Structural polyprotein Recombinant Protein | C recombinant protein

Recombinant Rubella virus Structural polyprotein

Cat. Num. AAA1085337

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Structural polyprotein; Recombinant Rubella virus Structural polyprotein; C recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 583-1063aa; Partial (Spike glycoprotein E1 Chain)
• Sequence: EEAFTYLCTAPGCATQTPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR

• Species: Rubella virus (strain M33) (RUBV)
• Preparation and Storage: Store at -20 degree C. For extended storage, store at -20 or -80 degree C.

NCBI and Uniprot Product Information

• NCBI GI #: 108935935
• UniProt Accession #: P08563; P21480; Q86373; Q86374; Q86375
• Molecular Weight: 114,736 Da
• NCBI Official Full Name: Structural polyprotein
• UniProt Protein Name: Structural polyprotein
• Protein Family: Structural polyprotein
• UniProt Gene Name: C
• UniProt Synonym Gene Names: C
• UniProt Entry Name: POLS_RUBVM

Uniprot Description

Function: Capsid protein interacts with genomic RNA and assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion, but this interaction seems not to be important for its biological function. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. Ref.14 Ref.15E2 envelope glycoprotein is responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. Ref.14 Ref.15E1 envelope glycoprotein is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion

By similarity. E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function. Ref.14 Ref.15

Subunit structure: Capsid protein homooligomerizes. Forms dimer shortly after synthesis, this dimer become disulfide-linked in the virion. Interacts with human C1QBP. E1 and E2 envelope glycoproteins heterodimerize. Ref.11

Subcellular location: Capsid protein: Virion. Host cytoplasm. Host mitochondrion. Note: The capsid protein is concentrated around Golgi region. Ref.5 Ref.6 Ref.8E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. Ref.5 Ref.6 Ref.8E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note: E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. Ref.5 Ref.6 Ref.8

Domain: The signal peptide at the C-terminus remains bound to the mature capsid protein. It may have a role as an anchor peptide, localizing the capsid assembly at the Golgi complex, where budding occurs.

Post-translational modification: Specific enzymatic cleavages in vivo yield mature proteins. An internal signal peptide at the capsid C-terminus directs E2-E1 sequences of the polyprotein precursor to the endoplasmic reticulum. Signal peptidase cleaves the precursor between Capsid and E2, releasing the capsid in the cytoplasm and the E2 N-terminus in ER. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism.Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity. Dephosphorylated by human PP1A

By similarity. Ref.17

Miscellaneous: Structural polyprotein is translated from a subgenomic RNA synthesized during togaviruses replication.

Sequence caution: The sequence CAA28880.1 differs from that shown. Reason: Frameshift at several positions.