P27958 (POLG_HCVH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	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 Short name=p23 EC=3.4.22.- 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
Organism	Hepatitis C virus genotype 1a (isolate H) (HCV) [Reference proteome]
Taxonomic identifier	11108 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Hepacivirus › Hepatitis C virus › Hepatitis C virus genotype 1 › Hepatitis C virus subtype 1a
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	3011 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.31 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. Ref.31 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. Ref.31 Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation By similarity. Ref.31 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. Ref.31 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. Ref.31 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. Ref.31 NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication. Ref.31
Catalytic activity	Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). NTP + H2O = NDP + phosphate. ATP + H2O = ADP + phosphate.
Cofactor	Binds 1 zinc ion per NS3 protease domain By similarity. Binds 1 zinc ion per NS5A N-terminal domain By similarity.
Enzyme regulation	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. Ref.38
Subunit structure	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. Ref.8 Ref.10 Ref.20 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.34 Ref.36 Ref.38 Ref.40
Subcellular location	Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Host mitochondrion membrane; Single-pass type I membrane protein By similarity. Host lipid droplet By similarity. Note: The C-terminal transmembrane domain of core protein p21 contains an ER signal leading the nascent polyprotein to the ER membrane. Only a minor proportion of core protein is present in the nucleus and an unknown proportion is secreted. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 Core protein p19: Virion By similarity. Host cytoplasm By similarity. Host nucleus By similarity. Secreted By similarity Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39. Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein Potential. 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. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein Potential. 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. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39. Host cell membrane. Note: The C-terminus of p7 membrane domain acts as a signal sequence. After cleavage by host signal peptidase, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. Only a fraction localizes to the plasma membrane. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Note: NS3 is associated to the ER membrane through its binding to NS4A. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Note: Host membrane insertion occurs after processing by the NS3 protease. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39. Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. Host cytoplasm › host perinuclear region. Host mitochondrion. Note: Host membrane insertion occurs after processing by the NS3 protease. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39 RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Note: Host membrane insertion occurs after processing by the NS3 protease. Ref.6 Ref.8 Ref.9 Ref.14 Ref.21 Ref.35 Ref.39
Domain	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. Ref.1 Ref.9 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. Ref.1 Ref.9 The SH3-binding domain of NS5A is involved in the interaction with human Bin1, GRB2 and Src-family kinases By similarity. Ref.1 Ref.9 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. Ref.1 Ref.9
Post-translational modification	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. Ref.5 Ref.26 Ref.28 Envelope E1 and E2 glycoproteins are highly N-glycosylated. Core protein is phosphorylated by host PKC and PKA By similarity. Ref.7 Ref.38 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. Ref.7 Ref.38 The N-terminus of a fraction of NS4B molecules seems to be relocated post-translationally from the cytoplasm to the ER lumen, with a 5th transmembrane segment. The C-terminus of NS2 may be lumenal with a fourth transmembrane segment By similarity. Core protein is ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation By similarity. NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions. Ref.30
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.
Sequence similarities	Belongs to the hepacivirus polyprotein family. Contains 1 helicase ATP-binding domain. Contains 1 peptidase C18 domain. Contains 1 peptidase S29 domain. Contains 1 RdRp catalytic domain.
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.

Ontologies

Keywords
Biological process	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 IFN-mediated response initiation by virus Inhibition of host MAVS by virus Inhibition of host STAT1 by virus Inhibition of host TRAFs by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Interferon antiviral system evasion Ion transport Modulation of host cell cycle by virus Transcription Transcription regulation Transport Viral RNA replication Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host cell membrane Host cytoplasm Host endoplasmic reticulum Host lipid droplet Host membrane Host mitochondrion Host nucleus Membrane Secreted Viral envelope protein Virion
Coding sequence diversity	Ribosomal frameshifting
Disease	Oncogene
Domain	SH3-binding Transmembrane Transmembrane helix
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Viral nucleoprotein Zinc
Molecular function	Capsid protein Helicase Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Ribonucleoprotein Serine protease Thiol protease Transferase Viral ion channel
PTM	Acetylation Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW modulation by virus of host G1/S transition checkpoint Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host MAVS activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host STAT1 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host TRAF activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transformation of host cell by virus Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell lipid particle Inferred from electronic annotation. Source: UniProtKB-SubCell host cell mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell host cell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type exopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C1QBP	Q07021	4	EBI-6377335,EBI-347528	From a different organism.
FYN	P06241	4	EBI-706378,EBI-515315	From a different organism.
GRB2	P62993	3	EBI-706378,EBI-401755	From a different organism.
HCK	P08631	5	EBI-706378,EBI-346340	From a different organism.
Lck	P06240	3	EBI-706378,EBI-1401	From a different organism.
LYN	P07948	5	EBI-706378,EBI-79452	From a different organism.
TBK1	Q9UHD2	4	EBI-3649474,EBI-356402	From a different organism.

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

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)

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.

Note: Produced by conventional translation.

Isoform F protein (identifier: P0C045-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 191

190

Core protein p21 Potential

PRO_0000037566

Chain

2 – 177

176

Core protein p19 By similarity

PRO_0000037567

Propeptide

178 – 191

14

ER anchor for the core protein, removed in mature form by host signal peptidase By similarity

PRO_0000037568

Chain

192 – 383

192

Envelope glycoprotein E1 Potential

PRO_0000037569

Chain

384 – 746

363

Envelope glycoprotein E2 Potential

PRO_0000037570

Chain

747 – 809

63

p7

PRO_0000037571

Chain

810 – 1026

217

Protease NS2-3 Potential

PRO_0000037572

Chain

1027 – 1657

631

Serine protease NS3 Potential

PRO_0000037573

Chain

1658 – 1711

54

Non-structural protein 4A Potential

PRO_0000037574

Chain

1712 – 1972

261

Non-structural protein 4B Potential

PRO_0000037575

Chain

1973 – 2420

448

Non-structural protein 5A Potential

PRO_0000037576

Chain

2421 – 3011

591

RNA-directed RNA polymerase Potential

PRO_0000037577

Regions

Topological domain

2 – 168

167

Cytoplasmic Potential

Transmembrane

169 – 189

21

Helical; Potential

Topological domain

190 – 358

169

Lumenal Potential

Transmembrane

359 – 379

21

Helical; Potential

Topological domain

380 – 725

346

Lumenal Potential

Transmembrane

726 – 746

21

Helical; Potential

Topological domain

747 – 757

11

Lumenal Potential

Transmembrane

758 – 778

21

Helical; Potential

Topological domain

779 – 782

4

Cytoplasmic Potential

Transmembrane

783 – 803

21

Helical; Potential

Topological domain

804 – 813

10

Lumenal Potential

Transmembrane

814 – 834

21

Helical; Potential

Topological domain

835 – 881

47

Cytoplasmic Potential

Transmembrane

882 – 902

21

Helical; Potential

Topological domain

903 – 928

26

Lumenal Potential

Transmembrane

929 – 949

21

Helical; Potential

Topological domain

950 – 1657

708

Cytoplasmic Potential

Transmembrane

1658 – 1678

21

Helical; Potential

Topological domain

1679 – 1805

127

Cytoplasmic Potential

Transmembrane

1806 – 1826

21

Helical; Potential

Topological domain

1827 – 1828

2

Lumenal Potential

Transmembrane

1829 – 1849

21

Helical; Potential

Topological domain

1850

1

Cytoplasmic Potential

Transmembrane

1851 – 1871

21

Helical; Potential

Topological domain

1872 – 1881

10

Lumenal Potential

Transmembrane

1882 – 1902

21

Helical; Potential

Topological domain

1903 – 1972

70

Cytoplasmic Potential

Intramembrane

1973 – 2002

30

By similarity

Topological domain

2003 – 2990

988

Cytoplasmic Potential

Transmembrane

2991 – 3011

21

Helical; By similarity

Domain

1217 – 1369

153

Helicase ATP-binding

Domain

2634 – 2752

119

RdRp catalytic

Nucleotide binding

1230 – 1237

8

ATP Potential

Region

2 – 59

58

Interaction with DDX3X By similarity

Region

2 – 23

22

Interaction with STAT1 By similarity

Region

122 – 173

52

Interaction with APOA2 By similarity

Region

150 – 159

10

Mitochondrial targeting signal By similarity

Region

164 – 167

4

Important for lipid droplets localization By similarity

Region

265 – 296

32

Fusion peptide Potential

Region

385 – 411

27

HVR1 By similarity

Region

475 – 481

7

HVR2 By similarity

Region

482 – 494

13

CD81-binding 1 Potential

Region

522 – 553

32

CD81-binding 2 Potential

Region

660 – 671

12

PKR/eIF2-alpha phosphorylation homology domain (PePHD)

Region

1679 – 1690

12

NS3-binding (by NS4A) Potential

Region

2120 – 2332

213

Transcriptional activation Potential

Region

2120 – 2208

89

FKBP8-binding Potential

Region

2200 – 2250

51

Basal phosphorylation By similarity

Region

2210 – 2275

66

PKR-binding Potential

Region

2249 – 2306

58

NS4B-binding Potential

Region

2351 – 2420

70

Basal phosphorylation By similarity

Region

2354 – 2377

24

V3

Motif

5 – 13

9

Nuclear localization signal Potential

Motif

38 – 43

6

Nuclear localization signal Potential

Motif

58 – 64

7

Nuclear localization signal Potential

Motif

66 – 71

6

Nuclear localization signal Potential

Motif

1316 – 1319

4

DECH box

Motif

2322 – 2325

4

SH3-binding Potential

Motif

2327 – 2335

9

Nuclear localization signal Potential

Compositional bias

796 – 803

8

Poly-Leu

Compositional bias

1432 – 1435

4

Poly-Val

Compositional bias

2286 – 2327

42

Pro-rich

Compositional bias

2996 – 2999

4

Poly-Leu

Sites

Active site

952

1

For protease NS2-3 activity; shared with dimeric partner

Active site

972

1

For protease NS2-3 activity; shared with dimeric partner

Active site

993

1

For protease NS2-3 activity; shared with dimeric partner

Active site

1083

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1107

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1165

1

Charge relay system; for serine protease NS3 activity

Metal binding

1123

1

Zinc

Metal binding

1125

1

Zinc

Metal binding

1171

1

Zinc

Metal binding

1175

1

Zinc

Metal binding

2011

1

Zinc By similarity

Metal binding

2029

1

Zinc By similarity

Metal binding

2031

1

Zinc By similarity

Metal binding

2052

1

Zinc By similarity

Site

177 – 178

2

Cleavage; by host signal peptidase By similarity

Site

191 – 192

2

Cleavage; by host signal peptidase Potential

Site

383 – 384

2

Cleavage; by host signal peptidase Potential

Site

746 – 747

2

Cleavage; by host signal peptidase

Site

809 – 810

2

Cleavage; by host signal peptidase

Site

1026 – 1027

2

Cleavage; by protease NS2-3 Potential

Site

1657 – 1658

2

Cleavage; by serine protease NS3 Potential

Site

1711 – 1712

2

Cleavage; by serine protease NS3 Potential

Site

1972 – 1973

2

Cleavage; by serine protease NS3 Potential

Site

2420 – 2421

2

Cleavage; by serine protease NS3 Potential

Amino acid modifications

Modified residue

2

1

N-acetylserine; by host By similarity

Modified residue

53

1

Phosphoserine; by host By similarity

Modified residue

99

1

Phosphoserine; by host By similarity

Modified residue

116

1

Phosphoserine; by host PKA By similarity

Modified residue

2194

1

Phosphoserine; by host; in p56 By similarity

Modified residue

2197

1

Phosphoserine; by host; in p58 By similarity

Modified residue

2201

1

Phosphoserine; by host; in p58 By similarity

Modified residue

2204

1

Phosphoserine; by host; in p58 By similarity

Modified residue

2321

1

Phosphoserine; by host Ref.7

Lipidation

1968

1

S-palmitoyl cysteine; by host Ref.30

Lipidation

1972

1

S-palmitoyl cysteine; by host; partial Ref.30

Glycosylation

196

1

N-linked (GlcNAc...); by host Potential

Glycosylation

209

1

N-linked (GlcNAc...); by host Potential

Glycosylation

234

1

N-linked (GlcNAc...); by host Potential

Glycosylation

305

1

N-linked (GlcNAc...); by host Potential

Glycosylation

417

1

N-linked (GlcNAc...); by host Potential

Glycosylation

423

1

N-linked (GlcNAc...); by host Potential

Glycosylation

430

1

N-linked (GlcNAc...); by host Potential

Glycosylation

448

1

N-linked (GlcNAc...); by host Potential

Glycosylation

476

1

N-linked (GlcNAc...); by host Potential

Glycosylation

532

1

N-linked (GlcNAc...); by host Potential

Glycosylation

540

1

N-linked (GlcNAc...); by host Potential

Glycosylation

556

1

N-linked (GlcNAc...); by host Potential

Glycosylation

576

1

N-linked (GlcNAc...); by host Potential

Glycosylation

623

1

N-linked (GlcNAc...); by host Potential

Glycosylation

645

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

2114 ↔ 2162

By similarity

Natural variations

Natural variant

212

1

V → I in strain: Isolate H77.

Natural variant

297

1

H → R in strain: Isolate H77.

Natural variant

303

1

D → S in strain: Isolate H77.

Natural variant

321

1

N → D in strain: Isolate H77.

Natural variant

360

1

K → A in strain: Isolate H77.

Natural variant

391

1

N → S in strain: Isolate H77.

Natural variant

394

1

R → H in strain: Isolate H77.

Natural variant

431

1

E → D in strain: Isolate H77.

Natural variant

434

1

N → T in strain: Isolate H77.

Natural variant

444

1

Q → R in strain: Isolate H77.

Natural variant

457

1

A → T in strain: Isolate H77.

Natural variant

564 – 566

3

CGA → RGV in strain: Isolate H77.

Natural variant

589

1

Y → H in strain: Isolate H77.

Natural variant

602

1

R → W in strain: Isolate H77.

Natural variant

650

1

E → G in strain: Isolate H77.

Natural variant

773

1

C → R in strain: Isolate H77.

Natural variant

787

1

V → A in strain: Isolate H77.

Natural variant

790

1

L → F in strain: Isolate H77.

Natural variant

877

1

T → M in strain: Isolate H77.

Natural variant

883

1

A → T in strain: Isolate H77.

Natural variant

948

1

C → Y in strain: Isolate H77.

Natural variant

954

1

A → T in strain: Isolate H77.

Natural variant

1026

1

L → Q in strain: Isolate H77.

Natural variant

1033

1

A → T in strain: Isolate H77.

Natural variant

1049

1

G → S in strain: Isolate H77.

Natural variant

1100

1

T → M in strain: Isolate H77.

Natural variant

1121

1

T → A in strain: Isolate H77.

Natural variant

1173

1

T → A in strain: Isolate H77.

Natural variant

1202

1

E → G in strain: Isolate H77.

Natural variant

1214

1

S → P in strain: Isolate H77.

Natural variant

1247

1

K → Q in strain: Isolate H77.

Natural variant

1303

1

A → G in strain: Isolate H77.

Natural variant

1327

1

S → L in strain: Isolate H77.

Natural variant

1556

1

G → E in strain: Isolate H77.

Natural variant

1608

1

R → W in strain: Isolate H77.

Natural variant

1742

1

H → Q in strain: Isolate H77.

Natural variant

1839 – 1840

2

LD → IG in strain: Isolate H77.

Natural variant

1893

1

A → V in strain: Isolate H77.

Natural variant

1898 – 1900

3

FAS → CAA in strain: Isolate H77.

Natural variant

1905

1

R → H in strain: Isolate H77.

Natural variant

1940

1

A → V in strain: Isolate H77.

Natural variant

2043

1

T → A in strain: Isolate H77.

Natural variant

2053

1

K → R in strain: Isolate H77.

Natural variant

2061

1

F → L in strain: Isolate H77.

Natural variant

2102

1

V → I in strain: Isolate H77.

Natural variant

2185

1

A → E in strain: Isolate H77.

Natural variant

2283

1

P → R in strain: Isolate H77.

Natural variant

2296

1

L → P in strain: Isolate H77.

Natural variant

2341

1

P → S in strain: Isolate H77.

Natural variant

2355

1

S → P in strain: Isolate H77.

Natural variant

2400

1

L → F in strain: Isolate H77.

Natural variant

2425

1

S → T in strain: Isolate H77.

Natural variant

2469

1

K → Q in strain: Isolate H77.

Natural variant

2512

1

A → T in strain: Isolate H77.

Natural variant

2637

1

L → F in strain: Isolate H77.

Natural variant

2703

1

R → G in strain: Isolate H77.

Natural variant

2715

1

R → C in strain: Isolate H77.

Natural variant

2755

1

S → N in strain: Isolate H77.

Natural variant

2925

1

W → R in strain: Isolate H77.

Natural variant

2933

1

A → S in strain: Isolate H77.

Natural variant

2937

1

K → R in strain: Isolate H77.

Natural variant

2960

1

T → A in strain: Isolate H77.

Experimental info

Mutagenesis

720

1

V → L: Increases processing between E2 and p7. Ref.28

Mutagenesis

779

1

K → I: Virus can no longer infect chimpanzee. Ref.19

Mutagenesis

781

1

R → S: Virus can no longer infect chimpanzee. Ref.19

Mutagenesis

952

1

H → A: Complete loss of NS2-NS3 cleavage. Ref.4 Ref.46

Mutagenesis

993

1

C → A: Complete loss of NS2-NS3 cleavage. Ref.4 Ref.46

Mutagenesis

1165

1

S → A: Complete loss of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B cleavages. Ref.4

Mutagenesis

1968

1

C → A: Strong decrease in NS4B palmitoylation. Ref.30

Mutagenesis

1972

1

C → A: Slight decrease in NS4B palmitoylation. Ref.30

Mutagenesis

2321

1

S → A: Loss of phosphorylation. Ref.7

Secondary structure

1

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3011

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Beta strand

16 – 18

3

Turn

19 – 23

5

Beta strand

30 – 35

6

Turn

36 – 38

3

Beta strand

39 – 41

3

Helix

911 – 923

13

Turn

924 – 927

4

Helix

931 – 944

14

Turn

951 – 953

3

Helix

956 – 958

3

Helix

964 – 967

4

Turn

971 – 974

4

Beta strand

975 – 977

3

Beta strand

982 – 984

3

Turn

988 – 990

3

Beta strand

1000 – 1008

9

Beta strand

1010 – 1013

4

Turn

1016 – 1018

3

Helix

1019 – 1021

3

Beta strand

1032 – 1035

4

Helix

1039 – 1048

10

Beta strand

1057 – 1063

7

Beta strand

1068 – 1074

7

Beta strand

1077 – 1081

5

Helix

1082 – 1085

4

Beta strand

1100 – 1103

4

Turn

1104 – 1107

4

Beta strand

1108 – 1112

5

Beta strand

1129 – 1133

5

Beta strand

1139 – 1146

8

Beta strand

1149 – 1157

9

Helix

1158 – 1161

4

Beta strand

1168 – 1170

3

Beta strand

1176 – 1197

22

Helix

1198 – 1204

7

Beta strand

1224 – 1226

3

Turn

1236 – 1238

3

Helix

1239 – 1246

8

Beta strand

1251 – 1256

6

Helix

1258 – 1271

14

Beta strand

1277 – 1280

4

Beta strand

1283 – 1285

3

Beta strand

1290 – 1295

6

Helix

1296 – 1301

6

Helix

1304 – 1307

4

Beta strand

1311 – 1316

6

Turn

1317 – 1319

3

Helix

1323 – 1335

13

Turn

1336 – 1340

5

Beta strand

1342 – 1347

6

Beta strand

1362 – 1366

5

Beta strand

1371 – 1375

5

Beta strand

1378 – 1380

3

Helix

1382 – 1385

4

Beta strand

1386 – 1393

8

Helix

1397 – 1409

13

Beta strand

1414 – 1417

4

Helix

1423 – 1425

3

Beta strand

1428 – 1436

9

Beta strand

1442 – 1444

3

Beta strand

1449 – 1453

5

Beta strand

1456 – 1463

8

Beta strand

1467 – 1469

3

Beta strand

1471 – 1478

8

Helix

1481 – 1488

8

Beta strand

1493 – 1495

3

Beta strand

1497 – 1502

6

Helix

1514 – 1527

14

Helix

1532 – 1544

13

Beta strand

1545 – 1548

4

Helix

1555 – 1564

10

Helix

1570 – 1578

9

Helix

1584 – 1597

14

Helix

1606 – 1611

6

Turn

1614 – 1618

5

Beta strand

1627 – 1629

3

Beta strand

1635 – 1637

3

Helix

1640 – 1652

13

Beta strand

1680 – 1687

8

Helix

1753 – 1777

25

Helix

1940 – 1964

25

Helix

1976 – 1999

24

Beta strand

2422 – 2426

5

Helix

2445 – 2450

6

Helix

2454 – 2456

3

Beta strand

2457 – 2459

3

Helix

2462 – 2464

3

Helix

2465 – 2472

8

Helix

2482 – 2495

14

Helix

2505 – 2510

6

Helix

2525 – 2529

5

Helix

2533 – 2548

16

Beta strand

2550 – 2552

3

Beta strand

2556 – 2560

5

Beta strand

2564 – 2566

3

Helix

2569 – 2571

3

Beta strand

2579 – 2582

4

Helix

2585 – 2607

23

Helix

2608 – 2610

3

Helix

2612 – 2614

3

Helix

2617 – 2629

13

Beta strand

2631 – 2639

9

Helix

2644 – 2647

4

Helix

2650 – 2660

11

Helix

2667 – 2679

13

Turn

2680 – 2682

3

Beta strand

2684 – 2687

4

Beta strand

2693 – 2697

5

Helix

2707 – 2726

20

Beta strand

2729 – 2736

8

Beta strand

2739 – 2745

7

Helix

2749 – 2765

17

Beta strand

2770 – 2772

3

Helix

2780 – 2782

3

Beta strand

2788 – 2794

7

Beta strand

2800 – 2806

7

Helix

2809 – 2820

12

Helix

2827 – 2835

9

Helix

2839 – 2843

5

Helix

2845 – 2855

11

Beta strand

2863 – 2867

5

Beta strand

2870 – 2874

5

Helix

2876 – 2878

3

Helix

2879 – 2887

9

Helix

2889 – 2892

4

Helix

2899 – 2912

14

Helix

2917 – 2934

18

Helix

2936 – 2945

10

Helix

2947 – 2949

3

Beta strand

2950 – 2952

3

Helix

2960 – 2964

5

Turn

2968 – 2971

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Genome polyprotein [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 772CBB29CCD94753	FASTA	3,011	327,146
	10 20 30 40 50 60 MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG 70 80 90 100 110 120 RRQPIPKARR PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG 130 140 150 160 170 180 KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA 190 200 210 220 230 240 LLSCLTVPAS AYQVRNSSGL YHVTNDCPNS SVVYEAADAI LHTPGCVPCV REGNASRCWV 250 260 270 280 290 300 AVTPTVATRD GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRHHWT 310 320 330 340 350 360 TQDCNCSIYP GHITGHRMAW NMMMNWSPTA ALVVAQLLRI PQAIMDMIAG AHWGVLAGIK 370 380 390 400 410 420 YFSMVGNWAK VLVVLLLFAG VDAETHVTGG NAGRTTAGLV GLLTPGAKQN IQLINTNGSW 430 440 450 460 470 480 HINSTALNCN ESLNTGWLAG LFYQHKFNSS GCPERLASCR RLTDFAQGWG PISYANGSGL 490 500 510 520 530 540 DERPYCWHYP PRPCGIVPAK SVCGPVYCFT PSPVVVGTTD RSGAPTYSWG ANDTDVFVLN 550 560 570 580 590 600 NTRPPLGNWF GCTWMNSTGF TKVCGAPPCV IGGVGNNTLL CPTDCFRKYP EATYSRCGSG 610 620 630 640 650 660 PRITPRCMVD YPYRLWHYPC TINYTIFKVR MYVGGVEHRL EAACNWTRGE RCDLEDRDRS 670 680 690 700 710 720 ELSPLLLSTT QWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGVGSSIA SWAIKWEYVV 730 740 750 760 770 780 LLFLLLADAR VCSCLWMMLL ISQAEAALEN LVILNAASLA GTHGLVSFLV FFCFAWYLKG 790 800 810 820 830 840 RWVPGAVYAL YGMWPLLLLL LALPQRAYAL DTEVAASCGG VVLVGLMALT LSPYYKRYIS 850 860 870 880 890 900 WCMWWLQYFL TRVEAQLHVW VPPLNVRGGR DAVILLTCVV HPALVFDITK LLLAIFGPLW 910 920 930 940 950 960 ILQASLLKVP YFVRVQGLLR ICALARKIAG GHYVQMAIIK LGALTGTCVY NHLAPLRDWA 970 980 990 1000 1010 1020 HNGLRDLAVA VEPVVFSRME TKLITWGADT AACGDIINGL PVSARRGQEI LLGPADGMVS 1030 1040 1050 1060 1070 1080 KGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ IVSTATQTFL ATCINGVCWT 1090 1100 1110 1120 1130 1140 VYHGAGTRTI ASPKGPVIQT YTNVDQDLVG WPAPQGSRSL TPCTCGSSDL YLVTRHADVI 1150 1160 1170 1180 1190 1200 PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPTGHAVGLF RAAVCTRGVA KAVDFIPVEN 1210 1220 1230 1240 1250 1260 LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAKGYK VLVLNPSVAA 1270 1280 1290 1300 1310 1320 TLGFGAYMSK AHGVDPNIRT GVRTITTGSP ITYSTYGKFL ADAGCSGGAY DIIICDECHS 1330 1340 1350 1360 1370 1380 TDATSISGIG TVLDQAETAG ARLVVLATAT PPGSVTVSHP NIEEVALSTT GEIPFYGKAI 1390 1400 1410 1420 1430 1440 PLEVIKGGRH LIFCHSKKKC DELAAKLVAL GINAVAYYRG LDVSVIPTSG DVVVVSTDAL 1450 1460 1470 1480 1490 1500 MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR 1510 1520 1530 1540 1550 1560 FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV CQDHLGFWEG 1570 1580 1590 1600 1610 1620 VFTGLTHIDA HFLSQTKQSG ENFPYLVAYQ ATVCARAQAP PPSWDQMRKC LIRLKPTLHG 1630 1640 1650 1660 1670 1680 PTPLLYRLGA VQNEVTLTHP ITKYIMTCMS ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV 1690 1700 1710 1720 1730 1740 VIVGRIVLSG KPAIIPDREV LYQEFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS 1750 1760 1770 1780 1790 1800 RHAEVITPAV QTNWQKLEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP 1810 1820 1830 1840 1850 1860 LTTGQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAALD SVGLGKVLVD ILAGYGAGVA 1870 1880 1890 1900 1910 1920 GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALAVGVVFAS ILRRRVGPGE GAVQWMNRLI 1930 1940 1950 1960 1970 1980 AFASRGNHVS PTHYVPESDA AARVTAILSS LTVTQLLRRL HQWISSECTT PCSGSWLRDI 1990 2000 2010 2020 2030 2040 WDWICEVLSD FKTWLKAKLM PQLPGIPFVS CQRGYRGVWR GDGIMHTRCH CGAEITGHVK 2050 2060 2070 2080 2090 2100 NGTMRIVGPR TCKNMWSGTF FINAYTTGPC TPLPAPNYKF ALWRVSAEEY VEIRRVGDFH 2110 2120 2130 2140 2150 2160 YVSGMTTDNL KCPCQIPSPE FFTELDGVRL HRFAPPCKPL LREEVSFRVG LHEYPVGSQL 2170 2180 2190 2200 2210 2220 PCEPEPDVAV LTSMLTDPSH ITAEAAGRRL ARGSPPSMAS SSASQLSAPS LKATCTANHD 2230 2240 2250 2260 2270 2280 SPDAELIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLV AEEDEREVSV PAEILRKSRR 2290 2300 2310 2320 2330 2340 FAPALPVWAR PDYNPLLVET WKKPDYEPPV VHGCPLPPPR SPPVPPPRKK RTVVLTESTL 2350 2360 2370 2380 2390 2400 PTALAELATK SFGSSSTSGI TGDNTTTSSE PAPSGCPPDS DVESYSSMPP LEGEPGDPDL 2410 2420 2430 2440 2450 2460 SDGSWSTVSS GADTEDVVCC SMSYSWTGAL VTPCAAEEQK LPINALSNSL LRHHNLVYST 2470 2480 2490 2500 2510 2520 TSRSACQRKK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA NLLSVEEACS LAPPHSAKSK 2530 2540 2550 2560 2570 2580 FGYGAKDVRC HARKAVAHIN SVWKDLLEDS VTPIDTTIMA KNEVFCVQPE KGGRKPARLI 2590 2600 2610 2620 2630 2640 VFPDLGVRVC EKMALYDVVS KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGLSYD 2650 2660 2670 2680 2690 2700 TRCFDSTVTE SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR 2710 2720 2730 2740 2750 2760 ASRVLTTSCG NTLTRYIKAR AACRAAGLQD CTMLVCGDDL VVICESAGVQ EDAASLRAFT 2770 2780 2790 2800 2810 2820 EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR VYYLTRDPTT PLARAAWETA 2830 2840 2850 2860 2870 2880 RHTPVNSWLG NIIMFAPTLW ARMILMTHFF SVLIARDQLE QALNCEIYGA CYSIEPLDLP 2890 2900 2910 2920 2930 2940 PIIQRLHGLS AFSLHSYSPG EINRVAACLR KLGVPPLRAW RHRAWSVRAR LLARGGKAAI 2950 2960 2970 2980 2990 3000 CGKYLFNWAV RTKLKLTPIT AAGRLDLSGW FTAGYSGGDI YHSVSHARPR WFWFCLLLLA 3010 AGVGIYLLPN R
	Isoform F protein (Frameshifted protein) [UniParc]. See P0C045.		–	–

References

[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]	"A second hepatitis C virus-encoded proteinase." Grakoui A., McCourt D.W., Wychowski C., Feinstone S.M., Rice C.M. Proc. Natl. Acad. Sci. U.S.A. 90:10583-10587(1993) [PubMed] [Europe PMC] [Abstract] 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]	"Structural biology of hepatitis C virus." Penin F., Dubuisson J., Rey F.A., Moradpour D., Pawlotsky J.-M. Hepatology 39:5-19(2004) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

euHCVdb

The European HCV database

Virus Pathogen Resource

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

GNWVCH. A36814.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1353-1507	[»]
1N1L	X-ray	2.60	A/B	1027-1206	[»]
1ONB	NMR	-	A	1353-1507	[»]
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	1027-1206	[»]
2A4R	X-ray	2.40	A/C	1027-1207	[»]
			B/D	1680-1696	[»]
2F9V	X-ray	2.60	A/C	1027-1207	[»]
			B/D	1680-1696	[»]
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	C/D	1678-1695	[»]
2OBO	X-ray	2.60	A/C	1022-1207	[»]
			B/D	1677-1695	[»]
2OBQ	X-ray	2.50	B/D	1678-1695	[»]
2OC0	X-ray	2.30	A/C	1022-1207	[»]
			B/D	1677-1695	[»]
2OC1	X-ray	2.70	A/C	1022-1207	[»]
			B/D	1677-1695	[»]
2OC7	X-ray	2.70	A/C	1022-1207	[»]
			B/D	1677-1695	[»]
2OC8	X-ray	2.66	A/C	1022-1207	[»]
			B/D	1677-1695	[»]
2OIN	X-ray	2.50	A/B	1027-1207	[»]
2P59	X-ray	2.90	A/B	1027-1207	[»]
			C/D	1678-1696	[»]
2XI2	X-ray	1.80	A/B/C	2421-2990	[»]
2XI3	X-ray	1.70	A/B	2421-2990	[»]

ProteinModelPortal

P27958.

SMR

P27958. Positions 2-45, 902-1026, 1029-1657, 1973-2003, 2008-2170, 2421-2982.

ModBase

Search...

Protein-protein interaction databases

IntAct

P27958. 43 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

euHCVdb

AF009606.
AF011751.
AF011752.
AF011753.
M67463.

Family and domain databases

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.
IPR024350. HCV_NS5a_C.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR013192. NS5A_1a.
IPR004109. Peptidase_S29.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

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.
[Graphical view]

ProDom

PD001388. HCV_env. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00487. DEXDc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. False negative.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27958.

Entry information

Entry name

POLG_HCVH

Accession

Primary (citable) accession number: P27958
Secondary accession number(s): O36579 , O36608, O36609, O36610

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program