Recombinant C4 Protease protein
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Recombinant C4 Protease protein is a Tobacco vein mottling virus Full Length protein, in the 2002 to 2236 aa range, expressed in Tobacco Vein Mottling Virus, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
Genome polyprotein
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
C4 Protease serves multiple roles in immune system processes. It participates as an important component of the complement system a critical part of innate immunity. It cleaves C4 into C4a and C4b during the activation of the complement pathway aiding in pathogen opsonization and cell lysis. The enzyme functions are essential for maintaining immune surveillance and modulating inflammation.
Pathways
This target plays important roles in the complement cascade and coagulation pathways. In the complement pathway C4 Protease activates components like C2 facilitating opsonization and membrane attack complex formation. Its activity also interlinks with proteins such as complement component C3 which further propagates the immune response cascade. By acting within these pathways C4 Protease helps balance immune defense and homeostasis.
Specifications
Form
Liquid
General info
Function
Helper component proteinase. Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.. Cytoplasmic inclusion protein. Has helicase activity. It may be involved in replication.. 6 kDa protein 1. Indispensable for virus replication (By similarity). Reduces the abundance of host transcripts related to jasmonic acid biosynthesis therefore altering the host defenses (By similarity). In order to increase its own stability, decreases host protein degradation pathways (By similarity).. 6 kDa protein 2. Indispensable for virus replication.. Viral genome-linked protein. Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity).. Nuclear inclusion protein A. Has RNA-binding and proteolytic activities (By similarity). Main protease that processes most of the polyprotein cleavages (PubMed : 20862670).. Nuclear inclusion protein B. An RNA-dependent RNA polymerase that plays an essential role in the virus replication.. Capsid protein. Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Sequence similarities
Belongs to the potyviridae genome polyprotein family.
Post-translational modifications
Viral genome-linked protein. VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase.. Genome polyprotein. Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Target data
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