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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.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 By similarity. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity.By similarity1 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.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 By similarity. Cleaves and inhibits the host antiviral protein MAVS.By similarity1 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.By similarity
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).PROSITE-ProRule annotation
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.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei177 – 1782Cleavage; by host signal peptidaseBy similarity
Sitei191 – 1922Cleavage; by host signal peptidaseSequence Analysis
Sitei383 – 3842Cleavage; by host signal peptidaseSequence Analysis
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 NS2-3PROSITE-ProRule annotation
Active sitei1083 – 10831Charge relay system; for serine protease NS3 activityBy similarity
Active sitei1107 – 11071Charge relay system; for serine protease NS3 activityBy 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 NS3Sequence Analysis
Sitei1711 – 17122Cleavage; by serine protease NS3Sequence Analysis
Sitei1972 – 19732Cleavage; by serine protease NS3Sequence Analysis
Metal bindingi2011 – 20111ZincBy similarity
Metal bindingi2029 – 20291ZincBy similarity
Metal bindingi2031 – 20311ZincBy similarity
Metal bindingi2052 – 20521ZincBy similarity
Sitei2420 – 24212Cleavage; by serine protease NS3Sequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1230 – 12378ATPPROSITE-ProRule annotation

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. RNA binding Source: UniProtKB-KW
  8. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  9. serine-type endopeptidase activity Source: InterPro
  10. serine-type exopeptidase activity Source: InterPro
  11. structural molecule activity Source: InterPro
  12. 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 By similarity; Single-pass membrane protein By similarity. Host mitochondrion membrane By similarity; 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.
Chain Core protein p19 : Virion By similarity. Host cytoplasm By similarity. Host nucleus By similarity. Secreted By similarity
Chain Envelope glycoprotein E1 : Virion membrane Curated; Single-pass type I membrane protein Curated. 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.
Chain Envelope glycoprotein E2 : Virion membrane Curated; Single-pass type I membrane protein Curated. 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.
Chain p7 : Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Host cell membrane 1 Publication
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.
Chain Serine protease NS3 : Host endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
Note: NS3 is associated to the ER membrane through its binding to NS4A.
Chain Non-structural protein 4A : Host endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated
Note: Host membrane insertion occurs after processing by the NS3 protease.
Chain Non-structural protein 4B : Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication
Chain RNA-directed RNA polymerase : Host endoplasmic reticulum membrane Curated; Single-pass type I membrane protein Curated
Note: Host membrane insertion occurs after processing by the NS3 protease.

GO - Cellular componenti

  1. host cell endoplasmic reticulum Source: UniProtKB-KW
  2. host cell lipid particle Source: UniProtKB-KW
  3. host cell mitochondrion Source: UniProtKB-KW
  4. host cell nucleus Source: UniProtKB-KW
  5. host cell plasma membrane Source: UniProtKB-KW
  6. integral component of membrane Source: UniProtKB-KW
  7. integral to membrane of host cell Source: UniProtKB-KW
  8. ribonucleoprotein complex Source: UniProtKB-KW
  9. viral envelope Source: UniProtKB-KW
  10. viral nucleocapsid Source: UniProtKB-KW
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 hostBy similarity
Chaini2 – 191190Core protein p21Sequence AnalysisPRO_0000037566Add
BLAST
Chaini2 – 177176Core protein p19By similarityPRO_0000037567Add
BLAST
Propeptidei178 – 19114ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityPRO_0000037568Add
BLAST
Chaini192 – 383192Envelope glycoprotein E1Sequence AnalysisPRO_0000037569Add
BLAST
Chaini384 – 746363Envelope glycoprotein E2Sequence AnalysisPRO_0000037570Add
BLAST
Chaini747 – 80963p7PRO_0000037571Add
BLAST
Chaini810 – 1026217Protease NS2-3PROSITE-ProRule annotationPRO_0000037572Add
BLAST
Chaini1027 – 1657631Serine protease NS3Sequence AnalysisPRO_0000037573Add
BLAST
Chaini1658 – 171154Non-structural protein 4ASequence AnalysisPRO_0000037574Add
BLAST
Chaini1712 – 1972261Non-structural protein 4BSequence AnalysisPRO_0000037575Add
BLAST
Chaini1973 – 2420448Non-structural protein 5ASequence AnalysisPRO_0000037576Add
BLAST
Chaini2421 – 3011591RNA-directed RNA polymeraseSequence AnalysisPRO_0000037577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; by hostBy similarity
Modified residuei53 – 531Phosphoserine; by hostBy similarity
Modified residuei99 – 991Phosphoserine; by hostBy similarity
Modified residuei116 – 1161Phosphoserine; by host PKABy similarity
Glycosylationi196 – 1961N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi234 – 2341N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi305 – 3051N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi423 – 4231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi476 – 4761N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi540 – 5401N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi556 – 5561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi576 – 5761N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi623 – 6231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi645 – 6451N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi1968 – 19681S-palmitoyl cysteine; by host1 Publication
Lipidationi1972 – 19721S-palmitoyl cysteine; by host; partial1 Publication
Disulfide bondi2114 ↔ 2162By similarity
Modified residuei2194 – 21941Phosphoserine; by host; in p56By similarity
Modified residuei2197 – 21971Phosphoserine; by host; in p58By similarity
Modified residuei2201 – 22011Phosphoserine; by host; in p58By similarity
Modified residuei2204 – 22041Phosphoserine; by host; in p58By 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.By similarity
Envelope E1 and E2 glycoproteins are highly N-glycosylated.
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
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
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.By similarity

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.
BIN1O0049911EBI-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.
DDX3XO0057111EBI-6377335,EBI-353779From a different organism.
DDX5P1784412EBI-6904388,EBI-351962From a different organism.
EIF2AK2P195254EBI-6904269,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.
LTFP027884EBI-6904269,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.
SNRPD1P623147EBI-3649474,EBI-372177From 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. 215 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[»]
4Q0XX-ray2.90E421-446[»]
DisProtiDP00588.
ProteinModelPortaliP27958.
SMRiP27958. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2421-2982.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27958.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 168167CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini190 – 358169LumenalSequence AnalysisAdd
BLAST
Topological domaini380 – 725346LumenalSequence AnalysisAdd
BLAST
Topological domaini747 – 75711LumenalSequence AnalysisAdd
BLAST
Topological domaini779 – 7824CytoplasmicSequence Analysis
Topological domaini804 – 81310LumenalSequence Analysis
Topological domaini835 – 88147CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini903 – 92826LumenalSequence AnalysisAdd
BLAST
Topological domaini950 – 1657708CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1679 – 1805127CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1827 – 18282LumenalSequence Analysis
Topological domaini1850 – 18501CytoplasmicSequence Analysis
Topological domaini1872 – 188110LumenalSequence Analysis
Topological domaini1903 – 197270CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini2003 – 2990988CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1973 – 200230By similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Transmembranei359 – 37921HelicalSequence AnalysisAdd
BLAST
Transmembranei726 – 74621HelicalSequence AnalysisAdd
BLAST
Transmembranei758 – 77821HelicalSequence AnalysisAdd
BLAST
Transmembranei783 – 80321HelicalSequence AnalysisAdd
BLAST
Transmembranei814 – 83421HelicalSequence AnalysisAdd
BLAST
Transmembranei882 – 90221HelicalSequence AnalysisAdd
BLAST
Transmembranei929 – 94921HelicalSequence AnalysisAdd
BLAST
Transmembranei1658 – 167821HelicalSequence AnalysisAdd
BLAST
Transmembranei1806 – 182621HelicalSequence AnalysisAdd
BLAST
Transmembranei1829 – 184921HelicalSequence AnalysisAdd
BLAST
Transmembranei1851 – 187121HelicalSequence AnalysisAdd
BLAST
Transmembranei1882 – 190221HelicalSequence AnalysisAdd
BLAST
Transmembranei2991 – 301121HelicalBy similarityAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini899 – 1026128Peptidase C18PROSITE-ProRule annotationAdd
BLAST
Domaini1217 – 1369153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2634 – 2752119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5958Interaction with DDX3XBy similarityAdd
BLAST
Regioni2 – 2322Interaction with STAT1By similarityAdd
BLAST
Regioni122 – 17352Interaction with APOA2By similarityAdd
BLAST
Regioni150 – 15910Mitochondrial targeting signalBy similarity
Regioni164 – 1674Important for lipid droplets localizationBy similarity
Regioni265 – 29632Fusion peptideSequence AnalysisAdd
BLAST
Regioni385 – 41127HVR1By similarityAdd
BLAST
Regioni475 – 4817HVR2By similarity
Regioni482 – 49413CD81-binding 1Sequence AnalysisAdd
BLAST
Regioni522 – 55332CD81-binding 2Sequence AnalysisAdd
BLAST
Regioni660 – 67112PKR/eIF2-alpha phosphorylation homology domain (PePHD)Add
BLAST
Regioni1679 – 169012NS3-binding (by NS4A)Sequence AnalysisAdd
BLAST
Regioni2120 – 2332213Transcriptional activationSequence AnalysisAdd
BLAST
Regioni2120 – 220889FKBP8-bindingSequence AnalysisAdd
BLAST
Regioni2200 – 225051Basal phosphorylationBy similarityAdd
BLAST
Regioni2210 – 227566PKR-bindingSequence AnalysisAdd
BLAST
Regioni2249 – 230658NS4B-bindingSequence AnalysisAdd
BLAST
Regioni2351 – 242070Basal phosphorylationBy similarityAdd
BLAST
Regioni2354 – 237724V3Add
BLAST

Motif

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

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.By similarity
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.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 NS3.1 Publication

Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 peptidase C18 domain.PROSITE-ProRule annotation
Contains 1 peptidase S29 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR
60 70 80 90 100
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP
110 120 130 140 150
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA
160 170 180 190 200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTVPAS AYQVRNSSGL
210 220 230 240 250
YHVTNDCPNS SVVYEAADAI LHTPGCVPCV REGNASRCWV AVTPTVATRD
260 270 280 290 300
GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRHHWT
310 320 330 340 350
TQDCNCSIYP GHITGHRMAW NMMMNWSPTA ALVVAQLLRI PQAIMDMIAG
360 370 380 390 400
AHWGVLAGIK YFSMVGNWAK VLVVLLLFAG VDAETHVTGG NAGRTTAGLV
410 420 430 440 450
GLLTPGAKQN IQLINTNGSW HINSTALNCN ESLNTGWLAG LFYQHKFNSS
460 470 480 490 500
GCPERLASCR RLTDFAQGWG PISYANGSGL DERPYCWHYP PRPCGIVPAK
510 520 530 540 550
SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ANDTDVFVLN NTRPPLGNWF
560 570 580 590 600
GCTWMNSTGF TKVCGAPPCV IGGVGNNTLL CPTDCFRKYP EATYSRCGSG
610 620 630 640 650
PRITPRCMVD YPYRLWHYPC TINYTIFKVR MYVGGVEHRL EAACNWTRGE
660 670 680 690 700
RCDLEDRDRS ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ
710 720 730 740 750
YLYGVGSSIA SWAIKWEYVV LLFLLLADAR VCSCLWMMLL ISQAEAALEN
760 770 780 790 800
LVILNAASLA GTHGLVSFLV FFCFAWYLKG RWVPGAVYAL YGMWPLLLLL
810 820 830 840 850
LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIS WCMWWLQYFL
860 870 880 890 900
TRVEAQLHVW VPPLNVRGGR DAVILLTCVV HPALVFDITK LLLAIFGPLW
910 920 930 940 950
ILQASLLKVP YFVRVQGLLR ICALARKIAG GHYVQMAIIK LGALTGTCVY
960 970 980 990 1000
NHLAPLRDWA HNGLRDLAVA VEPVVFSRME TKLITWGADT AACGDIINGL
1010 1020 1030 1040 1050
PVSARRGQEI LLGPADGMVS KGWRLLAPIT AYAQQTRGLL GCIITSLTGR
1060 1070 1080 1090 1100
DKNQVEGEVQ IVSTATQTFL ATCINGVCWT VYHGAGTRTI ASPKGPVIQT
1110 1120 1130 1140 1150
YTNVDQDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG
1160 1170 1180 1190 1200
SLLSPRPISY LKGSSGGPLL CPTGHAVGLF RAAVCTRGVA KAVDFIPVEN
1210 1220 1230 1240 1250
LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAKGYK
1260 1270 1280 1290 1300
VLVLNPSVAA TLGFGAYMSK AHGVDPNIRT GVRTITTGSP ITYSTYGKFL
1310 1320 1330 1340 1350
ADAGCSGGAY DIIICDECHS TDATSISGIG TVLDQAETAG ARLVVLATAT
1360 1370 1380 1390 1400
PPGSVTVSHP NIEEVALSTT GEIPFYGKAI PLEVIKGGRH LIFCHSKKKC
1410 1420 1430 1440 1450
DELAAKLVAL GINAVAYYRG LDVSVIPTSG DVVVVSTDAL MTGFTGDFDS
1460 1470 1480 1490 1500
VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR
1510 1520 1530 1540 1550
FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV
1560 1570 1580 1590 1600
CQDHLGFWEG VFTGLTHIDA HFLSQTKQSG ENFPYLVAYQ ATVCARAQAP
1610 1620 1630 1640 1650
PPSWDQMRKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMTCMS
1660 1670 1680 1690 1700
ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV VIVGRIVLSG KPAIIPDREV
1710 1720 1730 1740 1750
LYQEFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS RHAEVITPAV
1760 1770 1780 1790 1800
QTNWQKLEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP
1810 1820 1830 1840 1850
LTTGQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAALD SVGLGKVLVD
1860 1870 1880 1890 1900
ILAGYGAGVA GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALAVGVVFAS
1910 1920 1930 1940 1950
ILRRRVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTAILSS
1960 1970 1980 1990 2000
LTVTQLLRRL HQWISSECTT PCSGSWLRDI WDWICEVLSD FKTWLKAKLM
2010 2020 2030 2040 2050
PQLPGIPFVS CQRGYRGVWR GDGIMHTRCH CGAEITGHVK NGTMRIVGPR
2060 2070 2080 2090 2100
TCKNMWSGTF FINAYTTGPC TPLPAPNYKF ALWRVSAEEY VEIRRVGDFH
2110 2120 2130 2140 2150
YVSGMTTDNL KCPCQIPSPE FFTELDGVRL HRFAPPCKPL LREEVSFRVG
2160 2170 2180 2190 2200
LHEYPVGSQL PCEPEPDVAV LTSMLTDPSH ITAEAAGRRL ARGSPPSMAS
2210 2220 2230 2240 2250
SSASQLSAPS LKATCTANHD SPDAELIEAN LLWRQEMGGN ITRVESENKV
2260 2270 2280 2290 2300
VILDSFDPLV AEEDEREVSV PAEILRKSRR FAPALPVWAR PDYNPLLVET
2310 2320 2330 2340 2350
WKKPDYEPPV VHGCPLPPPR SPPVPPPRKK RTVVLTESTL PTALAELATK
2360 2370 2380 2390 2400
SFGSSSTSGI TGDNTTTSSE PAPSGCPPDS DVESYSSMPP LEGEPGDPDL
2410 2420 2430 2440 2450
SDGSWSTVSS GADTEDVVCC SMSYSWTGAL VTPCAAEEQK LPINALSNSL
2460 2470 2480 2490 2500
LRHHNLVYST TSRSACQRKK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA
2510 2520 2530 2540 2550
NLLSVEEACS LAPPHSAKSK FGYGAKDVRC HARKAVAHIN SVWKDLLEDS
2560 2570 2580 2590 2600
VTPIDTTIMA KNEVFCVQPE KGGRKPARLI VFPDLGVRVC EKMALYDVVS
2610 2620 2630 2640 2650
KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGLSYD TRCFDSTVTE
2660 2670 2680 2690 2700
SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR
2710 2720 2730 2740 2750
ASRVLTTSCG NTLTRYIKAR AACRAAGLQD CTMLVCGDDL VVICESAGVQ
2760 2770 2780 2790 2800
EDAASLRAFT EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR
2810 2820 2830 2840 2850
VYYLTRDPTT PLARAAWETA RHTPVNSWLG NIIMFAPTLW ARMILMTHFF
2860 2870 2880 2890 2900
SVLIARDQLE QALNCEIYGA CYSIEPLDLP PIIQRLHGLS AFSLHSYSPG
2910 2920 2930 2940 2950
EINRVAACLR KLGVPPLRAW RHRAWSVRAR LLARGGKAAI CGKYLFNWAV
2960 2970 2980 2990 3000
RTKLKLTPIT AAGRLDLSGW FTAGYSGGDI YHSVSHARPR WFWFCLLLLA
3010
AGVGIYLLPN R

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 [» ]
4Q0X X-ray 2.90 E 421-446 [» ]
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. 215 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: October 29, 2014
This is version 169 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