Literature summary for 3.4.21.B7 extracted from

Degn, S.E.; Thiel, S.; Jensenius, J.C.
Recombinant expression of the autocatalytic complement protease MASP-1 is crucially dependent on co-expression with its inhibitor, C1 inhibitor (2013), Protein Expr. Purif., 88, 173-182.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and catalytically inactive mutant full-length recombinant human MASP-1 entirely in the zymogen form in Hep-G2 and Chang liver cells or HEK-293F cells. The active protease is produced through co-expression with the serine protease inhibitor C1 inhibitor avoiding the self-suppression of enzyme expression by its autocatalytic activity, the expressed protease is capable of binding MBL and autoactivating, and is catalytically active	Homo sapiens

Cloned (Comment)

Organism

expression of wild-type and catalytically inactive mutant full-length recombinant human MASP-1 entirely in the zymogen form in Hep-G2 and Chang liver cells or HEK-293F cells. The active protease is produced through co-expression with the serine protease inhibitor C1 inhibitor avoiding the self-suppression of enzyme expression by its autocatalytic activity, the expressed protease is capable of binding MBL and autoactivating, and is catalytically active

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
S646A	site-directed mutagenesis, the mutant remains as inactive zymogen	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
C1 inhibitor	C1INH, a serine protease inhibitor	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	required, enzyme-bound	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
proform mannan-binding lectin-associated serine protease 1 + H2O	Homo sapiens	autocatalytic cleavage, a complement substrate, activation	mature mannan-binding lectin-associated serine protease 1 + ?	-	?
proform mannan-binding lectin-associated serine protease 2 + H2O	Homo sapiens	a complement substrate, activation	mature mannan-binding lectin-associated serine protease 2 + ?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P48740	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	enzyme MASP-1 performs autoactivation through proteolytic cleavage of its zymogen. Natural MASP-1 is activated by cleavage in the activation peptide, generating an A-chain (CUB-EGF-CUB-CCPCCP) and a B-chain (the serine protease domain), which remain associated through a disulphide bridge. MASP-1 autodegradation occurs intracellularly, not inhibited by addition of inhibitors to the culture medium	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
proform mannan-binding lectin-associated serine protease 1 + H2O	autocatalytic cleavage, a complement substrate, activation	Homo sapiens	mature mannan-binding lectin-associated serine protease 1 + ?	-	?
proform mannan-binding lectin-associated serine protease 2 + H2O	a complement substrate, activation	Homo sapiens	mature mannan-binding lectin-associated serine protease 2 + ?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain, domain organization of MASP-1, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
MASP-1	-	Homo sapiens

Expression

Organism	Comment	Expression
Homo sapiens	the catalytic activity of MASP-1 suppresses its expression through rapid auto-activation and autodegradation intracellularly, not inhibited by addition of inhibitors to the culture medium	down

General Information

General Information	Comment	Organism
metabolism	MASP-1 is a protease of the lectin pathway of complement	Homo sapiens
additional information	the catalytic activity of MASP-1 suppresses its expression through intracellular rapid autoactivation and autodegradation	Homo sapiens