4C0A92E7016BEFE40C235AA147B00EBF5B0CDD6E686742CEC7BDC858B18A987A2213FFE9C983F5B86BC1A5E94DD8EF29

Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion (By similarity).

Source:http://purl.uniprot.org/SHA-384/4C0A92E7016BEFE40C235AA147B00EBF5B0CDD6E686742CEC7BDC858B18A987A2213FFE9C983F5B86BC1A5E94DD8EF29

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rdf:type	uniprot:PTM_Annotation
rdfs:comment	Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion (By similarity).