3.4.21.45: complement factor I
This is an abbreviated version!
For detailed information about complement factor I, go to the full flat file.
Word Map on EC 3.4.21.45
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3.4.21.45
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hemolytic
-
convertase
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macular
-
properdin
-
uremic
-
cell-bound
-
c3d
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fluid-phase
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glomerulonephritis
-
complement-mediated
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opsonization
-
medicine
-
i-mediated
-
eculizumab
-
alpha\'-chain
-
c4-binding
-
c4bp
-
microangiopathic
-
opsonin
- 3.4.21.45
-
hemolytic
-
convertase
-
macular
- properdin
-
uremic
-
cell-bound
- c3d
-
fluid-phase
- glomerulonephritis
-
complement-mediated
-
opsonization
- medicine
-
i-mediated
- eculizumab
-
alpha\'-chain
-
c4-binding
- c4bp
-
microangiopathic
-
opsonin
Reaction
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage =
Synonyms
C3b inactivator, C3b/C4b inactivator, C3bINA, CFI, complement C3b inactivator, complement C3b/C4b inactivator, complement C4b inactivator, complement C4bi, complement compoment C3b inactivator, complement factor I, complement inhibitor factor I, complement regulator factor I, conglutinogen-activating factor C, factor I, factor I-like activity, fI, GcIf-1, GcIf-2, GcIf-3, GcIf-4, IF, plasma protease factor I, serine protease Factor I
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.45 - complement factor I
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REACTION DIAGRAM
benzoyl-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Gly-Gly-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
benzyloxycarbonyl-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Leu-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
complement component C3 + H2O
?
structural but not functional roles for the three N-linked oligosaccharide chains indicated, N-linked glycan pool composition of the heavy and light chains indicated
-
-
?
complement component C3b + H2O
complement component iC3b
-
-
a major opsonin
-
?
complement component C3bi + H2O
?
-
the breakdown of human erythrocyte-bound C3bi molecules in serum or plasma is mediated only by factor I
-
-
?
complement component C3bi + H2O
complement component C3c + ?
-
complement component C3bi bound to human erythrocytes is rapidly cleaved, unlike complement component C3bi bound to other species
-
?
methylsulfonyl-D-Phe-Gly-Arg-4-methylcoumaryl-7-amide + H2O
methylsulfonyl-D-Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-alpha-tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
N-alpha-tert-butyloxycarbonyl-Val-Pro-Lys + 7-amino-4-methylcoumarin
-
low activity
-
?
N-alpha-tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
N-alpha-tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Phe-Gly-Arg-4-methylcoumaryl-7-amide + H2O
Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
tert-butyloxycarbonyl-Asp(benzyl ester)-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp(benzyl ester)-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Ile-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
low activity
-
?
?
-
enzyme is involved in the regulation of complement activation, it catalyzes the limited proteolysis of the alpha-chains of complement component C4b and complement component C4b
-
-
?
complement component C3b + H2O
?
-
cleavage at five different sites in the alpha-chain, generating complement component C3d.g-like fragments with three different N-terminal and two different C-terminal ends
-
-
?
complement component C3b + H2O
?
-
degradation in presence of C4b binding protein and factor H
-
-
?
complement component C3b + H2O
?
-
cleavage of three peptide bonds in the alpha chain of complement component C3b, thereby inactivating this protein
-
-
?
complement component C3b + H2O
?
-
enzyme is involved in the regulation of complement activation, it catalyzes the limited proteolysis of the alpha-chains of complement component C4b and complement component C4b
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
-
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
phosphorylation of complement component C3b inhibits the cleavage of the alpha'-chain of complement component C3b
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
cleavage at five different sites in the alpha-chain, generating complement component C3d.g-like fragments with three different N-terminal and two different C-terminal ends
-
-
?
complement component C3b + H2O
complement component C3c + ?
mutation of complement factor I associated to atypical hemolytic uremic syndrome analyzed, activity observed in mutant protein comparable to wild-type
-
-
?
complement component C3b + H2O
complement component C3c + ?
complement factor I mutants predisposing to atypical hemolytic uremic syndrome analyzed, cofactor function of complement components C3b and Cb4 tested
-
-
?
complement component C3b + H2O
complement component C3c + ?
complement factor I production of human keratinocytes analyzed, with and without stimulation by IFN-gamma, IL-1alpha, IL-6, TNF-alpha, TGF-beta1
-
-
?
complement component C3b + H2O
complement component C3c + ?
production of complement factor I in non-small cell lung cancer cell lines analyzed
-
-
?
complement component C3b + H2O
complement component C3c + ?
studies on membranoproliferative glomerulonephritis, potential relation to complement factor I analyzed
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
cleavage of three peptide bonds in the alpha-chain of complement component C3b
-
-
?
complement component iC3b + ?
-
cleavage does not require presence of factor H
-
?
complement component C3b + H2O
complement component iC3b + ?
-
the complement C3 fragments C3b and iC3b appear on the surface of several virulent Staphylococcus aureus strains of capsule polysaccharide type 5 and 8. Factor I mediates the cleavage of C3b to iC3b on the surface of Staphylococcus aureus and appears to be able to function without the serum cofactor, factor H
-
?
complement component C3b + H2O
complement component iC3b + ?
-
Nipah virus-dependent inactivation of C3b only occurs with the cofactors factor H and soluble CR1 but not with CD46. When factor I is coupled with factor H, this cleavage can occur at two possible sites in the alpha' chain: R1281 and R1298, sites 1 and 2. In the presence of CR1, factor I can cleave the alpha' chain at sites 1 and 2 but also at an additional site at R932
-
-
?
complement component C3b + H2O
inactivated C3b + ?
-
factor I mediates cleavage of C3b between Arg1298 and Ser1299
-
-
?
complement component C4b + H2O
?
-
enzyme is involved in the regulation of complement activation, it catalyzes the limited proteolysis of the alpha chains of complement component C4b and C4b
-
-
?
complement component C4b + H2O
?
-
-
-
-
?
complement component C4b + H2O
?
-
degradation in presence of C4b binding protein and factor H
-
-
?
complement component C4b + H2O
?
-
cleavage of two peptide bonds in the alpha chain of complement component C4b, thereby inactivating this protein
-
-
?
complement component C4b + H2O
?
-
enzyme is involved in the regulation of complement activation, it catalyzes the limited proteolysis of the alpha chains of complement component C4b and C4b
-
-
?
complement component C4b + H2O
complement component C4c + C4d
-
-
-
-
?
complement component C4b + H2O
complement component C4c + C4d
-
-
-
?
complement component C4b + H2O
complement component C4c + C4d
-
-
-
?
complement component C4b + H2O
complement component C4c + C4d
-
a nicked form of complement component C4b, complement component C4b', consisting of four disulfide-linked polypeptide chains, is formed as an intermediate product before cleavage of complement component C4b into complement component C4c and complement component C4d
-
?
complement component C4b + H2O
complement component C4c + C4d
-
cleavage of two peptide bonds in the alpha chain of C4b
-
-
?
?
-
-
no cleavage of H-Gly-Arg-7-amido-4-methylcoumarin, MeOSuc-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin or N-alpha-tert-butyloxycarbonyl-leu-Gly-Arg-7-amido-4-methylcoumarin
-
?
additional information
?
-
complement factor I production analyzed by RT-PCR
-
-
?
additional information
?
-
complement factor I production analyzed, no mRNA expression detected
-
-
?
additional information
?
-
production of complement factor I analyzed, no mRNA expression detected
-
-
?
additional information
?
-
human factor I has little species-specificity like pig factor I, according to the relatively high homology of the AA sequences in the serine protease region, in comparison with those of membrane complement regulatory proteins
-
-
?
additional information
?
-
-
human factor I has little species-specificity like pig factor I, according to the relatively high homology of the AA sequences in the serine protease region, in comparison with those of membrane complement regulatory proteins
-
-
?
additional information
?
-
-
Staphylococcus aureus expressing clumping factor A (ClfA) (P336A Y338S) is more susceptible to complement-mediated phagocytosis than a ClfA-null mutant or the wild type. Unlike clumping factor A, the mutant ClfA(P336A Y338S) does not enhance factor I cleavage of C3b to iC3b and inhibits the cofactor function of factor H. Fibrinogen enhances factor I binding to clumping factor A and the Staphylococcus aureus surface
-
-
?
additional information
?
-
-
no activity with complement component C4b
-
-
?