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P27958

- POLG_HCVH

UniProt

P27958 - POLG_HCVH

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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 1a (isolate H) (HCV)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication
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.1 Publication
P7 seems to be a heptameric ion channel protein (viroporin) and is inhibited by the antiviral drug amantadine By similarity. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity.1 Publication
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation By similarity.1 Publication
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand By similarity. Cleaves and inhibits the host antiviral protein MAVS.1 Publication
NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex. NS4B polymerization or in protein-protein interactions activity may contribute to its function in membranous web formation.1 Publication
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.1 Publication
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.1 Publication

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'.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.

Cofactori

Binds 1 zinc ion per NS3 protease domain By similarity.
Binds 1 zinc ion per NS5A N-terminal domain By similarity.

Enzyme 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. Activity is up-regulated by PKN2-mediated phosphorylation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei177 – 1782Cleavage; by host signal peptidase By similarity
Sitei191 – 1922Cleavage; by host signal peptidase Reviewed prediction
Sitei383 – 3842Cleavage; by host signal peptidase Reviewed prediction
Sitei746 – 7472Cleavage; by host signal peptidase
Sitei809 – 8102Cleavage; by host signal peptidase
Active sitei952 – 9521For protease NS2-3 activity; shared with dimeric partner
Active sitei972 – 9721For protease NS2-3 activity; shared with dimeric partner
Active sitei993 – 9931For protease NS2-3 activity; shared with dimeric partner
Sitei1026 – 10272Cleavage; by protease NS2-3 Reviewed prediction
Active sitei1083 – 10831Charge relay system; for serine protease NS3 activity By similarity
Active sitei1107 – 11071Charge relay system; for serine protease NS3 activity By similarity
Metal bindingi1123 – 11231Zinc
Metal bindingi1125 – 11251Zinc
Active sitei1165 – 11651Charge relay system; for serine protease NS3 activity
Metal bindingi1171 – 11711Zinc
Metal bindingi1175 – 11751Zinc
Sitei1657 – 16582Cleavage; by serine protease NS3 Reviewed prediction
Sitei1711 – 17122Cleavage; by serine protease NS3 Reviewed prediction
Sitei1972 – 19732Cleavage; by serine protease NS3 Reviewed prediction
Metal bindingi2011 – 20111Zinc By similarity
Metal bindingi2029 – 20291Zinc By similarity
Metal bindingi2031 – 20311Zinc By similarity
Metal bindingi2052 – 20521Zinc By similarity
Sitei2420 – 24212Cleavage; by serine protease NS3 Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1230 – 12378ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. cysteine-type endopeptidase activity Source: InterPro
  4. DEAD/H-box RNA helicase binding Source: AgBase
  5. identical protein binding Source: IntAct
  6. ion channel activity Source: UniProtKB-KW
  7. protein binding Source: IntAct
  8. RNA binding Source: UniProtKB-KW
  9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  10. serine-type endopeptidase activity Source: InterPro
  11. serine-type exopeptidase activity Source: InterPro
  12. structural molecule activity Source: InterPro
  13. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  4. induction by virus of host autophagy Source: UniProtKB-KW
  5. modulation by virus of host G1/S transition checkpoint Source: UniProtKB-KW
  6. negative regulation of defense response to virus by host Source: AgBase
  7. negative regulation of interleukin-6 production Source: AgBase
  8. negative regulation of toll-like receptor 2 signaling pathway Source: AgBase
  9. negative regulation of toll-like receptor 4 signaling pathway Source: AgBase
  10. negative regulation of toll-like receptor 7 signaling pathway Source: AgBase
  11. negative regulation of toll-like receptor 9 signaling pathway Source: AgBase
  12. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  13. protein oligomerization Source: UniProtKB-KW
  14. regulation of transcription, DNA-templated Source: UniProtKB-KW
  15. suppression by virus of host MAVS activity Source: UniProtKB-KW
  16. suppression by virus of host MAVS activity by MAVS proteolysis Source: AgBase
  17. suppression by virus of host STAT1 activity Source: UniProtKB-KW
  18. suppression by virus of host TRAF activity Source: UniProtKB-KW
  19. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  20. transcription, DNA-templated Source: UniProtKB-KW
  21. transformation of host cell by virus Source: InterPro
  22. viral protein processing Source: AgBase
  23. viral RNA genome replication Source: InterPro
  24. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation 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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Alternative name(s):
Capsid protein C
p21
Alternative name(s):
gp32
gp35
Alternative name(s):
NS1
gp68
gp70
Protease NS2-3 (EC:3.4.22.-)
Short name:
p23
Alternative name(s):
Hepacivirin
NS3P
p70
Alternative name(s):
p8
Alternative name(s):
p27
Alternative name(s):
p56
Alternative name(s):
NS5B
p68
OrganismiHepatitis C virus genotype 1a (isolate H) (HCV)
Taxonomic identifieri11108 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000000518: Genome

Subcellular locationi

Chain Core protein p21 : Host endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Host mitochondrion membrane; Single-pass type I membrane protein By similarity. Host lipid droplet By similarity
Note: The C-terminal transmembrane domain of core protein p21 contains an ER signal leading the nascent polyprotein to the ER membrane. Only a minor proportion of core protein is present in the nucleus and an unknown proportion is secreted.7 Publications
Chain Core protein p19 : Virion By similarity. Host cytoplasm By similarity. Host nucleus By similarity. Secreted By similarity 7 Publications
Chain Envelope glycoprotein E1 : Virion membrane; Single-pass type I membrane protein Reviewed prediction. Host endoplasmic reticulum membrane; Single-pass type I membrane protein
Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.7 Publications
Chain Envelope glycoprotein E2 : Virion membrane; Single-pass type I membrane protein Reviewed prediction. Host endoplasmic reticulum membrane; Single-pass type I membrane protein
Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.7 Publications
Chain p7 : Host endoplasmic reticulum membrane; Multi-pass membrane protein. Host cell membrane
Note: The C-terminus of p7 membrane domain acts as a signal sequence. After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. Only a fraction localizes to the plasma membrane.7 Publications
Chain Protease NS2-3 : Host endoplasmic reticulum membrane; Multi-pass membrane protein Reviewed prediction 7 Publications
Chain Serine protease NS3 : Host endoplasmic reticulum membrane; Peripheral membrane protein By similarity
Note: NS3 is associated to the ER membrane through its binding to NS4A.7 Publications
Chain Non-structural protein 4A : Host endoplasmic reticulum membrane; Single-pass type I membrane protein Reviewed prediction
Note: Host membrane insertion occurs after processing by the NS3 protease.7 Publications
Chain Non-structural protein 4B : Host endoplasmic reticulum membrane; Multi-pass membrane protein 7 Publications
Chain Non-structural protein 5A : Host endoplasmic reticulum membrane; Peripheral membrane protein. Host cytoplasmhost perinuclear region. Host mitochondrion
Note: Host membrane insertion occurs after processing by the NS3 protease.7 Publications
Chain RNA-directed RNA polymerase : Host endoplasmic reticulum membrane; Single-pass type I membrane protein Reviewed prediction
Note: Host membrane insertion occurs after processing by the NS3 protease.7 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 168167Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei169 – 18921Helical; Reviewed predictionAdd
BLAST
Topological domaini190 – 358169Lumenal Reviewed predictionAdd
BLAST
Transmembranei359 – 37921Helical; Reviewed predictionAdd
BLAST
Topological domaini380 – 725346Lumenal Reviewed predictionAdd
BLAST
Transmembranei726 – 74621Helical; Reviewed predictionAdd
BLAST
Topological domaini747 – 75711Lumenal Reviewed predictionAdd
BLAST
Transmembranei758 – 77821Helical; Reviewed predictionAdd
BLAST
Topological domaini779 – 7824Cytoplasmic Reviewed prediction
Transmembranei783 – 80321Helical; Reviewed predictionAdd
BLAST
Topological domaini804 – 81310Lumenal Reviewed prediction
Transmembranei814 – 83421Helical; Reviewed predictionAdd
BLAST
Topological domaini835 – 88147Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei882 – 90221Helical; Reviewed predictionAdd
BLAST
Topological domaini903 – 92826Lumenal Reviewed predictionAdd
BLAST
Transmembranei929 – 94921Helical; Reviewed predictionAdd
BLAST
Topological domaini950 – 1657708Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1658 – 167821Helical; Reviewed predictionAdd
BLAST
Topological domaini1679 – 1805127Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1806 – 182621Helical; Reviewed predictionAdd
BLAST
Topological domaini1827 – 18282Lumenal Reviewed prediction
Transmembranei1829 – 184921Helical; Reviewed predictionAdd
BLAST
Topological domaini1850 – 18501Cytoplasmic Reviewed prediction
Transmembranei1851 – 187121Helical; Reviewed predictionAdd
BLAST
Topological domaini1872 – 188110Lumenal Reviewed prediction
Transmembranei1882 – 190221Helical; Reviewed predictionAdd
BLAST
Topological domaini1903 – 197270Cytoplasmic Reviewed predictionAdd
BLAST
Intramembranei1973 – 200230 By similarityAdd
BLAST
Topological domaini2003 – 2990988Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei2991 – 301121Helical; By similarityAdd
BLAST

GO - Cellular componenti

  1. host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. host cell lipid particle Source: UniProtKB-SubCell
  3. host cell mitochondrial membrane Source: UniProtKB-SubCell
  4. host cell nucleus Source: UniProtKB-SubCell
  5. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  6. host cell plasma membrane Source: UniProtKB-SubCell
  7. integral component of membrane Source: UniProtKB-KW
  8. integral to membrane of host cell Source: UniProtKB-KW
  9. ribonucleoprotein complex Source: UniProtKB-KW
  10. viral envelope Source: UniProtKB-KW
  11. viral nucleocapsid Source: UniProtKB-KW
  12. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi720 – 7201V → L: Increases processing between E2 and p7. 1 Publication
Mutagenesisi779 – 7791K → I: Virus can no longer infect chimpanzee. 1 Publication
Mutagenesisi781 – 7811R → S: Virus can no longer infect chimpanzee. 1 Publication
Mutagenesisi952 – 9521H → A: Complete loss of NS2-NS3 cleavage. 2 Publications
Mutagenesisi993 – 9931C → A: Complete loss of NS2-NS3 cleavage. 2 Publications
Mutagenesisi1165 – 11651S → A: Complete loss of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B cleavages. 1 Publication
Mutagenesisi1968 – 19681C → A: Strong decrease in NS4B palmitoylation. 1 Publication
Mutagenesisi1972 – 19721C → A: Slight decrease in NS4B palmitoylation. 1 Publication
Mutagenesisi2321 – 23211S → A: Loss of phosphorylation. 1 Publication

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 191190Core protein p21 Reviewed predictionPRO_0000037566Add
BLAST
Chaini2 – 177176Core protein p19 By similarityPRO_0000037567Add
BLAST
Propeptidei178 – 19114ER anchor for the core protein, removed in mature form by host signal peptidase By similarityPRO_0000037568Add
BLAST
Chaini192 – 383192Envelope glycoprotein E1 Reviewed predictionPRO_0000037569Add
BLAST
Chaini384 – 746363Envelope glycoprotein E2 Reviewed predictionPRO_0000037570Add
BLAST
Chaini747 – 80963p7PRO_0000037571Add
BLAST
Chaini810 – 1026217Protease NS2-3 Reviewed predictionPRO_0000037572Add
BLAST
Chaini1027 – 1657631Serine protease NS3 Reviewed predictionPRO_0000037573Add
BLAST
Chaini1658 – 171154Non-structural protein 4A Reviewed predictionPRO_0000037574Add
BLAST
Chaini1712 – 1972261Non-structural protein 4B Reviewed predictionPRO_0000037575Add
BLAST
Chaini1973 – 2420448Non-structural protein 5A Reviewed predictionPRO_0000037576Add
BLAST
Chaini2421 – 3011591RNA-directed RNA polymerase Reviewed predictionPRO_0000037577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; by host By similarity
Modified residuei53 – 531Phosphoserine; by host By similarity
Modified residuei99 – 991Phosphoserine; by host By similarity
Modified residuei116 – 1161Phosphoserine; by host PKA By similarity
Glycosylationi196 – 1961N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi209 – 2091N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi234 – 2341N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi305 – 3051N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi417 – 4171N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi423 – 4231N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi430 – 4301N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi448 – 4481N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi476 – 4761N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi532 – 5321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi540 – 5401N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi556 – 5561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi576 – 5761N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi623 – 6231N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi645 – 6451N-linked (GlcNAc...); by host Reviewed prediction
Lipidationi1968 – 19681S-palmitoyl cysteine; by host1 Publication
Lipidationi1972 – 19721S-palmitoyl cysteine; by host; partial1 Publication
Disulfide bondi2114 ↔ 2162 By similarity
Modified residuei2194 – 21941Phosphoserine; by host; in p56 By similarity
Modified residuei2197 – 21971Phosphoserine; by host; in p58 By similarity
Modified residuei2201 – 22011Phosphoserine; by host; in p58 By similarity
Modified residuei2204 – 22041Phosphoserine; by host; in p58 By similarity
Modified residuei2321 – 23211Phosphoserine; by host1 Publication

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.3 Publications
Envelope E1 and E2 glycoproteins are highly N-glycosylated.
Core protein is phosphorylated by host PKC and PKA By similarity.2 Publications
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.2 Publications
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.
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation By similarity.
NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions.1 Publication

Keywords - PTMi

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

Interactioni

Subunit structurei

Core protein is a homomultimer that binds the C-terminal part of E1 and interacts with numerous cellular proteins. Interacts (via N-terminus finger domain) with human PKN2. Interaction with human STAT1 SH2 domain seems to result in decreased STAT1 phosphorylation, leading to decreased IFN-stimulated gene transcription. In addition to blocking the formation of phosphorylated STAT1, the core protein also promotes ubiquitin-mediated proteasome-dependent degradation of STAT1. Interacts with, and constitutively activates human STAT3. Associates with human LTBR and TNFRSF1A receptors and possibly induces apoptosis. Binds to human SP110 isoform 3/Sp110b, HNRPK, C1QR1, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins. Interacts with human CREB3 nuclear transcription protein, triggering cell transformation. May interact with human p53. Also binds human cytokeratins KRT8, KRT18, KRT19 and VIM (vimentin). Interacts with human ACY3. E1 and E2 glycoproteins form a heterodimer that binds to human LDLR, CLDN1, CD81 and SCARB1 receptors. E2 binds and inhibits human EIF2AK2/PKR. Also binds human CD209/DC-SIGN and CLEC4M/DC-SIGNR. p7 forms a homoheptamer in vitro. NS2 forms a homodimer containing a pair of composite active sites at the dimerization interface. NS2 seems to interact with all other non-structural (NS) proteins. NS4A interacts with NS3 serine protease and stabilizes its folding. NS3-NS4A complex is essential for the activation of the latter and allows membrane anchorage of NS3. NS3 interacts with human TANK-binding kinase TBK1 and MAVS. NS4B and NS5A form homodimers and seem to interact with all other non-structural (NS) proteins. NS5A also interacts with human EIF2AK2/PKR, FKBP8, GRB2, BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases. NS5B is a homooligomer and interacts with human VAPB, HNRNPA1 and SEPT6 By similarity.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P266604EBI-6377335,EBI-6875462From a different organism.
Q99IB83EBI-8753518,EBI-6858513From a different organism.
ACTN1P128147EBI-6904388,EBI-351710From a different organism.
AP2M1Q96CW14EBI-6377335,EBI-297683From a different organism.
ARAP1Q96P483EBI-8753518,EBI-710003From a different organism.
ATF6BQ999415EBI-8763498,EBI-2841031From a different organism.
ATMQ133153EBI-6904388,EBI-495465From a different organism.
BIN1O004995EBI-8753518,EBI-719094From a different organism.
BIN1O00499-72EBI-8753518,EBI-8870146From a different organism.
C1QBPQ070214EBI-6377335,EBI-347528From a different organism.
CCDC86Q9H6F53EBI-8753518,EBI-721289From a different organism.
CD81P600339EBI-6904269,EBI-712921From a different organism.
CDKN1AP389363EBI-6377335,EBI-375077From a different organism.
CHEK2O960173EBI-6904388,EBI-1180783From a different organism.
CIDEBQ9UHD46EBI-6919131,EBI-7062247From a different organism.
CNXQ920L92EBI-6904269,EBI-9209498From a different organism.
CRABP1P297623EBI-8753518,EBI-725950From a different organism.
DDX5P1784412EBI-6904388,EBI-351962From a different organism.
EIF2AK2P195255EBI-8753518,EBI-640775From a different organism.
Eif2ak3Q9Z2B55EBI-6904269,EBI-1226344From a different organism.
EIF4A2Q142404EBI-6904388,EBI-73473From a different organism.
ERC1Q8IUD2-38EBI-3649474,EBI-9352449From a different organism.
ERC1Q8IUD2-43EBI-3649474,EBI-9352501From a different organism.
FGBP026754EBI-6377335,EBI-1034445From a different organism.
FYNP062414EBI-706378,EBI-515315From a different organism.
GRB2P629933EBI-706378,EBI-401755From a different organism.
HCKP086315EBI-706378,EBI-346340From a different organism.
HNRNPA1P096514EBI-6904388,EBI-352662From a different organism.
HSPA5P078233EBI-6904269,EBI-371776From a different organism.
IKBKEQ141642EBI-6919131,EBI-307369From a different organism.
IPO5O004105EBI-8753518,EBI-356424From a different organism.
LckP062403EBI-706378,EBI-1401From a different organism.
LTFP027883EBI-6904259,EBI-1058602From a different organism.
LYNP079485EBI-706378,EBI-79452From a different organism.
MAPKAPK3Q166445EBI-6377335,EBI-1384657From a different organism.
NCLP193384EBI-6904388,EBI-346967From a different organism.
PI4KAP423567EBI-8753518,EBI-723050From a different organism.
PMLP295906EBI-6377335,EBI-295890From a different organism.
PSMB8P280624EBI-3649474,EBI-372294From a different organism.
SCARB1Q8WTV02EBI-6904269,EBI-78657From a different organism.
SEPT6Q141414EBI-6904388,EBI-745901From a different organism.
STAT1P422242EBI-6377335,EBI-1057697From a different organism.
TBC1D20Q96BZ911EBI-8753518,EBI-9254454From a different organism.
TBK1Q9UHD22EBI-6919131,EBI-356402From a different organism.
TMEM173Q86WV65EBI-8763498,EBI-2800345From a different organism.
Traf2P394295EBI-8753518,EBI-520016From a different organism.
VAPAQ9P0L07EBI-8753518,EBI-1059156From a different organism.

Protein-protein interaction databases

IntActiP27958. 212 interactions.
MINTiMINT-106294.

Structurei

Secondary structure

1
3011
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123
Beta strandi16 – 183
Turni19 – 235
Beta strandi30 – 356
Turni36 – 383
Beta strandi39 – 413
Helixi422 – 4243
Beta strandi425 – 4273
Turni432 – 4354
Turni437 – 4426
Beta strandi496 – 4983
Helixi499 – 5013
Beta strandi502 – 5043
Beta strandi507 – 5159
Beta strandi532 – 5343
Beta strandi536 – 5383
Beta strandi550 – 5567
Beta strandi561 – 5655
Helixi568 – 5714
Turni574 – 5774
Beta strandi579 – 5813
Beta strandi602 – 6043
Beta strandi607 – 6093
Helixi614 – 6174
Helixi619 – 6213
Beta strandi625 – 6339
Beta strandi636 – 6449
Helixi911 – 92313
Turni924 – 9274
Helixi931 – 94414
Turni951 – 9533
Helixi956 – 9583
Helixi964 – 9674
Turni971 – 9744
Beta strandi975 – 9773
Beta strandi982 – 9843
Turni988 – 9903
Beta strandi1000 – 10089
Beta strandi1010 – 10134
Turni1016 – 10183
Helixi1019 – 10213
Beta strandi1032 – 10354
Helixi1039 – 104810
Beta strandi1057 – 10637
Beta strandi1068 – 10747
Beta strandi1077 – 10815
Helixi1082 – 10854
Beta strandi1090 – 10923
Beta strandi1095 – 10973
Beta strandi1100 – 11034
Turni1104 – 11074
Beta strandi1108 – 11125
Beta strandi1128 – 11336
Beta strandi1139 – 11446
Beta strandi1146 – 115712
Helixi1158 – 11603
Turni1161 – 11633
Beta strandi1168 – 11703
Turni1172 – 11743
Beta strandi1176 – 118611
Beta strandi1189 – 11979
Helixi1198 – 12069
Beta strandi1224 – 12263
Turni1236 – 12383
Helixi1239 – 12468
Beta strandi1251 – 12566
Helixi1258 – 127114
Beta strandi1277 – 12804
Beta strandi1283 – 12853
Beta strandi1290 – 12956
Helixi1296 – 13016
Helixi1304 – 13074
Beta strandi1311 – 13166
Turni1317 – 13193
Helixi1323 – 133513
Turni1336 – 13405
Beta strandi1342 – 13476
Beta strandi1362 – 13665
Beta strandi1371 – 13755
Beta strandi1378 – 13803
Helixi1382 – 13854
Beta strandi1386 – 13938
Helixi1397 – 140913
Beta strandi1414 – 14174
Helixi1423 – 14253
Beta strandi1428 – 14369
Beta strandi1442 – 14443
Beta strandi1449 – 14535
Beta strandi1456 – 14638
Beta strandi1467 – 14693
Beta strandi1471 – 14788
Helixi1481 – 14888
Beta strandi1493 – 14953
Beta strandi1497 – 15026
Helixi1514 – 152714
Helixi1532 – 154413
Beta strandi1545 – 15484
Helixi1555 – 156410
Helixi1570 – 15789
Helixi1584 – 159714
Helixi1606 – 16116
Turni1614 – 16185
Beta strandi1627 – 16293
Beta strandi1635 – 16373
Helixi1640 – 165213
Beta strandi1680 – 16878
Helixi1753 – 177725
Helixi1940 – 196425
Helixi1976 – 199924
Beta strandi2422 – 24265
Helixi2445 – 24506
Helixi2454 – 24563
Beta strandi2457 – 24593
Helixi2462 – 24643
Helixi2465 – 24728
Helixi2482 – 249514
Helixi2505 – 25106
Helixi2525 – 25295
Helixi2533 – 254816
Beta strandi2550 – 25523
Beta strandi2556 – 25605
Beta strandi2564 – 25663
Helixi2569 – 25713
Beta strandi2579 – 25824
Helixi2585 – 260723
Helixi2608 – 26103
Helixi2612 – 26143
Helixi2617 – 262913
Beta strandi2631 – 26399
Helixi2644 – 26474
Helixi2650 – 266011
Helixi2667 – 267913
Turni2680 – 26823
Beta strandi2684 – 26874
Beta strandi2693 – 26975
Helixi2707 – 272620
Beta strandi2729 – 27368
Beta strandi2739 – 27457
Helixi2749 – 276517
Beta strandi2770 – 27723
Helixi2780 – 27823
Beta strandi2788 – 27947
Beta strandi2800 – 28067
Helixi2809 – 282012
Helixi2827 – 28359
Helixi2839 – 28435
Helixi2845 – 285511
Beta strandi2863 – 28675
Beta strandi2870 – 28745
Helixi2876 – 28783
Helixi2879 – 28879
Helixi2889 – 28924
Helixi2899 – 291214
Helixi2917 – 293418
Helixi2936 – 294510
Helixi2947 – 29493
Beta strandi2950 – 29523
Helixi2960 – 29645
Turni2968 – 29714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A1RX-ray2.50A/B1027-1206[»]
1A1VX-ray2.20A1193-1657[»]
1CWXNMR-A2-45[»]
1HEIX-ray2.10A/B1206-1656[»]
1JR6NMR-A1353-1456[»]
A1478-1507[»]
1N1LX-ray2.60A/B1027-1206[»]
1ONBNMR-A1353-1456[»]
A1478-1507[»]
1R7CNMR-A1973-2003[»]
1R7DNMR-A1973-2003[»]
1R7ENMR-A1973-2003[»]
1R7FNMR-A1973-2003[»]
1R7GNMR-A1973-2003[»]
1RGQX-ray2.90A/B1027-1207[»]
2A4RX-ray2.40A/C1027-1207[»]
B/D1680-1696[»]
2F9VX-ray2.60A/C1027-1207[»]
B/D1678-1696[»]
2HD0X-ray2.28A/B/C/D/E/F/G/H/I/J/K/L903-1026[»]
2JXFNMR-A1751-1780[»]
2KDRNMR-X1938-1965[»]
2O8MX-ray2.00A/B1027-1207[»]
C/D1678-1696[»]
2OBOX-ray2.60A/C1022-1207[»]
B/D1677-1695[»]
2OBQX-ray2.50A/C1027-1207[»]
B/D1678-1696[»]
2OC0X-ray2.30A/C1027-1207[»]
B/D1680-1696[»]
2OC1X-ray2.70A/C1027-1207[»]
B/D1680-1696[»]
2OC7X-ray2.70A/C1027-1207[»]
B/D1680-1696[»]
2OC8X-ray2.66A/C1027-1207[»]
B/D1680-1696[»]
2OINX-ray2.50A/B1027-1207[»]
C/D1678-1696[»]
2P59X-ray2.90C/D1678-1696[»]
2QV1X-ray2.40C/D1678-1696[»]
2XI2X-ray1.80A/B/C2421-2990[»]
2XI3X-ray1.70A/B2421-2990[»]
2XNIX-ray3.30A/B1027-1206[»]
4CL1X-ray3.50A/B/C/D2005-2174[»]
4JZNX-ray2.05K434-446[»]
4JZOX-ray2.22I/J/K/L434-446[»]
4MWFX-ray2.64C/D412-459[»]
C/D486-645[»]
DisProtiDP00588.
ProteinModelPortaliP27958.
SMRiP27958. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2421-2982.

Miscellaneous databases

EvolutionaryTraceiP27958.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini899 – 1026128Peptidase C18Add
BLAST
Domaini1217 – 1369153Helicase ATP-bindingAdd
BLAST
Domaini2634 – 2752119RdRp catalyticAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5958Interaction with DDX3X By similarityAdd
BLAST
Regioni2 – 2322Interaction with STAT1 By similarityAdd
BLAST
Regioni122 – 17352Interaction with APOA2 By similarityAdd
BLAST
Regioni150 – 15910Mitochondrial targeting signal By similarity
Regioni164 – 1674Important for lipid droplets localization By similarity
Regioni265 – 29632Fusion peptide Reviewed predictionAdd
BLAST
Regioni385 – 41127HVR1 By similarityAdd
BLAST
Regioni475 – 4817HVR2 By similarity
Regioni482 – 49413CD81-binding 1 Reviewed predictionAdd
BLAST
Regioni522 – 55332CD81-binding 2 Reviewed predictionAdd
BLAST
Regioni660 – 67112PKR/eIF2-alpha phosphorylation homology domain (PePHD)Add
BLAST
Regioni1679 – 169012NS3-binding (by NS4A) Reviewed predictionAdd
BLAST
Regioni2120 – 2332213Transcriptional activation Reviewed predictionAdd
BLAST
Regioni2120 – 220889FKBP8-binding Reviewed predictionAdd
BLAST
Regioni2200 – 225051Basal phosphorylation By similarityAdd
BLAST
Regioni2210 – 227566PKR-binding Reviewed predictionAdd
BLAST
Regioni2249 – 230658NS4B-binding Reviewed predictionAdd
BLAST
Regioni2351 – 242070Basal phosphorylation By similarityAdd
BLAST
Regioni2354 – 237724V3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 139Nuclear localization signal Reviewed prediction
Motifi38 – 436Nuclear localization signal Reviewed prediction
Motifi58 – 647Nuclear localization signal Reviewed prediction
Motifi66 – 716Nuclear localization signal Reviewed prediction
Motifi1316 – 13194DECH box
Motifi2322 – 23254SH3-binding Reviewed prediction
Motifi2327 – 23359Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi796 – 8038Poly-Leu
Compositional biasi1432 – 14354Poly-Val
Compositional biasi2286 – 232742Pro-richAdd
BLAST
Compositional biasi2996 – 29994Poly-Leu

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 two highly variable regions called hypervariable region 1 and 2 (HVR1 and HVR2). E2 also contain two segments involved in CD81-binding. HVR1 is implicated in the SCARB1-mediated cell entry. HVR2 and CD81-binding regions may be involved in sensitivity and/or resistance to IFN-alpha therapy By similarity.2 Publications
The N-terminus of NS5A acts as membrane anchor. The central part of NS5A seems to be intrinsically disordered and interacts with NS5B and host PKR. The C-terminus of NS5A contains a variable region called variable region 3 (V3) By similarity.2 Publications
The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases By similarity.2 Publications
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 NS3.2 Publications

Sequence similaritiesi

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
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.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF07652. Flavi_DEAD. 1 hit.
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.
[Graphical view]
ProDomiPD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Note: The exact location of the ribosomal frameshift is unknown. The F protein seems to be generated by a -2 ribosomal frameshift located in the vicinity of codon 11 of the core protein coding sequence. However, some F proteins may also be generated by +1 ribosomal frameshift. Since the core gene encodes alternative reading frame proteins (ARFPs), many functions depicted for the core protein might belong to the ARFPs.

Isoform Genome polyprotein (identifier: P27958-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR     50
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP 100
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA 150
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTVPAS AYQVRNSSGL 200
YHVTNDCPNS SVVYEAADAI LHTPGCVPCV REGNASRCWV AVTPTVATRD 250
GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRHHWT 300
TQDCNCSIYP GHITGHRMAW NMMMNWSPTA ALVVAQLLRI PQAIMDMIAG 350
AHWGVLAGIK YFSMVGNWAK VLVVLLLFAG VDAETHVTGG NAGRTTAGLV 400
GLLTPGAKQN IQLINTNGSW HINSTALNCN ESLNTGWLAG LFYQHKFNSS 450
GCPERLASCR RLTDFAQGWG PISYANGSGL DERPYCWHYP PRPCGIVPAK 500
SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ANDTDVFVLN NTRPPLGNWF 550
GCTWMNSTGF TKVCGAPPCV IGGVGNNTLL CPTDCFRKYP EATYSRCGSG 600
PRITPRCMVD YPYRLWHYPC TINYTIFKVR MYVGGVEHRL EAACNWTRGE 650
RCDLEDRDRS ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ 700
YLYGVGSSIA SWAIKWEYVV LLFLLLADAR VCSCLWMMLL ISQAEAALEN 750
LVILNAASLA GTHGLVSFLV FFCFAWYLKG RWVPGAVYAL YGMWPLLLLL 800
LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIS WCMWWLQYFL 850
TRVEAQLHVW VPPLNVRGGR DAVILLTCVV HPALVFDITK LLLAIFGPLW 900
ILQASLLKVP YFVRVQGLLR ICALARKIAG GHYVQMAIIK LGALTGTCVY 950
NHLAPLRDWA HNGLRDLAVA VEPVVFSRME TKLITWGADT AACGDIINGL 1000
PVSARRGQEI LLGPADGMVS KGWRLLAPIT AYAQQTRGLL GCIITSLTGR 1050
DKNQVEGEVQ IVSTATQTFL ATCINGVCWT VYHGAGTRTI ASPKGPVIQT 1100
YTNVDQDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG 1150
SLLSPRPISY LKGSSGGPLL CPTGHAVGLF RAAVCTRGVA KAVDFIPVEN 1200
LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAKGYK 1250
VLVLNPSVAA TLGFGAYMSK AHGVDPNIRT GVRTITTGSP ITYSTYGKFL 1300
ADAGCSGGAY DIIICDECHS TDATSISGIG TVLDQAETAG ARLVVLATAT 1350
PPGSVTVSHP NIEEVALSTT GEIPFYGKAI PLEVIKGGRH LIFCHSKKKC 1400
DELAAKLVAL GINAVAYYRG LDVSVIPTSG DVVVVSTDAL MTGFTGDFDS 1450
VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR 1500
FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV 1550
CQDHLGFWEG VFTGLTHIDA HFLSQTKQSG ENFPYLVAYQ ATVCARAQAP 1600
PPSWDQMRKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMTCMS 1650
ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV VIVGRIVLSG KPAIIPDREV 1700
LYQEFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS RHAEVITPAV 1750
QTNWQKLEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP 1800
LTTGQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAALD SVGLGKVLVD 1850
ILAGYGAGVA GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALAVGVVFAS 1900
ILRRRVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTAILSS 1950
LTVTQLLRRL HQWISSECTT PCSGSWLRDI WDWICEVLSD FKTWLKAKLM 2000
PQLPGIPFVS CQRGYRGVWR GDGIMHTRCH CGAEITGHVK NGTMRIVGPR 2050
TCKNMWSGTF FINAYTTGPC TPLPAPNYKF ALWRVSAEEY VEIRRVGDFH 2100
YVSGMTTDNL KCPCQIPSPE FFTELDGVRL HRFAPPCKPL LREEVSFRVG 2150
LHEYPVGSQL PCEPEPDVAV LTSMLTDPSH ITAEAAGRRL ARGSPPSMAS 2200
SSASQLSAPS LKATCTANHD SPDAELIEAN LLWRQEMGGN ITRVESENKV 2250
VILDSFDPLV AEEDEREVSV PAEILRKSRR FAPALPVWAR PDYNPLLVET 2300
WKKPDYEPPV VHGCPLPPPR SPPVPPPRKK RTVVLTESTL PTALAELATK 2350
SFGSSSTSGI TGDNTTTSSE PAPSGCPPDS DVESYSSMPP LEGEPGDPDL 2400
SDGSWSTVSS GADTEDVVCC SMSYSWTGAL VTPCAAEEQK LPINALSNSL 2450
LRHHNLVYST TSRSACQRKK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA 2500
NLLSVEEACS LAPPHSAKSK FGYGAKDVRC HARKAVAHIN SVWKDLLEDS 2550
VTPIDTTIMA KNEVFCVQPE KGGRKPARLI VFPDLGVRVC EKMALYDVVS 2600
KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGLSYD TRCFDSTVTE 2650
SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR 2700
ASRVLTTSCG NTLTRYIKAR AACRAAGLQD CTMLVCGDDL VVICESAGVQ 2750
EDAASLRAFT EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR 2800
VYYLTRDPTT PLARAAWETA RHTPVNSWLG NIIMFAPTLW ARMILMTHFF 2850
SVLIARDQLE QALNCEIYGA CYSIEPLDLP PIIQRLHGLS AFSLHSYSPG 2900
EINRVAACLR KLGVPPLRAW RHRAWSVRAR LLARGGKAAI CGKYLFNWAV 2950
RTKLKLTPIT AAGRLDLSGW FTAGYSGGDI YHSVSHARPR WFWFCLLLLA 3000
AGVGIYLLPN R 3011

Note: Produced by conventional translation.

Length:3,011
Mass (Da):327,146
Last modified:January 23, 2007 - v3
Checksum:i772CBB29CCD94753
GO
Isoform F protein (identifier: P0C045-1) [UniParc]FASTAAdd to Basket

Also known as: Frameshifted protein

The sequence of this isoform can be found in the external entry P0C045.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by ribosomal frameshifting.

Length:162
Mass (Da):17,006
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti212 – 2121V → I in strain: Isolate H77.
Natural varianti297 – 2971H → R in strain: Isolate H77.
Natural varianti303 – 3031D → S in strain: Isolate H77.
Natural varianti321 – 3211N → D in strain: Isolate H77.
Natural varianti360 – 3601K → A in strain: Isolate H77.
Natural varianti391 – 3911N → S in strain: Isolate H77.
Natural varianti394 – 3941R → H in strain: Isolate H77.
Natural varianti431 – 4311E → D in strain: Isolate H77.
Natural varianti434 – 4341N → T in strain: Isolate H77.
Natural varianti444 – 4441Q → R in strain: Isolate H77.
Natural varianti457 – 4571A → T in strain: Isolate H77.
Natural varianti564 – 5663CGA → RGV in strain: Isolate H77.
Natural varianti589 – 5891Y → H in strain: Isolate H77.
Natural varianti602 – 6021R → W in strain: Isolate H77.
Natural varianti650 – 6501E → G in strain: Isolate H77.
Natural varianti773 – 7731C → R in strain: Isolate H77.
Natural varianti787 – 7871V → A in strain: Isolate H77.
Natural varianti790 – 7901L → F in strain: Isolate H77.
Natural varianti877 – 8771T → M in strain: Isolate H77.
Natural varianti883 – 8831A → T in strain: Isolate H77.
Natural varianti948 – 9481C → Y in strain: Isolate H77.
Natural varianti954 – 9541A → T in strain: Isolate H77.
Natural varianti1026 – 10261L → Q in strain: Isolate H77.
Natural varianti1033 – 10331A → T in strain: Isolate H77.
Natural varianti1049 – 10491G → S in strain: Isolate H77.
Natural varianti1100 – 11001T → M in strain: Isolate H77.
Natural varianti1121 – 11211T → A in strain: Isolate H77.
Natural varianti1173 – 11731T → A in strain: Isolate H77.
Natural varianti1202 – 12021E → G in strain: Isolate H77.
Natural varianti1214 – 12141S → P in strain: Isolate H77.
Natural varianti1247 – 12471K → Q in strain: Isolate H77.
Natural varianti1303 – 13031A → G in strain: Isolate H77.
Natural varianti1327 – 13271S → L in strain: Isolate H77.
Natural varianti1556 – 15561G → E in strain: Isolate H77.
Natural varianti1608 – 16081R → W in strain: Isolate H77.
Natural varianti1742 – 17421H → Q in strain: Isolate H77.
Natural varianti1839 – 18402LD → IG in strain: Isolate H77.
Natural varianti1893 – 18931A → V in strain: Isolate H77.
Natural varianti1898 – 19003FAS → CAA in strain: Isolate H77.
Natural varianti1905 – 19051R → H in strain: Isolate H77.
Natural varianti1940 – 19401A → V in strain: Isolate H77.
Natural varianti2043 – 20431T → A in strain: Isolate H77.
Natural varianti2053 – 20531K → R in strain: Isolate H77.
Natural varianti2061 – 20611F → L in strain: Isolate H77.
Natural varianti2102 – 21021V → I in strain: Isolate H77.
Natural varianti2185 – 21851A → E in strain: Isolate H77.
Natural varianti2283 – 22831P → R in strain: Isolate H77.
Natural varianti2296 – 22961L → P in strain: Isolate H77.
Natural varianti2341 – 23411P → S in strain: Isolate H77.
Natural varianti2355 – 23551S → P in strain: Isolate H77.
Natural varianti2400 – 24001L → F in strain: Isolate H77.
Natural varianti2425 – 24251S → T in strain: Isolate H77.
Natural varianti2469 – 24691K → Q in strain: Isolate H77.
Natural varianti2512 – 25121A → T in strain: Isolate H77.
Natural varianti2637 – 26371L → F in strain: Isolate H77.
Natural varianti2703 – 27031R → G in strain: Isolate H77.
Natural varianti2715 – 27151R → C in strain: Isolate H77.
Natural varianti2755 – 27551S → N in strain: Isolate H77.
Natural varianti2925 – 29251W → R in strain: Isolate H77.
Natural varianti2933 – 29331A → S in strain: Isolate H77.
Natural varianti2937 – 29371K → R in strain: Isolate H77.
Natural varianti2960 – 29601T → A in strain: Isolate H77.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M67463 Genomic RNA. Translation: AAA45534.1.
AF009606 Genomic RNA. Translation: AAB66324.1.
AF011751 Genomic RNA. Translation: AAB67036.1.
AF011752 Genomic RNA. Translation: AAB67037.1.
AF011753 Genomic RNA. Translation: AAB67038.1.
PIRiA36814. GNWVCH.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

euHCVdb

The European HCV database

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M67463 Genomic RNA. Translation: AAA45534.1 .
AF009606 Genomic RNA. Translation: AAB66324.1 .
AF011751 Genomic RNA. Translation: AAB67036.1 .
AF011752 Genomic RNA. Translation: AAB67037.1 .
AF011753 Genomic RNA. Translation: AAB67038.1 .
PIRi A36814. GNWVCH.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A1R X-ray 2.50 A/B 1027-1206 [» ]
1A1V X-ray 2.20 A 1193-1657 [» ]
1CWX NMR - A 2-45 [» ]
1HEI X-ray 2.10 A/B 1206-1656 [» ]
1JR6 NMR - A 1353-1456 [» ]
A 1478-1507 [» ]
1N1L X-ray 2.60 A/B 1027-1206 [» ]
1ONB NMR - A 1353-1456 [» ]
A 1478-1507 [» ]
1R7C NMR - A 1973-2003 [» ]
1R7D NMR - A 1973-2003 [» ]
1R7E NMR - A 1973-2003 [» ]
1R7F NMR - A 1973-2003 [» ]
1R7G NMR - A 1973-2003 [» ]
1RGQ X-ray 2.90 A/B 1027-1207 [» ]
2A4R X-ray 2.40 A/C 1027-1207 [» ]
B/D 1680-1696 [» ]
2F9V X-ray 2.60 A/C 1027-1207 [» ]
B/D 1678-1696 [» ]
2HD0 X-ray 2.28 A/B/C/D/E/F/G/H/I/J/K/L 903-1026 [» ]
2JXF NMR - A 1751-1780 [» ]
2KDR NMR - X 1938-1965 [» ]
2O8M X-ray 2.00 A/B 1027-1207 [» ]
C/D 1678-1696 [» ]
2OBO X-ray 2.60 A/C 1022-1207 [» ]
B/D 1677-1695 [» ]
2OBQ X-ray 2.50 A/C 1027-1207 [» ]
B/D 1678-1696 [» ]
2OC0 X-ray 2.30 A/C 1027-1207 [» ]
B/D 1680-1696 [» ]
2OC1 X-ray 2.70 A/C 1027-1207 [» ]
B/D 1680-1696 [» ]
2OC7 X-ray 2.70 A/C 1027-1207 [» ]
B/D 1680-1696 [» ]
2OC8 X-ray 2.66 A/C 1027-1207 [» ]
B/D 1680-1696 [» ]
2OIN X-ray 2.50 A/B 1027-1207 [» ]
C/D 1678-1696 [» ]
2P59 X-ray 2.90 C/D 1678-1696 [» ]
2QV1 X-ray 2.40 C/D 1678-1696 [» ]
2XI2 X-ray 1.80 A/B/C 2421-2990 [» ]
2XI3 X-ray 1.70 A/B 2421-2990 [» ]
2XNI X-ray 3.30 A/B 1027-1206 [» ]
4CL1 X-ray 3.50 A/B/C/D 2005-2174 [» ]
4JZN X-ray 2.05 K 434-446 [» ]
4JZO X-ray 2.22 I/J/K/L 434-446 [» ]
4MWF X-ray 2.64 C/D 412-459 [» ]
C/D 486-645 [» ]
DisProti DP00588.
ProteinModelPortali P27958.
SMRi P27958. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2421-2982.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P27958. 212 interactions.
MINTi MINT-106294.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

euHCVdbi AF009606.
AF011751.
AF011752.
AF011753.
M67463.

Miscellaneous databases

EvolutionaryTracei P27958.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011492. DEAD_Flavivir.
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.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR027417. P-loop_NTPase.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF07652. Flavi_DEAD. 1 hit.
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.
[Graphical view ]
ProDomi PD001388. HCV_env. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00487. DEXDc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51693. HCV_NS2_PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genomic structure of the human prototype strain H of hepatitis C virus: comparison with American and Japanese isolates."
    Inchauspe G., Zebedee S., Lee D.H.H., Sugitani M., Nasoff M., Prince A.M.
    Proc. Natl. Acad. Sci. U.S.A. 88:10292-10296(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], DOMAIN V3 REGION.
  2. "Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA."
    Kolykhalov A.A., Agapov E.V., Blight K.J., Mihalik K., Feinstone S.M., Rice C.M.
    Science 277:570-574(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate H77.
  3. "Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee."
    Yanagi M., Purcell R.H., Emerson S.U., Bukh J.
    Proc. Natl. Acad. Sci. U.S.A. 94:8738-8743(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate H77.
  4. Cited for: IDENTIFICATION OF THE CYSTEINE PROTEASE, MUTAGENESIS OF HIS-952; CYS-993 AND SER-1165.
  5. "Expression and identification of hepatitis C virus polyprotein cleavage products."
    Grakoui A., Wychowski C., Lin C., Feinstone S.M., Rice C.M.
    J. Virol. 67:1385-1395(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  6. "Characterization of the nuclear localization signal and subcellular distribution of hepatitis C virus nonstructural protein NS5A."
    Ide Y., Zhang L., Chen M., Inchauspe G., Bahl C., Sasaguri Y., Padmanabhan R.
    Gene 182:203-211(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF NS5A, NUCLEAR LOCALIZATION SIGNAL.
  7. "Identification of the major phosphorylation site of the hepatitis C virus H strain NS5A protein as serine 2321."
    Reed K.E., Rice C.M.
    J. Biol. Chem. 274:28011-28018(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2321, MUTAGENESIS OF SER-2321.
  8. "Hepatitis C virus NS5A protein modulates transcription through a novel cellular transcription factor SRCAP."
    Ghosh A.K., Majumder M., Steele R., Yaciuk P., Chrivia J., Ray R., Ray R.B.
    J. Biol. Chem. 275:7184-7188(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH SRCAP, SUBCELLULAR LOCATION OF NS5A.
  9. "Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins."
    Cocquerel L., Wychowski C., Minner F., Penin F., Dubuisson J.
    J. Virol. 74:3623-3633(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF E1 AND E2, ROLE OF TRANSMEMBRANE DOMAINS.
  10. "Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation."
    Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.
    J. Clin. Invest. 106:1239-1249(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CORE PROTEIN WITH HUMAN C1QR1.
  11. "Conservation of the conformation and positive charges of hepatitis C virus E2 envelope glycoprotein hypervariable region 1 points to a role in cell attachment."
    Penin F., Combet C., Germanidis G., Frainais P.-O., Deleage G., Pawlotsky J.-M.
    J. Virol. 75:5703-5710(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF HVR1 REGION.
  12. "Determinants for membrane association of the hepatitis C virus RNA-dependent RNA polymerase."
    Schmidt-Mende J., Bieck E., Huegle T., Penin F., Rice C.M., Blum H.E., Moradpour D.
    J. Biol. Chem. 276:44052-44063(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY OF NS5B.
  13. "Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins."
    Cocquerel L., Op de Beeck A., Lambot M., Roussel J., Delgrange D., Pillez A., Wychowski C., Penin F., Dubuisson J.
    EMBO J. 21:2893-2902(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY OF ENVELOPE GLYCOPROTEINS E1 AND E2.
  14. "Subcellular localization and topology of the p7 polypeptide of hepatitis C virus."
    Carrere-Kremer S., Montpellier-Pala C., Cocquerel L., Wychowski C., Penin F., Dubuisson J.
    J. Virol. 76:3720-3730(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, SUBCELLULAR LOCATION OF P7.
  15. "An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A."
    Brass V., Bieck E., Montserret R., Woelk B., Hellings J.A., Blum H.E., Penin F., Moradpour D.
    J. Biol. Chem. 277:8130-8139(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY OF NS5A.
  16. "Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex."
    Egger D., Woelk B., Gosert R., Bianchi L., Blum H.E., Moradpour D., Bienz K.
    J. Virol. 76:5974-5984(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REPLICATION COMPLEX.
  17. "Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons."
    Gosert R., Egger D., Lohmann V., Bartenschlager R., Blum H.E., Bienz K., Moradpour D.
    J. Virol. 77:5487-5492(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REPLICATION COMPLEX.
  18. "The hepatitis C virus p7 protein forms an ion channel that is inhibited by long-alkyl-chain iminosugar derivatives."
    Pavlovic D., Neville D.C., Argaud O., Blumberg B., Dwek R.A., Fischer W.B., Zitzmann N.
    Proc. Natl. Acad. Sci. U.S.A. 100:6104-6108(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION OF P7 BY LONG-ALKYL-CHAIN IMINOSUGAR DERIVATIVES.
  19. "The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences."
    Sakai A., Claire M.S., Faulk K., Govindarajan S., Emerson S.U., Purcell R.H., Bukh J.
    Proc. Natl. Acad. Sci. U.S.A. 100:11646-11651(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-779 AND ARG-781.
    Strain: Isolate H77.
  20. "Protein-protein interactions between hepatitis C virus nonstructural proteins."
    Dimitrova M., Imbert I., Kieny M.P., Schuster C.
    J. Virol. 77:5401-5414(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION BETWEEN NON-STRUCTURAL PROTEINS.
  21. "Topology of the membrane-associated hepatitis C virus protein NS4B."
    Lundin M., Monne M., Widell A., Von Heijne G., Persson M.A.A.
    J. Virol. 77:5428-5438(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, SUBCELLULAR LOCATION OF NS4B.
    Strain: Isolate H77.
  22. "CD81-dependent binding of hepatitis C virus E1E2 heterodimers."
    Cocquerel L., Kuo C.-C., Dubuisson J., Levy S.
    J. Virol. 77:10677-10683(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81.
  23. "Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes."
    Bartosch B., Dubuisson J., Cosset F.-L.
    J. Exp. Med. 197:633-642(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81; LDLR AND SCARB1.
  24. "Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor."
    Bartosch B., Vitelli A., Granier C., Goujon C., Dubuisson J., Pascale S., Scarselli E., Cortese R., Nicosia A., Cosset F.-L.
    J. Biol. Chem. 278:41624-41630(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF E1/E2 HETERODIMER WITH HUMAN CD81.
  25. "Characterization of functional hepatitis C virus envelope glycoproteins."
    Op De Beeck A., Voisset C., Bartosch B., Ciczora Y., Cocquerel L., Keck Z., Foung S., Cosset F.-L., Dubuisson J.
    J. Virol. 78:2994-3002(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF E1 AND E2.
  26. "Regulation of hepatitis C virus polyprotein processing by signal peptidase involves structural determinants at the p7 sequence junctions."
    Carrere-Kremer S., Montpellier C., Lorenzo L., Brulin B., Cocquerel L., Belouzard S., Penin F., Dubuisson J.
    J. Biol. Chem. 279:41384-41392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  27. "L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus."
    Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C., Olson W.C., Gardner J.P., Dragic T.
    Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN CD209/DC-SIGN AND CLEC4M/DC-SIGNR.
    Strain: Isolate H77.
  28. "Analysis of the processing and transmembrane topology of the E2p7 protein of hepatitis C virus."
    Isherwood B.J., Patel A.H.
    J. Gen. Virol. 86:667-676(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BETWEEN E2 AND P7, TOPOLOGY OF P7, MUTAGENESIS OF VAL-720.
  29. "Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity."
    Li X.D., Sun L., Seth R.B., Pineda G., Chen Z.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:17717-17722(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS3 PROTEASE WITH HUMAN MAVS.
  30. "Palmitoylation and polymerization or in protein-protein interactions of hepatitis C virus NS4B protein."
    Yu G.-Y., Lee K.-J., Gao L., Lai M.M.C.
    J. Virol. 80:6013-6023(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-1968 AND CYS-1972 (NS4B) BY HOST, MUTAGENESIS OF CYS-1968 AND CYS-1972.
    Strain: Isolate H77.
  31. "Entry of hepatitis C virus pseudotypes into primary human hepatocytes by clathrin-dependent endocytosis."
    Codran A., Royer C., Jaeck D., Bastien-Valle M., Baumert T.F., Kieny M.P., Pereira C.A., Martin J.P.
    J. Gen. Virol. 87:2583-2593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF E1 AND E2.
    Strain: Isolate H77.
  32. "The membrane-active regions of the hepatitis C virus E1 and E2 envelope glycoproteins."
    Perez-Berna A.J., Moreno M.R., Guillen J., Bernabeu A., Villalain J.
    Biochemistry 45:3755-3768(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE FUSION PEPTIDE.
    Strain: Isolate H77.
  33. "Dual topology of the processed hepatitis C virus protein NS4B is influenced by the NS5A protein."
    Lundin M., Lindstrom H., Groenwall C., Persson M.A.
    J. Gen. Virol. 87:3263-3272(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY OF NS4B.
    Strain: Isolate H77.
  34. "Molecular and structural characterization of the domain 2 of hepatitis C virus non-structural protein 5A."
    Liang Y., Kang C.B., Yoon H.S.
    Mol. Cells 22:13-20(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NS5A WITH NS5B AND HOST PKR.
  35. "Conserved determinants for membrane association of nonstructural protein 5A from hepatitis C virus and related viruses."
    Brass V., Pal Z., Sapay N., Deleage G., Blum H.E., Penin F., Moradpour D.
    J. Virol. 81:2745-2757(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF NS5A.
  36. "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
    Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
    J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPA1 AND SEPT6.
  37. "Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes."
    McLauchlan J.
    J. Viral Hepat. 7:2-14(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  38. "Protein kinase C-related kinase 2 regulates hepatitis C virus RNA polymerase function by phosphorylation."
    Kim S.J., Kim J.H., Kim Y.G., Lim H.S., Oh J.W.
    J. Biol. Chem. 279:50031-50041(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH PKN2.
  39. Cited for: REVIEW, SUBCELLULAR LOCATION.
  40. "Identification of a novel protein binding to hepatitis C virus core protein."
    Chen Y.R., Chen T.Y., Zhang S.L., Lin S.M., Zhao Y.R., Ye F., Zhang X., Shi L., Dang S.S., Liu M.
    J. Gastroenterol. Hepatol. 24:1300-1304(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACY3.
  41. "Structure of the hepatitis C virus RNA helicase domain."
    Yao N., Hesson T., Cable M.B., Hong Z., Kwong A.D., Le H.V., Weber P.C.
    Nat. Struct. Biol. 4:463-467(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1206-1656.
  42. "Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide."
    Kim J.L., Morgenstern K.A., Lin C., Fox T., Dwyer M.D., Landro J.A., Chambers S.P., Markland W., Lepre C.A., O'Malley E.T., Harbeson S.L., Rice C.M., Murcko M.A., Caron P.R., Thomson J.A.
    Cell 87:343-355(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1027-1206 IN COMPLEX WITH NS4A.
  43. "Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding."
    Kim J.L., Morgenstern K.A., Griffith J.P., Dwyer M.D., Thomson J.A., Murcko M.A., Lin C., Caron P.R.
    Structure 6:89-100(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1192-1657.
  44. "Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase."
    Liu D., Wang Y.-S., Gesell J.J., Wyss D.F.
    J. Mol. Biol. 314:543-561(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1353-1507.
  45. "Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray crystal structure data in the optimization of P3 and P4 substituents."
    Andrews D.M., Chaignot H., Coomber B.A., Good A.C., Hind S.L., Johnson M.R., Jones P.S., Mills G., Robinson J.E., Skarzynski T., Slater M.J., Somers D.O.
    Org. Lett. 4:4479-4482(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1027-1207.
  46. "Structure of the catalytic domain of the hepatitis C virus NS2-3 protease."
    Lorenz I.C., Marcotrigiano J., Dentzer T.G., Rice C.M.
    Nature 442:831-835(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 903-1026, MUTAGENESIS OF HIS-952 AND CYS-993.

Entry informationi

Entry nameiPOLG_HCVH
AccessioniPrimary (citable) accession number: P27958
Secondary accession number(s): O36579
, O36608, O36609, O36610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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