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Protein

Genome polyprotein

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

Functioni

Core protein p21: 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 (PubMed:23799612). Interacts with, and activates STAT3 leading to cellular transformation. 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. 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 (PubMed:11086025). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:14602201).5 Publications
Envelope glycoprotein E1: Forms a heterodimer with envelope glycoprotein E2 that mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to host LDLR, CD81 and SCARB1/SR-BI receptors (PubMed:12615904). However, additional liver specific cofactors may be required for entry. The fusion function is carried by E1 (PubMed:14990718, PubMed:15371595, PubMed:16894197, PubMed:16533059).5 Publications
Envelope glycoprotein E2: Forms a heterodimer with envelope glycoprotein E1 that mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to host LDLR, CD81 and SCARB1/SR-BI receptors (PubMed:12615904), but additional liver specific cofactors may be rewquired for entry. 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.3 Publications
Viroporin p7: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. Targets also host mitochondria and induces mitochondrial depolarization (PubMed:29039530). In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. In addition of its role as a viroporin, acts as a lipid raft adhesion factor (PubMed:27320856).4 Publications
Protease NS2-3: Cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation.1 Publication
Serine protease NS3: Displays three enzymatic activities: a serine protease with a chymotrypsin-like fold, a NTPase and a RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (PubMed:8189513). NS3/NS4A complex also prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS (PubMed:16301520).2 Publications
Non-structural protein 4A: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease.1 Publication
Non-structural protein 4B: 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 (PubMed:23868571). Plays also a role in the inhibition of host innate response by inhibiting host TLR3-mediated interferon signaling. Mechanistically, promotes host TRIF protein degradation in a caspase8-dependent manner (PubMed:29782532).3 Publications
Non-structural protein 5A: Component of the replication complex involved in RNA-binding. Its interaction with host 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. The hyperphosphorylated form of NS5A is an inhibitor of viral replication.2 Publications
RNA-directed RNA polymerase: Plays an essential role in the virus replication.1 Publication

Miscellaneous

Cell culture adaptation of the virus leads to mutations in NS5A, reducing its inhibitory effect on replication.By similarity
Core protein exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding.By similarity

Caution

The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs.Curated

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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per NS3 protease domain.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per NS5A N-terminal domain.By similarity

Activity regulationi

Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA. Serine protease NS3 is also activated by zinc ions (By similarity). Activity is up-regulated by PKN2-mediated phosphorylation.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei952For protease NS2-3 activity; shared with dimeric partner1
Active sitei972For protease NS2-3 activity; shared with dimeric partner1
Active sitei993For protease NS2-3 activity; shared with dimeric partner1
Active sitei1083Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1107Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Metal bindingi1123ZincPROSITE-ProRule annotation1
Metal bindingi1125ZincPROSITE-ProRule annotation1
Active sitei1165Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Metal bindingi1171ZincPROSITE-ProRule annotation1
Metal bindingi1175ZincPROSITE-ProRule annotation1
Metal bindingi2011ZincBy similarity1
Metal bindingi2029ZincBy similarity1
Metal bindingi2031ZincBy similarity1
Metal bindingi2052ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1230 – 1237ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Multifunctional enzyme, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-binding, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel, Viral nucleoprotein
Biological processActivation of host autophagy by virus, Apoptosis, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, G1/S host cell cycle checkpoint dysregulation by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host TRAFs by virus, Interferon antiviral system evasion, Ion transport, Modulation of host cell cycle by virus, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.21.98 2642
3.6.4.13 2642
ReactomeiR-HSA-8854214 TBC/RABGAPs

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 virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeHepacivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000115192 Componenti: Genome
  • UP000000518 Componenti: Genome

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 168CytoplasmicSequence analysisAdd BLAST167
Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 358LumenalSequence analysisAdd BLAST169
Transmembranei359 – 379HelicalSequence analysisAdd BLAST21
Topological domaini380 – 725LumenalSequence analysisAdd BLAST346
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 757LumenalSequence analysisAdd BLAST11
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 782CytoplasmicSequence analysis4
Transmembranei783 – 803HelicalSequence analysisAdd BLAST21
Topological domaini804 – 813LumenalSequence analysis10
Transmembranei814 – 834HelicalSequence analysisAdd BLAST21
Topological domaini835 – 881CytoplasmicSequence analysisAdd BLAST47
Transmembranei882 – 902HelicalSequence analysisAdd BLAST21
Topological domaini903 – 928LumenalSequence analysisAdd BLAST26
Transmembranei929 – 949HelicalSequence analysisAdd BLAST21
Topological domaini950 – 1657CytoplasmicSequence analysisAdd BLAST708
Transmembranei1658 – 1678HelicalSequence analysisAdd BLAST21
Topological domaini1679 – 1805CytoplasmicSequence analysisAdd BLAST127
Transmembranei1806 – 1826HelicalSequence analysisAdd BLAST21
Topological domaini1827 – 1828LumenalSequence analysis2
Transmembranei1829 – 1849HelicalSequence analysisAdd BLAST21
Topological domaini1850CytoplasmicSequence analysis1
Transmembranei1851 – 1871HelicalSequence analysisAdd BLAST21
Topological domaini1872 – 1881LumenalSequence analysis10
Transmembranei1882 – 1902HelicalSequence analysisAdd BLAST21
Topological domaini1903 – 1972CytoplasmicSequence analysisAdd BLAST70
Intramembranei1973 – 2002By similarityAdd BLAST30
Topological domaini2003 – 2990CytoplasmicSequence analysisAdd BLAST988
Transmembranei2991 – 3011HelicalBy similarityAdd BLAST21

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi720V → L: Increases processing between E2 and p7. 1 Publication1
Mutagenesisi779K → I: Virus can no longer infect chimpanzee. 1 Publication1
Mutagenesisi781R → S: Virus can no longer infect chimpanzee. 1 Publication1
Mutagenesisi952H → A: Complete loss of NS2-NS3 cleavage. 2 Publications1
Mutagenesisi993C → A: Complete loss of NS2-NS3 cleavage. 2 Publications1
Mutagenesisi1165S → A: Complete loss of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B cleavages. 1 Publication1
Mutagenesisi1968C → A: Strong decrease in NS4B palmitoylation. 1 Publication1
Mutagenesisi1972C → A: Slight decrease in NS4B palmitoylation. 1 Publication1
Mutagenesisi2321S → A: Loss of phosphorylation. 1 Publication1

Keywords - Diseasei

Oncogene

Chemistry databases

ChEMBLiCHEMBL3638344
DrugBankiDB08644 {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00000375662 – 191Core protein p21Sequence analysisAdd BLAST190
ChainiPRO_00000375672 – 177Core protein p19By similarityAdd BLAST176
PropeptideiPRO_0000037568178 – 191ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityAdd BLAST14
ChainiPRO_0000037569192 – 383Envelope glycoprotein E1Sequence analysisAdd BLAST192
ChainiPRO_0000037570384 – 746Envelope glycoprotein E2Sequence analysisAdd BLAST363
ChainiPRO_0000037571747 – 809Viroporin p7Add BLAST63
ChainiPRO_0000037572810 – 1026Protease NS2-3PROSITE-ProRule annotationAdd BLAST217
ChainiPRO_00000375731027 – 1657Serine protease NS3Sequence analysisAdd BLAST631
ChainiPRO_00000375741658 – 1711Non-structural protein 4ASequence analysisAdd BLAST54
ChainiPRO_00000375751712 – 1972Non-structural protein 4BSequence analysisAdd BLAST261
ChainiPRO_00000375761973 – 2420Non-structural protein 5ASequence analysisAdd BLAST448
ChainiPRO_00000375772421 – 3011RNA-directed RNA polymeraseSequence analysisAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine; by hostBy similarity1
Modified residuei53Phosphoserine; by hostBy similarity1
Modified residuei99Phosphoserine; by hostBy similarity1
Modified residuei116Phosphoserine; by host PKABy similarity1
Glycosylationi196N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi209N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi305N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi417N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi423N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi430N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi476N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi532N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi540N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi556N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi576N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi623N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi645N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Lipidationi1968S-palmitoyl cysteine; by host1 Publication1
Lipidationi1972S-palmitoyl cysteine; by host; partial1 Publication1
Disulfide bondi2114 ↔ 2162By similarity
Modified residuei2194Phosphoserine; by host; in p56By similarity1
Modified residuei2197Phosphoserine; by host; in p58By similarity1
Modified residuei2201Phosphoserine; by host; in p58By similarity1
Modified residuei2204Phosphoserine; by host; in p58By similarity1
Modified residuei2321Phosphoserine; by host1 Publication1
Cross-linki2350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Non-structural protein 5A: Ubiquitinated. Ubiquitination, most probably at Lys-2350, mediated by host IFI27 and SKP2 leads to proteasomal degradation, restricting viral infection.1 Publication
Genome polyprotein: 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.2 Publications
Envelope glycoprotein E1: Highly N-glycosylated.
Envelope glycoprotein E2: Highly N-glycosylated.
Core protein Phosphorylated by host PKC and PKA.By similarity
Non-structural protein 5A: 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
Core protein p21: Ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity
Non-structural protein 4B: Palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei177 – 178Cleavage; by host signal peptidaseBy similarity2
Sitei191 – 192Cleavage; by host signal peptidaseSequence analysis2
Sitei383 – 384Cleavage; by host signal peptidaseSequence analysis2
Sitei746 – 747Cleavage; by host signal peptidase2
Sitei809 – 810Cleavage; by host signal peptidase2
Sitei1026 – 1027Cleavage; by protease NS2-3PROSITE-ProRule annotation2
Sitei1657 – 1658Cleavage; by serine protease NS3Sequence analysis2
Sitei1711 – 1712Cleavage; by serine protease NS3Sequence analysis2
Sitei1972 – 1973Cleavage; by serine protease NS3Sequence analysis2
Sitei2420 – 2421Cleavage; by serine protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP27958

PTM databases

iPTMnetiP27958
SwissPalmiP27958

Interactioni

Subunit structurei

Core protein p21: Homooligomer (PubMed:25351725). Interacts with the C-terminal part of E1 (PubMed:8764026). Interacts (via N-terminus) with host STAT1; this interaction results in decreased STAT1 phosphorylation, leading to decreased IFN-stimulated gene transcription (PubMed:23799612). 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, YWHAE, UBE3A/E6AP, DDX3X, APOA2 and RXRA proteins. Interacts with human cytokeratins KRT8, KRT18, KRT19 and VIM/vimentin. Interacts with human ACY3 (PubMed:19486448). Interacts with host C1QR1 (PubMed:11086025). Envelope glycoprotein E1: Forms a heterodimer with envelope glycoprotein E2 that binds to human LDLR, CLDN1, CD81 and SCARB1 receptors (PubMed:12970454, PubMed:12615904, PubMed:12913001). Interacts with core protein p21 (PubMed:8764026). Envelope glycoprotein E2: Forms a heterodimer with envelope glycoprotein E1 that binds to human LDLR, CLDN1, CD81 and SCARB1 receptors. Interacts with and inhibits host EIF2AK2/PKR. Interacts with host CD209/DC-SIGN and CLEC4M/DC-SIGNR (PubMed:15371595). Viroporin p7: forms a homohexamer (PubMed:12560074). Protease NS2-3: Forms a homodimer containing a pair of composite active sites at the dimerization interface. Serine protease NS3: Interacts with host TANK-binding kinase/TBK1 and MAVS (PubMed:16301520). Interacts with non-structural protein 4A (PubMed:8861917). Non-structural protein 4A: 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. Non-structural protein NS4B: Homomultimerizes (PubMed:23868571). Interacts with non-structural protein NS5A (PubMed:23868571). Non-structural protein NS5A: Interacts with host EIF2AK2/PKR, FKBP8, GRB2, BIN1, PIK3R1, SRCAP, VAPB and with most Src-family kinases (PubMed:16951545, PubMed:10702287, PubMed:16530520). Interacts with host IFI27 and SKP2; promotes the ubiquitin-mediated proteasomal degradation of NS5A (PubMed:27194766). Interacts with non-structural protein NS4B (PubMed:23868571). RNA-directed RNA polymerase: Homooligomer. Interacts with host VAPB, HNRNPA1 and SEPT6. Interacts with host PKN2 (PubMed:15364941). Interacts with host HNRNPA1 and SEPT6 (PubMed:17229681).20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P266604EBI-6377335,EBI-6875462From Hepatitis C virus genotype 2a (isolate HC-J6).
Q99IB83EBI-8753518,EBI-6858513From Hepatitis C virus genotype 2a (isolate JFH-1).
ACTN1P128147EBI-6904388,EBI-351710From Homo sapiens.
AP2M1Q96CW14EBI-6377335,EBI-297683From Homo sapiens.
APOEP026494EBI-6904269,EBI-1222467From Homo sapiens.
ARAP1Q96P483EBI-8753518,EBI-710003From Homo sapiens.
ATF6BQ999415EBI-8763498,EBI-2841031From Homo sapiens.
ATMQ133153EBI-6904388,EBI-495465From Homo sapiens.
BIN1O0049911EBI-8753518,EBI-719094From Homo sapiens.
BIN1O00499-72EBI-8753518,EBI-8870146From a different organism.
C1QBPQ070214EBI-6377335,EBI-347528From Homo sapiens.
CCDC86Q9H6F53EBI-8753518,EBI-721289From Homo sapiens.
CD81P6003311EBI-6904269,EBI-712921From Homo sapiens.
CDKN1AP389363EBI-6377335,EBI-375077From Homo sapiens.
CHEK2O960173EBI-6904388,EBI-1180783From Homo sapiens.
CIDEBQ9UHD46EBI-6919131,EBI-7062247From Homo sapiens.
CNXQ920L92EBI-6904269,EBI-9209498From Mesocricetus auratus.
CRABP1P297623EBI-8753518,EBI-725950From Homo sapiens.
DDX3XO0057111EBI-6377335,EBI-353779From Homo sapiens.
DDX5P1784412EBI-6904388,EBI-351962From Homo sapiens.
EIF2AK2P195255EBI-8753518,EBI-640775From Homo sapiens.
Eif2ak3Q9Z2B55EBI-6904269,EBI-1226344From Mus musculus.
EIF4A2Q142404EBI-6904388,EBI-73473From Homo sapiens.
ERC1Q8IUD2-38EBI-3649474,EBI-9352449From a different organism.
ERC1Q8IUD2-43EBI-3649474,EBI-9352501From a different organism.
FGBP026754EBI-6377335,EBI-1034445From Homo sapiens.
FYNP062414EBI-706378,EBI-515315From Homo sapiens.
GRB2P629933EBI-706378,EBI-401755From Homo sapiens.
HCKP086315EBI-706378,EBI-346340From Homo sapiens.
HNRNPA1P096514EBI-6904388,EBI-352662From Homo sapiens.
HSPA5P078233EBI-6904269,EBI-371776From Mesocricetus auratus.
IKBKEQ141642EBI-6919131,EBI-307369From Homo sapiens.
IPO5O004105EBI-8753518,EBI-356424From Homo sapiens.
LckP062403EBI-706378,EBI-1401From Mus musculus.
LTFP027889EBI-6904269,EBI-1058602From Homo sapiens.
LTFP246273EBI-6904269,EBI-8076910From Bos taurus.
LYNP079484EBI-706378,EBI-79452From Homo sapiens.
MAPKAPK3Q166445EBI-6377335,EBI-1384657From Homo sapiens.
NCLP193384EBI-6904388,EBI-346967From Homo sapiens.
PI4KAP423567EBI-8753518,EBI-723050From Homo sapiens.
PMLP295906EBI-6377335,EBI-295890From Homo sapiens.
PSMB8P280624EBI-3649474,EBI-372294From Homo sapiens.
SCARB1Q8WTV02EBI-6904269,EBI-78657From Homo sapiens.
SEPT6Q141414EBI-6904388,EBI-745901From Homo sapiens.
SNRPD1P623147EBI-3649474,EBI-372177From Homo sapiens.
STAT1P422242EBI-6377335,EBI-1057697From Homo sapiens.
TBC1D20Q96BZ911EBI-8753518,EBI-9254454From Homo sapiens.
TBK1Q9UHD24EBI-3649474,EBI-356402From Homo sapiens.
TMEM173Q86WV65EBI-8763498,EBI-2800345From Homo sapiens.
TP53BP2Q136255EBI-6377335,EBI-77642From Homo sapiens.
Traf2P394295EBI-8753518,EBI-520016From Mus musculus.
VAPAQ9P0L07EBI-8753518,EBI-1059156From Homo sapiens.
VIMP086704EBI-6377335,EBI-353844From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

ELMiP27958
IntActiP27958, 234 interactors

Chemistry databases

BindingDBiP27958

Structurei

Secondary structure

13011
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00588
ProteinModelPortaliP27958
SMRiP27958
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27958

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini899 – 1026Peptidase C18PROSITE-ProRule annotationAdd BLAST128
Domaini1027 – 1208Peptidase S29PROSITE-ProRule annotationAdd BLAST182
Domaini1217 – 1369Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini2634 – 2752RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 59Interaction with DDX3XBy similarityAdd BLAST58
Regioni2 – 23Interaction with STAT1By similarityAdd BLAST22
Regioni122 – 173Interaction with APOA2By similarityAdd BLAST52
Regioni150 – 159Mitochondrial targeting signalBy similarity10
Regioni164 – 167Important for lipid droplets localizationBy similarity4
Regioni265 – 296Fusion peptide1 PublicationAdd BLAST32
Regioni385 – 411HVR11 PublicationAdd BLAST27
Regioni475 – 481HVR21 Publication7
Regioni482 – 494CD81-binding 1Sequence analysisAdd BLAST13
Regioni522 – 553CD81-binding 2Sequence analysisAdd BLAST32
Regioni660 – 671PKR/eIF2-alpha phosphorylation homology domain (PePHD)Add BLAST12
Regioni1679 – 1690NS3-binding (by NS4A)Sequence analysisAdd BLAST12
Regioni2120 – 2332Transcriptional activationSequence analysisAdd BLAST213
Regioni2120 – 2208FKBP8-bindingSequence analysisAdd BLAST89
Regioni2189 – 2441Interaction with host SKP21 PublicationAdd BLAST253
Regioni2200 – 2250Basal phosphorylationBy similarityAdd BLAST51
Regioni2210 – 2275PKR-bindingSequence analysisAdd BLAST66
Regioni2249 – 2306NS4B-bindingSequence analysisAdd BLAST58
Regioni2332 – 2441Interaction with host IFI271 PublicationAdd BLAST110
Regioni2351 – 2420Basal phosphorylationBy similarityAdd BLAST70
Regioni2354 – 2377V3Add BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi5 – 13Nuclear localization signalSequence analysis9
Motifi38 – 43Nuclear localization signalSequence analysis6
Motifi58 – 64Nuclear localization signalSequence analysis7
Motifi66 – 71Nuclear localization signalSequence analysis6
Motifi1316 – 1319DECH box4
Motifi2322 – 2325SH3-bindingSequence analysis4
Motifi2327 – 2335Nuclear localization signalSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi796 – 803Poly-Leu8
Compositional biasi1432 – 1435Poly-Val4
Compositional biasi2286 – 2327Pro-richAdd BLAST42
Compositional biasi2996 – 2999Poly-Leu4

Domaini

Envelope glycoprotein E1: The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins.1 Publication
Envelope glycoprotein E2: 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.1 Publication
Non-structural protein 5A: the N-terminal 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
Non-structural protein 5A: The SH3-binding domain is involved in the interaction with host BIN1, GRB2 and Src-family kinases.1 Publication
Serine protease NS3: The N-terminal 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

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900004E

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di2.20.25.210, 1 hit
2.20.25.220, 1 hit
InterProiView protein in InterPro
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
IPR038568 HCV_NS5A_1B_sf
IPR024350 HCV_NS5a_C
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR013192 NS5A_1a
IPR038170 NS5A_1a_sf
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR004109 Peptidase_S29_NS3
IPR007094 RNA-dir_pol_PSvirus
IPR002166 RNA_pol_HCV
PfamiView protein in Pfam
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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001388 HCV_env, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51693 HCV_NS2_PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51822 HV_PV_NS3_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

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. AlignAdd to basket
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)DescriptionActionsGraphical viewLength
Natural varianti212V → I in strain: Isolate H77. 1
Natural varianti297H → R in strain: Isolate H77. 1
Natural varianti303D → S in strain: Isolate H77. 1
Natural varianti321N → D in strain: Isolate H77. 1
Natural varianti360K → A in strain: Isolate H77. 1
Natural varianti391N → S in strain: Isolate H77. 1
Natural varianti394R → H in strain: Isolate H77. 1
Natural varianti431E → D in strain: Isolate H77. 1
Natural varianti434N → T in strain: Isolate H77. 1
Natural varianti444Q → R in strain: Isolate H77. 1
Natural varianti457A → T in strain: Isolate H77. 1
Natural varianti564 – 566CGA → RGV in strain: Isolate H77. 3
Natural varianti589Y → H in strain: Isolate H77. 1
Natural varianti602R → W in strain: Isolate H77. 1
Natural varianti650E → G in strain: Isolate H77. 1
Natural varianti773C → R in strain: Isolate H77. 1
Natural varianti787V → A in strain: Isolate H77. 1
Natural varianti790L → F in strain: Isolate H77. 1
Natural varianti877T → M in strain: Isolate H77. 1
Natural varianti883A → T in strain: Isolate H77. 1
Natural varianti948C → Y in strain: Isolate H77. 1
Natural varianti954A → T in strain: Isolate H77. 1
Natural varianti1026L → Q in strain: Isolate H77. 1
Natural varianti1033A → T in strain: Isolate H77. 1
Natural varianti1049G → S in strain: Isolate H77. 1
Natural varianti1100T → M in strain: Isolate H77. 1
Natural varianti1121T → A in strain: Isolate H77. 1
Natural varianti1173T → A in strain: Isolate H77. 1
Natural varianti1202E → G in strain: Isolate H77. 1
Natural varianti1214S → P in strain: Isolate H77. 1
Natural varianti1247K → Q in strain: Isolate H77. 1
Natural varianti1303A → G in strain: Isolate H77. 1
Natural varianti1327S → L in strain: Isolate H77. 1
Natural varianti1556G → E in strain: Isolate H77. 1
Natural varianti1608R → W in strain: Isolate H77. 1
Natural varianti1742H → Q in strain: Isolate H77. 1
Natural varianti1839 – 1840LD → IG in strain: Isolate H77. 2
Natural varianti1893A → V in strain: Isolate H77. 1
Natural varianti1898 – 1900FAS → CAA in strain: Isolate H77. 3
Natural varianti1905R → H in strain: Isolate H77. 1
Natural varianti1940A → V in strain: Isolate H77. 1
Natural varianti2043T → A in strain: Isolate H77. 1
Natural varianti2053K → R in strain: Isolate H77. 1
Natural varianti2061F → L in strain: Isolate H77. 1
Natural varianti2102V → I in strain: Isolate H77. 1
Natural varianti2185A → E in strain: Isolate H77. 1
Natural varianti2283P → R in strain: Isolate H77. 1
Natural varianti2296L → P in strain: Isolate H77. 1
Natural varianti2341P → S in strain: Isolate H77. 1
Natural varianti2355S → P in strain: Isolate H77. 1
Natural varianti2400L → F in strain: Isolate H77. 1
Natural varianti2425S → T in strain: Isolate H77. 1
Natural varianti2469K → Q in strain: Isolate H77. 1
Natural varianti2512A → T in strain: Isolate H77. 1
Natural varianti2637L → F in strain: Isolate H77. 1
Natural varianti2703R → G in strain: Isolate H77. 1
Natural varianti2715R → C in strain: Isolate H77. 1
Natural varianti2755S → N in strain: Isolate H77. 1
Natural varianti2925W → R in strain: Isolate H77. 1
Natural varianti2933A → S in strain: Isolate H77. 1
Natural varianti2937K → R in strain: Isolate H77. 1
Natural varianti2960T → A in strain: Isolate H77. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Cross-referencesi

Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N1PNMR-A2982-3011[»]
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[»]
4N0YX-ray1.75A314-324[»]
4Q0XX-ray2.90E421-446[»]
4XVJX-ray2.00A412-423[»]
4Z0XX-ray2.00C435-446[»]
5EOCX-ray1.98P/Q412-422[»]
5ERWX-ray2.90C434-446[»]
5FGBX-ray1.65F/G405-425[»]
5FGCX-ray1.90A405-425[»]
5JZIX-ray2.50C/H1406-1415[»]
DisProtiDP00588
ProteinModelPortaliP27958
SMRiP27958
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ELMiP27958
IntActiP27958, 234 interactors

Chemistry databases

BindingDBiP27958
ChEMBLiCHEMBL3638344
DrugBankiDB08644 {1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER

PTM databases

iPTMnetiP27958
SwissPalmiP27958

Proteomic databases

PRIDEiP27958

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

euHCVdbiAF009606
AF011751
AF011752
AF011753
M67463

Phylogenomic databases

OrthoDBiVOG0900004E

Enzyme and pathway databases

BRENDAi3.4.21.98 2642
3.6.4.13 2642
ReactomeiR-HSA-8854214 TBC/RABGAPs

Miscellaneous databases

EvolutionaryTraceiP27958

Family and domain databases

CDDicd00079 HELICc, 1 hit
Gene3Di2.20.25.210, 1 hit
2.20.25.220, 1 hit
InterProiView protein in InterPro
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
IPR038568 HCV_NS5A_1B_sf
IPR024350 HCV_NS5a_C
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR013192 NS5A_1a
IPR038170 NS5A_1a_sf
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR004109 Peptidase_S29_NS3
IPR007094 RNA-dir_pol_PSvirus
IPR002166 RNA_pol_HCV
PfamiView protein in Pfam
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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001388 HCV_env, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS51693 HCV_NS2_PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51822 HV_PV_NS3_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HCVH
AccessioniPrimary (citable) accession number: P27958
Secondary accession number(s): O36579
, O36608, O36609, O36610
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 209 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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