 HCV_env, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51693 HCV_NS2_PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51822 HV_PV_NS3_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_HCVED
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O39929
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 149 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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