| Accession: | |
|---|---|
| Functional site class: |   Melanisation activation site  | 
    
| Functional site description: | Prophenoloxidase activation cleavage site is cut by the PPAE enzyme which is also inhibited by some serpins. Activation leads to melanisation of invasive organisms.  | 
    
| ELM Description: |   Prophenoloxidase-activation proteinase is Anthropoda specific proprotein convertase. It activates the melanisation process, which is  a common response to parasite entry in invertebrate animals. Similar to several other proprotein convertases it cleaves polypeptide at carboxy-site of arginine. Note that this cleavage usually occurs at unstructured N-terminal end of target proteins.  | 
    
| Pattern: | [ILV]..R[VF][GS]. | 
| Pattern Probability: | 0.0001054 | 
| Present in taxon: | Arthropoda | 
| Interaction Domain: | 
		 
		    
		    
		    
			Trypsin (PF00089)
		    Trypsin
		    
		    (Stochiometry: 1 : 1) 
		     
		    
		 
   
        
 | 
 Prophenoloxidase activation cleavage site is cut by the PPAE enzyme which is also inhibited by some serpins. Activation leads to melanisation of invasive organisms.   | 
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
    
        Please cite: 
            ELM-the Eukaryotic Linear Motif resource-2024 update.
        
    (PMID:37962385)
    
    
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
