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Literature summary for 3.1.4.41 extracted from

  • van den Berg, C.W.; Goncalves-de-Andrade, R.M.; Okamoto, C.K.; Tambourgi, D.V.
    C5a receptor is cleaved by metalloproteases induced by sphingomyelinase D from Loxosceles spider venom (2012), Immunobiology, 217, 935-941.
    View publication on PubMed
Search for more literature for 3.1.4.41

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Loxosceles sp.
-
-

Organism

Organism UniProt Comment Textmining
Loxosceles sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Loxosceles sp.
-

Synonyms

Synonyms Comment Organism
SMaseD
-
 Loxosceles sp.
sphingomyelinase D
-
 Loxosceles sp.

General Information

General Information Comment Organism
physiological function the endogenous metalloprotease of the adamalysin (ADAM) family is activated by the sphingomyelinase D in the venom, the metalloprotease induces the activation of cleavage of pro-inflammatory agent C5a at two sites, resulting in the release of the extracellular N-terminus. That way the spider venom reduces expression and function of the C5a receptor, a component of the complement system, overview Loxosceles sp.