Genome polyprotein Recombinant Protein | NS1 recombinant protein
Recombinant Dengue virus type 2 Genome polyprotein
NCBI and Uniprot Product Information
Uniprot Description
Function: Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA
By similarity.prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated
By similarity.Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes
By similarity.Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome
By similarity.Non-structural protein 2A may be involved viral RNA replication and capsid assembly
Potential.Non-structural protein 2B is a required cofactor for the serine protease function of NS3
By similarity.Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction
By similarity.Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase
By similarity.Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter
By similarity.Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway
By similarity.RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway
By similarity.
Catalytic activity: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).NTP + H2O = NDP + phosphate.ATP + H2O = ADP + phosphate.S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.
Subunit structure: Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity. NS5 interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation
By similarity.
Subcellular location: Capsid protein C: Virion
Potential. Peptide pr: Secreted
By similarity. Small envelope protein M: Virion membrane; Multi-pass membrane protein
By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein
By similarity. Envelope protein E: Virion membrane; Multi-pass membrane protein
By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein
By similarity. Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side
By similarity. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein
Potential. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein
Potential. Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
By similarity. Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
By similarity. Note: Remains non-covalently associated to NS3 protease
By similarity.Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein
By similarity. Note: Located in RE-associated vesicles hosting the replication complex.Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein
By similarity. RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
By similarity. Host nucleus
By similarity. Note: Located in RE-associated vesicles hosting the replication complex.
Domain: Transmembrane domains of the small envelope protein M and envelope protein E contains an endoplasmic reticulum retention signals
By similarity.
Post-translational modification: Specific enzymatic cleavages in vivo yield mature proteins. The nascent protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site
By similarity.RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization
By similarity.Envelope protein E and non-structural protein 1 are N-glycosylated
By similarity.
Sequence similarities: In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.Contains 1 helicase ATP-binding domain.Contains 1 helicase C-terminal domain.Contains 1 mRNA cap 0-1 NS5-type MT domain.Contains 1 peptidase S7 domain.Contains 1 RdRp catalytic domain.
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Product Notes
The Genome polyprotein ns1 (Catalog #AAA1123419) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 2492-3391. The amino acid sequence is listed below: GTGNIGETLG EKWKSRLNAL GKSEFQIYKK SGIQEVDRTL AKEGIKRGET DHHAVSRGSA KLRWFVERNM VTPEGKVVDL GCGRGGWSYY CGGLKNVREV KGLTKGGPGH EEPIPMSTYG WNLVRLQSGV DVFFTPPEKC DTLLCDIGES SPNPTIEAGR TLRVLNLVEN WLNNNTQFCI KVLNPYMPSV IEKMETLQRK YGGALVRNPL SRNSTHEMYW VSNASGNIVS SVNMISRMLI NRFTMKHKKA TYETDVDLGS GTRNIGIESE IPNLDIIGKR IEKIKQEHET SWHYDQDHPY KTWAYHGSYE TKQTGSASSM VNGVVRLLTK PWDVVPMVTQ MAMTDTTPFG QQRVFKEKVD TRTQEPKEGT KKLMKITAEW LWKELGKKKT PRMCTREEFT RKVRSNAALG AIFTDENKWK SAREAVEDSR FWELVDRERN LHLEGKCETC VYNMMGKREK KLGEFGKAKG SRAIWYMWLG ARFLEFEALG FLNEDHWFSR GNSLSGVEGE GLHKLGYILR DVSKKEGGAM YADDTAGWDT RITLEDLKNE EMVTNHMEGE HKKLAEAIFK LTYQNKVVRV QRPTPRGTVM DIISRRDQRG SGQVGTYGLN TFTNMEAQLI RQMEGEGIFK SIQHLTVTEE IAVQNWLARV GRERLSRMAI SGDDCVVKPL DDRFASALTA LNDMGKVRKD IQQWEPSRGW NDWTQVPFCS HHFHELVMKD GRVLVVPCRN QDELIGRARI SQGAGWSLKE TACLGKSYAQ MWTLMYFHRR DLRLAANAIC SAVPSHWVPT SRTTWSIHAK HEWMTTEDML AVWNRVWIQE NPWMEDKTPV ESWEEVPYLG KREDQWCGSL IGLTSRATWA KNIQTAINQV RSLIGNEEYT DYMPSMKRFR REEEEAGVLW. It is sometimes possible for the material contained within the vial of "Genome polyprotein, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
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