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UniProtKB - P26663 (POLG_HCVBK)

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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis C virus genotype 1b (isolate BK) (HCV)
Status
Reviewed-Annotation score: -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. Also inhibited by long-alkyl-chain iminosugar derivatives. Essential for infectivity (By similarity).By similarity
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation (By similarity).By similarity
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS (By similarity).By similarity
NS4B induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex (By similarity).By similarity
NS5A is a component of the replication complex involved in RNA-binding. Its interaction with Human VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. Seems to inhibit apoptosis by interacting with BIN1 and FKBP8. The hyperphosphorylated form of NS5A is an inhibitor of viral replication (By similarity).By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Miscellaneous

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

Caution

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

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

Enzyme regulationi

Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA, 1,10-phenanthroline, iodocetamide and N-ethylmaleimide. According to PubMed:9261354, completely inhibited by the serine protease inhibitors TLCK and TPCK. According to PubMed:8189501, almost completely inhibited by TPCK and slightly inhibited by TLCK. Not inhibited by antipain, aprotinin, E64, PMSF and pepstatin. Also inhibited by NS2-3 and NS4A derived peptides. Serine protease NS3 is also activated by zinc ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei952For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei972For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei993For protease NS2-3 activity; shared with dimeric partnerPROSITE-ProRule annotation1
Active sitei1083Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1107Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

BRENDAi2.7.7.48 2642
3.4.21.98 2642
3.6.4.13 2642

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 11 chains:
Core protein p21
Alternative name(s):
Capsid protein C
p21
Core protein p19
Envelope glycoprotein E1
Alternative name(s):
gp32
gp35
Envelope glycoprotein E2
Alternative name(s):
NS1
gp68
gp70
p7
Protease NS2-3 (EC:3.4.22.-)
Short name:
p23
Serine protease NS3 (EC:3.4.21.98, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Hepacivirin
NS3P
p70
Non-structural protein 4A
Short name:
NS4A
Alternative name(s):
p8
Non-structural protein 4B
Short name:
NS4B
Alternative name(s):
p27
Non-structural protein 5A
Short name:
NS5A
Alternative name(s):
p56
RNA-directed RNA polymerase (EC:2.7.7.48)
Alternative name(s):
NS5B
p68
OrganismiHepatitis C virus genotype 1b (isolate BK) (HCV)
Taxonomic identifieri11105 [NCBI]
Taxonomic lineageiViruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Hepacivirus ›
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007413 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 By similarity; Single-pass type I membrane protein By similarity
    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E1 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
Envelope glycoprotein E2 :
  • Virion membrane Curated; Single-pass type I membrane protein Curated
  • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein. ER retention of E2 is leaky and, in overexpression conditions, only a small fraction reaches the plasma membrane.
p7 :
Protease NS2-3 :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
Non-structural protein 5A :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 – 2989CytoplasmicSequence analysisAdd BLAST987
Transmembranei2990 – 3010HelicalBy similarityAdd BLAST21

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • host cell cytoplasm Source: AgBase
  • host cell cytosol Source: AgBase
  • host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • host cell lipid droplet Source: UniProtKB-SubCell
  • host cell mitochondrial membrane Source: UniProtKB-SubCell
  • host cell nucleus Source: AgBase
  • host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • host cell plasma membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • integral to membrane of host cell Source: UniProtKB-KW
  • viral envelope Source: UniProtKB-KW
  • viral nucleocapsid Source: UniProtKB-KW
  • virion membrane Source: UniProtKB-SubCell
View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2194S → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi2322P → A: Complete loss of binding to GRB2. 1 Publication1
Mutagenesisi2323P → A: Complete loss of binding to GRB2. 1 Publication1
Mutagenesisi2326P → A: Complete loss of binding to GRB2. 1 Publication1

Keywords - Diseasei

Oncogene

Chemistry databases

ChEMBLiCHEMBL6040
DrugBankiDB07570 3-CYCLOHEXYL-1-(2-MORPHOLIN-4-YL-2-OXOETHYL)-2-PHENYL-1H-INDOLE-6-CARBOXYLIC ACID
DB08279 3-{ISOPROPYL[(TRANS-4-METHYLCYCLOHEXYL)CARBONYL]AMINO}-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID
DB08578 4-[(5-bromopyridin-2-yl)amino]-4-oxobutanoic acid
DB08580 4-bromo-2-{[(2R)-2-(2-chlorobenzyl)pyrrolidin-1-yl]carbonyl}aniline
DB07238 5-cyclopropyl-2-(4-fluorophenyl)-6-[(2-hydroxyethyl)(methylsulfonyl)amino]-N-methyl-1-benzofuran-3-carboxamide
DB04137 Guanosine-5'-Triphosphate
DB04005 Uridine 5'-Triphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00000375292 – 191Core protein p21Sequence analysisAdd BLAST190
ChainiPRO_00000375302 – 177Core protein p19By similarityAdd BLAST176
PropeptideiPRO_0000037531178 – 191ER anchor for the core protein, removed in mature form by host signal peptidaseBy similarityAdd BLAST14
ChainiPRO_0000037532192 – 383Envelope glycoprotein E1Sequence analysisAdd BLAST192
ChainiPRO_0000037533384 – 746Envelope glycoprotein E2Sequence analysisAdd BLAST363
ChainiPRO_0000037534747 – 809p7By similarityAdd BLAST63
ChainiPRO_0000037535810 – 1026Protease NS2-3PROSITE-ProRule annotationAdd BLAST217
ChainiPRO_00000375361027 – 1657Serine protease NS3Add BLAST631
ChainiPRO_00000375371658 – 1711Non-structural protein 4AAdd BLAST54
ChainiPRO_00000375381712 – 1972Non-structural protein 4BAdd BLAST261
ChainiPRO_00000375391973 – 2419Non-structural protein 5AAdd BLAST447
ChainiPRO_00000375402420 – 3010RNA-directed RNA polymeraseAdd 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
Glycosylationi250N-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
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 hostBy similarity1
Lipidationi1972S-palmitoyl cysteine; by hostBy similarity1
Disulfide bondi2114 ↔ 2162By similarity
Modified residuei2194Phosphoserine; by host; in p561 Publication1
Modified residuei2197Phosphoserine; by host; in p58By similarity1
Modified residuei2201Phosphoserine; by host; in p58By similarity1
Modified residuei2204Phosphoserine; by host; in p58By similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases. The core protein is synthesized as a 21 kDa precursor which is retained in the ER membrane through the hydrophobic signal peptide. Cleavage by the signal peptidase releases the 19 kDa mature core protein. The other proteins (p7, NS2-3, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity).By similarity
Envelope E1 and E2 glycoproteins are highly N-glycosylated.By similarity
Core protein is phosphorylated by host PKC and PKA.By similarity
NS5A is phosphorylated in a basal form termed p56. p58 is a hyperphosphorylated form of p56. p56 and p58 coexist in the cell in roughly equivalent amounts. Hyperphosphorylation is dependent on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1, MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for NS5A phosphorylation.1 Publication
NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions (By similarity).By similarity
The N-terminus of a fraction of NS4B molecules seems to be relocated post-translationally from the cytoplasm to the ER lumen, with a 5th transmembrane segment. The C-terminus of NS2 may be lumenal with a fourth transmembrane segment (By similarity).By similarity
Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei177 – 178Cleavage; by host signal peptidaseBy similarity2
Sitei191 – 192Cleavage; by host signal peptidaseSequence analysis2
Sitei383 – 384Cleavage; by host signal peptidaseSequence analysis2
Sitei746 – 747Cleavage; by host signal peptidaseBy similarity2
Sitei809 – 810Cleavage; by host signal peptidaseBy similarity2
Sitei1026 – 1027Cleavage; by protease NS2-3PROSITE-ProRule annotation2
Sitei1657 – 1658Cleavage; by serine protease NS3Sequence analysis2
Sitei1711 – 1712Cleavage; by serine protease NS3Sequence analysis2
Sitei1972 – 1973Cleavage; by serine protease NS3Sequence analysis2
Sitei2419 – 2420Cleavage; by serine protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRIDEiP26663

PTM databases

iPTMnetiP26663

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protease binding Source: AgBase
  • SH3 domain binding Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActiP26663, 6 interactors
MINTiP26663

Chemistry databases

BindingDBiP26663

Structurei

Secondary structure

13010
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi413 – 416Combined sources4
Beta strandi419 – 422Combined sources4
Helixi925 – 929Combined sources5
Beta strandi936 – 942Combined sources7
Beta strandi947 – 953Combined sources7
Beta strandi967 – 969Combined sources3
Beta strandi972 – 978Combined sources7
Turni979 – 982Combined sources4
Beta strandi983 – 987Combined sources5
Beta strandi995 – 1004Combined sources10
Beta strandi1006 – 1014Combined sources9
Helixi1015 – 1018Combined sources4
Beta strandi1024 – 1026Combined sources3
Beta strandi1031 – 1035Combined sources5
Helixi1039 – 1048Combined sources10
Beta strandi1057 – 1063Combined sources7
Beta strandi1068 – 1074Combined sources7
Beta strandi1077 – 1080Combined sources4
Helixi1082 – 1085Combined sources4
Beta strandi1090 – 1092Combined sources3
Beta strandi1095 – 1097Combined sources3
Beta strandi1100 – 1103Combined sources4
Turni1104 – 1107Combined sources4
Beta strandi1108 – 1112Combined sources5
Helixi1123 – 1127Combined sources5
Beta strandi1128 – 1133Combined sources6
Beta strandi1135 – 1137Combined sources3
Beta strandi1139 – 1144Combined sources6
Beta strandi1146 – 1157Combined sources12
Helixi1158 – 1161Combined sources4
Beta strandi1168 – 1170Combined sources3
Turni1172 – 1174Combined sources3
Beta strandi1176 – 1186Combined sources11
Beta strandi1189 – 1197Combined sources9
Helixi1198 – 1206Combined sources9
Beta strandi1207 – 1215Combined sources9
Beta strandi1224 – 1229Combined sources6
Beta strandi1232 – 1235Combined sources4
Turni1236 – 1238Combined sources3
Helixi1239 – 1246Combined sources8
Beta strandi1251 – 1256Combined sources6
Helixi1258 – 1272Combined sources15
Turni1273 – 1275Combined sources3
Beta strandi1277 – 1279Combined sources3
Helixi1287 – 1289Combined sources3
Beta strandi1290 – 1295Combined sources6
Helixi1296 – 1301Combined sources6
Beta strandi1307 – 1309Combined sources3
Beta strandi1311 – 1315Combined sources5
Turni1316 – 1319Combined sources4
Helixi1323 – 1335Combined sources13
Turni1336 – 1340Combined sources5
Beta strandi1342 – 1350Combined sources9
Beta strandi1362 – 1366Combined sources5
Beta strandi1371 – 1375Combined sources5
Beta strandi1378 – 1380Combined sources3
Helixi1382 – 1384Combined sources3
Beta strandi1386 – 1393Combined sources8
Helixi1397 – 1409Combined sources13
Beta strandi1414 – 1417Combined sources4
Beta strandi1419 – 1421Combined sources3
Helixi1423 – 1425Combined sources3
Beta strandi1428 – 1430Combined sources3
Beta strandi1432 – 1436Combined sources5
Helixi1438 – 1441Combined sources4
Turni1442 – 1444Combined sources3
Beta strandi1448 – 1453Combined sources6
Beta strandi1456 – 1463Combined sources8
Beta strandi1467 – 1469Combined sources3
Beta strandi1471 – 1478Combined sources8
Helixi1481 – 1488Combined sources8
Beta strandi1493 – 1495Combined sources3
Beta strandi1497 – 1503Combined sources7
Beta strandi1509 – 1511Combined sources3
Helixi1514 – 1526Combined sources13
Helixi1532 – 1544Combined sources13
Helixi1555 – 1563Combined sources9
Helixi1570 – 1579Combined sources10
Helixi1584 – 1596Combined sources13
Helixi1606 – 1611Combined sources6
Turni1612 – 1614Combined sources3
Helixi1615 – 1617Combined sources3
Beta strandi1625 – 1629Combined sources5
Beta strandi1635 – 1637Combined sources3
Helixi1640 – 1650Combined sources11
Turni1653 – 1655Combined sources3
Beta strandi1680 – 1688Combined sources9
Beta strandi1690 – 1693Combined sources4
Beta strandi2421 – 2425Combined sources5
Helixi2446 – 2449Combined sources4
Helixi2453 – 2455Combined sources3
Beta strandi2456 – 2458Combined sources3
Helixi2461 – 2463Combined sources3
Helixi2464 – 2471Combined sources8
Helixi2481 – 2494Combined sources14
Helixi2504 – 2509Combined sources6
Turni2519 – 2521Combined sources3
Helixi2524 – 2528Combined sources5
Helixi2532 – 2547Combined sources16
Beta strandi2549 – 2551Combined sources3
Beta strandi2555 – 2559Combined sources5
Beta strandi2563 – 2565Combined sources3
Turni2568 – 2571Combined sources4
Beta strandi2578 – 2581Combined sources4
Helixi2584 – 2606Combined sources23
Helixi2607 – 2609Combined sources3
Helixi2611 – 2613Combined sources3
Helixi2616 – 2629Combined sources14
Beta strandi2630 – 2638Combined sources9
Helixi2643 – 2646Combined sources4
Helixi2649 – 2659Combined sources11
Helixi2666 – 2678Combined sources13
Turni2679 – 2681Combined sources3
Beta strandi2683 – 2686Combined sources4
Beta strandi2688 – 2690Combined sources3
Beta strandi2692 – 2696Combined sources5
Beta strandi2701 – 2703Combined sources3
Helixi2706 – 2724Combined sources19
Beta strandi2728 – 2735Combined sources8
Beta strandi2738 – 2744Combined sources7
Helixi2748 – 2764Combined sources17
Beta strandi2769 – 2771Combined sources3
Beta strandi2776 – 2778Combined sources3
Helixi2779 – 2781Combined sources3
Beta strandi2787 – 2793Combined sources7
Beta strandi2795 – 2797Combined sources3
Beta strandi2799 – 2804Combined sources6
Helixi2808 – 2819Combined sources12
Helixi2826 – 2833Combined sources8
Turni2834 – 2836Combined sources3
Helixi2838 – 2842Combined sources5
Helixi2844 – 2854Combined sources11
Beta strandi2858 – 2860Combined sources3
Beta strandi2862 – 2866Combined sources5
Beta strandi2869 – 2873Combined sources5
Helixi2875 – 2877Combined sources3
Helixi2878 – 2886Combined sources9
Helixi2888 – 2891Combined sources4
Helixi2898 – 2911Combined sources14
Helixi2916 – 2933Combined sources18
Helixi2935 – 2944Combined sources10
Helixi2946 – 2948Combined sources3
Beta strandi2949 – 2951Combined sources3
Helixi2959 – 2962Combined sources4
Turni2967 – 2970Combined sources4
Beta strandi2976 – 2978Combined sources3
Beta strandi2980 – 2982Combined sources3

3D structure databases

ProteinModelPortaliP26663
SMRiP26663
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26663

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini903 – 1026Peptidase C18PROSITE-ProRule annotationAdd BLAST124
Domaini1027 – 1208Peptidase S29PROSITE-ProRule annotationAdd BLAST182
Domaini1217 – 1369Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST153
Domaini2633 – 2751RdRp 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
Regioni148 – 236Interaction with FKBP8Add BLAST89
Regioni150 – 159Mitochondrial targeting signalBy similarity10
Regioni164 – 167Important for lipid droplets localizationBy similarity4
Regioni265 – 296Fusion peptideSequence analysisAdd BLAST32
Regioni385 – 411HVR1Add BLAST27
Regioni475 – 481HVR27
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
Regioni2200 – 2250Basal phosphorylationBy similarityAdd BLAST51
Regioni2210 – 2275PKR-bindingSequence analysisAdd BLAST66
Regioni2210 – 2249ISDRAdd BLAST40
Regioni2249 – 2306NS4B-bindingSequence analysisAdd BLAST58
Regioni2351 – 2419Basal phosphorylationBy similarityAdd BLAST69
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 biasi2282 – 2327Pro-richAdd BLAST46
Compositional biasi2995 – 2998Poly-Leu4

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 contains a variable region called interferon sensitivity determining region (ISDR) and seems to be intrinsically disordered and interacts with NS5B and host PKR (By similarity). The C-terminus of NS5A contains a variable region called variable region 3 (V3). ISDR and V3 may be involved in sensitivity and/or resistance to IFN-alpha therapy.By similarity
The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases.
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.

Sequence similaritiesi

Belongs to the hepacivirus polyprotein family.Curated

Keywords - Domaini

SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG09000032

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
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

Sequencei

Sequence statusi: Complete.

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

P26663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRAPR 
        60         70         80         90        100
KTSERSQPRG RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP 
       110        120        130        140        150
RGSRPSWGPT DPRRRSRNLG KVIDTLTCGF ADLMGYIPLV GAPLGGAARA 
       160        170        180        190        200
LAHGVRVLED GVNYATGNLP GCSFSIFLLA LLSCLTTPAS AYEVHNVSGI 
       210        220        230        240        250
YHVTNDCSNA SIVYEAADLI MHTPGCVPCV REGNSSRCWV ALTPTLAARN 
       260        270        280        290        300
VTIPTTTIRR HVDLLVGAAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHVT 
       310        320        330        340        350
LQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG 
       360        370        380        390        400
AHWGVLAGLA YYSMAGNWAK VLIVMLLFAG VDGDTHVTGG AQAKTTNRLV 
       410        420        430        440        450
SMFASGPSQK IQLINTNGSW HINRTALNCN DSLQTGFLAA LFYTHSFNSS 
       460        470        480        490        500
GCPERMAQCR TIDKFDQGWG PITYAESSRS DQRPYCWHYP PPQCTIVPAS 
       510        520        530        540        550
EVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN NTRPPQGNWF 
       560        570        580        590        600
GCTWMNSTGF TKTCGGPPCN IGGVGNNTLT CPTDCFRKHP EATYTKCGSG 
       610        620        630        640        650
PWLTPRCMVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL NAACNWTRGE 
       660        670        680        690        700
RCDLEDRDRP ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ 
       710        720        730        740        750
YLYGIGSAVV SFAIKWEYVL LLFLLLADAR VCACLWMMLL IAQAEAALEN 
       760        770        780        790        800
LVVLNSASVA GAHGILSFLV FFCAAWYIKG RLVPGATYAL YGVWPLLLLL 
       810        820        830        840        850
LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA RLIWWLQYFT 
       860        870        880        890        900
TRAEADLHVW IPPLNARGGR DAIILLMCAV HPELIFDITK LLIAILGPLM 
       910        920        930        940        950
VLQAGITRVP YFVRAQGLIH ACMLVRKVAG GHYVQMAFMK LGALTGTYIY 
       960        970        980        990       1000
NHLTPLRDWP RAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL 
      1010       1020       1030       1040       1050
PVSARRGKEI LLGPADSLEG RGLRLLAPIT AYSQQTRGLL GCIITSLTGR 
      1060       1070       1080       1090       1100
DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT VYHGAGSKTL AAPKGPITQM 
      1110       1120       1130       1140       1150
YTNVDQDLVG WPKPPGARSL TPCTCGSSDL YLVTRHADVI PVRRRGDSRG 
      1160       1170       1180       1190       1200
SLLSPRPVSY LKGSSGGPLL CPFGHAVGIF RAAVCTRGVA KAVDFVPVES 
      1210       1220       1230       1240       1250
METTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK 
      1260       1270       1280       1290       1300
VLVLNPSVAA TLGFGAYMSK AHGIDPNIRT GVRTITTGAP VTYSTYGKFL 
      1310       1320       1330       1340       1350
ADGGCSGGAY DIIICDECHS TDSTTILGIG TVLDQAETAG ARLVVLATAT 
      1360       1370       1380       1390       1400
PPGSVTVPHP NIEEVALSNT GEIPFYGKAI PIEAIRGGRH LIFCHSKKKC 
      1410       1420       1430       1440       1450
DELAAKLSGL GINAVAYYRG LDVSVIPTIG DVVVVATDAL MTGYTGDFDS 
      1460       1470       1480       1490       1500
VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR 
      1510       1520       1530       1540       1550
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV 
      1560       1570       1580       1590       1600
CQDHLEFWES VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP 
      1610       1620       1630       1640       1650
PPSWDQMWKC LIRLKPTLHG PTPLLYRLGA VQNEVTLTHP ITKYIMACMS 
      1660       1670       1680       1690       1700
ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV VIVGRIILSG RPAIVPDREL 
      1710       1720       1730       1740       1750
LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT KQAEAAAPVV 
      1760       1770       1780       1790       1800
ESKWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP 
      1810       1820       1830       1840       1850
LTTQSTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD 
      1860       1870       1880       1890       1900
ILAGYGAGVA GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA 
      1910       1920       1930       1940       1950
ILRRHVGPGE GAVQWMNRLI AFASRGNHVS PTHYVPESDA AARVTQILSS 
      1960       1970       1980       1990       2000
LTITQLLKRL HQWINEDCST PCSGSWLRDV WDWICTVLTD FKTWLQSKLL 
      2010       2020       2030       2040       2050
PQLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK NGSMRIVGPK 
      2060       2070       2080       2090       2100
TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH 
      2110       2120       2130       2140       2150
YVTGMTTDNV KCPCQVPAPE FFSEVDGVRL HRYAPACRPL LREEVTFQVG 
      2160       2170       2180       2190       2200
LNQYLVGSQL PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS 
      2210       2220       2230       2240       2250
SSASQLSAPS LKATCTTHHV SPDADLIEAN LLWRQEMGGN ITRVESENKV 
      2260       2270       2280       2290       2300
VVLDSFDPLR AEEDEREVSV PAEILRKSKK FPAAMPIWAR PDYNPPLLES 
      2310       2320       2330       2340       2350
WKDPDYVPPV VHGCPLPPIK APPIPPPRRK RTVVLTESSV SSALAELATK 
      2360       2370       2380       2390       2400
TFGSSESSAV DSGTATALPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL 
      2410       2420       2430       2440       2450
SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL 
      2460       2470       2480       2490       2500
RHHNMVYATT SRSAGLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK 
      2510       2520       2530       2540       2550
LLSVEEACKL TPPHSAKSKF GYGAKDVRNL SSKAVNHIHS VWKDLLEDTV 
      2560       2570       2580       2590       2600
TPIDTTIMAK NEVFCVQPEK GGRKPARLIV FPDLGVRVCE KMALYDVVST 
      2610       2620       2630       2640       2650
LPQVVMGSSY GFQYSPGQRV EFLVNTWKSK KNPMGFSYDT RCFDSTVTEN 
      2660       2670       2680       2690       2700
DIRVEESIYQ CCDLAPEARQ AIKSLTERLY IGGPLTNSKG QNCGYRRCRA 
      2710       2720       2730       2740       2750
SGVLTTSCGN TLTCYLKASA ACRAAKLQDC TMLVNGDDLV VICESAGTQE 
      2760       2770       2780       2790       2800
DAASLRVFTE AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV 
      2810       2820       2830       2840       2850
YYLTRDPTTP LARAAWETAR HTPVNSWLGN IIMYAPTLWA RMILMTHFFS 
      2860       2870       2880       2890       2900
ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ IIERLHGLSA FSLHSYSPGE 
      2910       2920       2930       2940       2950
INRVASCLRK LGVPPLRVWR HRARSVRARL LSQGGRAATC GKYLFNWAVK 
      2960       2970       2980       2990       3000
TKLKLTPIPA ASRLDLSGWF VAGYSGGDIY HSLSRARPRW FMLCLLLLSV 
      3010
GVGIYLLPNR
Length:3,010
Mass (Da):327,194
Last modified:January 23, 2007 - v3
Checksum:iF8422D5ECCFDFD9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58335 Genomic RNA Translation: AAA72945.1
PIRiA38465 GNWVTC

Similar proteinsi

Entry informationi

Entry nameiPOLG_HCVBK
AccessioniPrimary (citable) accession number: P26663
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 202 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, Direct protein sequencing

Documents

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

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