Literature summary for 3.4.21.46 extracted from

Takahashi, M.; Ishida, Y.; Iwaki, D.; Kanno, K.; Suzuki, T.; Endo, Y.; Homma, Y.; Fujita, T.
Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D (2010), J. Exp. Med., 207, 29-37.

Search for more literature for 3.4.21.46

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	complement factor D is a zymgen with the activation peptide QPRGR at its N-terminus. Mannose-binding lectin-associated serine protease-1 and -3 (Masp 1/3) deficient mice fail convert pro-complement factor D in its active form. Mannose-binding lectin-associated serine protease-1 converts pro-complement factor D in vitro indicating that mannose-binding lectin-associated serine protease-1 (MASP-1) is an essential protease for activating complement factor D	Mus musculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
blood	-	Mus musculus	-

Synonyms

Synonyms	Comment	Organism
factor D	-	Mus musculus

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Release 2023.1 (January 2023)