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)
|
Abstract |
Prophenoloxidase activation cleavage site is cut by the PPAE enzyme which is also inhibited by some serpins. Activation leads to melanisation of invasive organisms. |
3 GO-Terms:
12 Instances for CLV_MEL_PAP_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
(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