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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
-
?
Boc-Asp(benzyl)-Pro-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
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 C3(NH3) + H2O
?
-
cleaved by SP domain-form
-
-
?
complement component C3b + H2O
?
complement component C3b + H2O
complement component C3c + ?
complement component C3b + H2O
complement component iC3b
-
-
a major opsonin
-
?
complement component C3b + H2O
complement component iC3b + ?
complement component C3b + H2O
inactivated C3b + ?
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
-
?
complement component C4b + H2O
?
complement component C4b + H2O
complement component C4c + C4d
complement factor C3b + H2O
?
-
-
-
-
?
complement factor C4b + H2O
?
-
-
-
-
?
FGR-7-amido-4-methylcoumarin + H2O
FGR + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
?
additional information
?
-
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 C3b + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
complement component C3b + H2O
?
-
-
-
-
?
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 + ?
-
-
-
?
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 + ?
-
-
-
?
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 + ?
-
-
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
cleavage of three peptide bonds in the alpha-chain of complement component C3b
-
-
?
complement component C3b + H2O
complement component C3c + ?
-
-
-
-
?
complement component C3b + H2O
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 + ?
-
-
-
-
?
complement component C3b + H2O
inactivated C3b + ?
-
factor I mediates cleavage of C3b between Arg1298 and Ser1299
-
-
?
complement component C3b + H2O
inactivated C3b + ?
-
-
-
-
?
complement component C4b + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
complement component C4b + H2O
?
-
degradation in presence of C4b binding protein and factor H
-
-
?
complement component C4b + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
complement component C4b + H2O
complement component C4c + C4d
-
cleavage of two peptide bonds in the alpha chain of C4b
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
can be expressed on xenogeneic cell membranes
-
-
?
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complement component C3(NH3) + H2O
?
-
cleaved by SP domain-form
-
-
?
complement component C3b + H2O
?
complement component C3b + H2O
complement component C3c + ?
complement component C3b + H2O
complement component iC3b
-
-
a major opsonin
-
?
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 C3bi + H2O
?
-
the breakdown of human erythrocyte-bound C3bi molecules in serum or plasma is mediated only by factor I
-
-
?
complement component C4b + H2O
?
complement component C4b + H2O
complement component C4c + C4d
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
-
-
?
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 C3b + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
complement component C3b + H2O
?
-
-
-
-
?
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 + ?
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 component C4b + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
complement component C4b + H2O
?
-
degradation in presence of C4b binding protein and factor H
-
-
?
complement component C4b + H2O
?
-
-
-
-
?
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
-
-
-
?
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2-mercaptoethanol
-
10 mM, strong
4-(2-aminoethyl)benzenesulfonyl fluoride
-
0.25 mM, inhibits SP domain form and fI
benzamidine
-
20 mM, 82% inhibition of amidolytic activity
benzenesulfonyl fluorides
-
inhibits amidolytic activity
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
-
0.05 mM, 82% inhibition; inhibits amidolytic activity
Cr2+
-
inhibition of proteolytic and amidolytic activity, 54% inhibition of amidolytic activity at 1 mM, 43% inhibition of proteolytic activity at 0.1 mM
Cu2+
-
23% inhibition of amidolytic activity at 1 mM
diisopropylfluorophosphate
-
-
dithiothreitol
-
1 mM, strong
epsilon-aminocaproic acid
-
20 mM, 10% inhibition of amidolytic activity
factor H
-
inhibits SP domain form
-
Fe3+
-
inhibition of proteolytic and amidolytic activity, 59% inhibition of amidolytic activity at 1 mM, 23% inhibition of proteolytic activity at 0.1 mM
Hg2+
-
26% inhibition of amidolytic activity at 1 mM
Lima bean trypsin inhibitor
-
0.05 mM, 20% inhibition of amidolytic activity
-
NEM
-
1 mM, partial inhibition
Pefabloc TH
-
0.25 mM, 58% inhibition of amidolytic activity
Pefabloc-SC
-
0.00025 mM, complete inhibition of amidolytic activity
Pefabloc-Xa
-
0.00025 mM, 93% inhibition of amidolytic activity
PMSF
-
1 mM, 42% inhibition of amidolytic activity
Soybean trypsin inhibitor
-
0.05 mM, 37% inhibition of amidolytic activity
-
Zn2+
-
0.1 mM, 59% inhibition of proteolytic activity
amyloid beta
-
binds to complement factor I which inhibits the ability of factor I to cleave C3b to inactivated C3b. Addition of factor I restores inactivated C3b production in amyloid beta-treated RPE cells. Preincubation of factor I with amyloid beta in the presence of factor H abolishes the ability of factor I to cleave FGR-7-amino-4-methylcoumarin
-
amyloid beta
-
production of inactivated C3b is significantly decreased when C3b and factor H are incubated with eyes from neprilysin gene-disrupted mice, which leads to an increased deposition of amyloid beta, compared with when C3b and factor H are incubated with eyes from wild-type mice
-
antipain
-
0.1 mM, 80% inhibition of amidolytic activity
antipain
-
0.1 mM, inhibits SP domain form and fI
Aprotinin
-
0.0005 mM, 23% inhibition of proteolytic activity. 0.0005 mM, 37% inhibition of amidolytic activity
Aprotinin
-
0.005 mM, inhibits SP domain form and fI
K-76COOH
-
-
leupeptin
-
0.01 mM, 24% inhibition of amidolytic activity; 0.01 mM, 29% inhibition of proteolytic activity
leupeptin
-
0.01 mM, inhibits SP domain form and fI
suramin
-
1 mM, 90% inhibition of proteolytic activity. 1 mM, 87% inhibition of amidolytic activity
suramin
-
1 mM, inhibits fI
suramin
-
weak inhibition
additional information
-
no inhibition by 0.1 mM 1,10-phenanthroline, 0.001 mM pepstatin A, 0.1 mM chymostatin, 0.0002 mM, C1 inhibitor and 0.1 mM bestatin
-
additional information
-
factor I is in a proteolytically inactive form, it circulates in a zymogen-like state despite being fully processed to the mature sequence. This inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain. Once the ternary complex of factor I, a cofactor and a substrate is formed, the allosteric inhibition is released, and factor I is oriented for cleavage
-
additional information
-
the enzyme does not have any known physiological inhibitor, although synthetic inhibitors, such as suramin, are able to weakly inhibit it
-
additional information
-
phosphorylation of C3b inhibits the cleavage of the alpha'-chain of C3b
-
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1622
A2G2, deduced molecular weight of N-linked glycan structure
1824
A3G2, deduced molecular weight of N-linked glycan structure
1912
A2G2S1, deduced molecular weight of N-linked glycan structure
2115
A3G2S1, deduced molecular weight of N-linked glycan structure
2202
A2G2S2, deduced molecular weight of N-linked glycan structure
2277
A3G3S1, deduced molecular weight of N-linked glycan structure
2405
A3G2S2, deduced molecular weight of N-linked glycan structure
2567
A3G3S2, deduced molecular weight of N-linked glycan structure
27000
-
1 * 27000 + 1 * 37500, calculation from nucleotide sequence
27590
calculated for non-glycosylated light chain, estimated basing upon results of the N-linked glycan analysis
28500
-
1 * 28500 + 1 * 38000, calculation from nucleotide sequence
30270
estimated for light chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
35290
calculated for non-glycosylated heavy chain, estimated basing upon results of the N-linked glycan analysis
3569
approximate reduction of molecular weight for the heavy chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
35900
native light chain, estimated basing upon results from the N-linked glycan analysis
37500
-
1 * 27000 + 1 * 37500, calculation from nucleotide sequence
37960
estimated for heavy chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
41530
native heavy chain, estimated basing upon results from the N-linked glycan analysis
5632
approximate reduction of molecular weight for the light chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
62880
total calculated molecular weight for non-glycosylated factor I, estimated basing upon results of the N-linked glycan analysis
66000
-
nonglycosylated proenzyme
68230
estimated for total protein bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
75000
-
x * 75000, SDS-PAGE
77430
deduced for total protein of the native factor I basing upon results from the N-linked glycan analysis
892
Man3GlcNAc2 core, deduced molecular weight of N-linked glycan structure
9201
approximate reduction of molecular weight for total molecule of factor I after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
additional information
mutant protein reveals a slightly different migration pattern during electrophoresis under reducing conditions, due to proximity of the mutation to a cysteine residue
38000
-
SP-domain-form, SDS-PAGE
38000
-
Western blotting, light chain of CFI under reducing conditions
38000
-
light-chain, Western blot, reducing condition
38000
-
1 * 28500 + 1 * 38000, calculation from nucleotide sequence
38000
-
1 * 38000 + 1 * 50000, non-catalytic 50000 Da subunit is disulfide-linked to the 38000 Da catalytic subunit
38000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview
50000
heavy chain of
50000
heavy chain, indicative of processing
50000
-
Western blotting, truncated Q336x mutant under non-reducing conditions and heavy chain of CFI under reducing conditions
50000
-
heavy-chain, Western blot, reducing condition
50000
-
1 * 38000 + 1 * 50000, non-catalytic 50000 Da subunit is disulfide-linked to the 38000 Da catalytic subunit
50000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview
88000
-
sucrose density gradient centrifugation
88000
-
SDS-PAGE, non-reducing conditions
88000
non-reduced CFI proteins, SDS-PAGE
88000
non-reduced form, SDS-PAGE
88000
reduced form, RRKR-linker peptide not cleaved, corresponds to pro-complemement factor I
88000
reduced form, RRKR-linker peptide not cleaved, corresponds to pro-complement factor I
88000
SDS-PAGE, nonreducing conditions, detection of murine complement factor I by using a crossreactive polyclonal goat antibody against human complement factor I
88000
-
coimmunoprecipitation analysis
88000
-
Western blotting, wild-type and the Q232K, C237Y and S250L mutants under non-reducing conditions
88000
-
Western blot, non-reducing condition
90000
unprocessed, under reducing conditions, SDS-PAGE
90000
-
Western blotting, unprocessed CFI protein under reducing conditions
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A222G
-
secretion of mutant protein significantly lower compared to wild-type when expressed in human embryonic kidney cells. Mutant cleaves the alpha'-chains of complement factor C4b and C3b as efficiently as wild-type in solution. Compared to wild-type mutant A22G shows impaired cleavage of complement factor C3b on the surface of sheep erythrocytes. Mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) as efficiently as wild-type
C196S
-
naturally occuring mutation, causes a failure in secretion of the enzyme
C237Y
-
mutation affects secretion, is expressed in smaller amounts as the wild-type. Does not degrade C4b and C3b as efficiently as the wild-type
C25F
-
mutant is as efficiently expressed in human embryonic kidney cells as wild-type, mutant protein is not secreted. Mutant is sensitive to EndoH digestion, indicating that it does not reach the late Golgi compartment and is retained in the endoplasmic reticulum
D104S
-
site-directed mutagenesis, altered kinetics compared to the wild-type
D207N/Q219A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
D207N/Q219A/M220A/K221Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
D26N/K27Q/F29A/Q31A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b and in the degradation of surface-bound C3b deposited on sheep erythrocytes
D385N/K387S
-
site-directed mutagenesis, altered kinetics compared to the wild-type
D420N/N422T
-
site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogue C3met
D497N
-
site-directed mutagenesis, altered kinetics compared to the wild-type
F29A/Q31A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b
F82N/N84T
-
site-directed mutagenesis, the mutation in the FIMAC domain impairs enzyme activity, which is rescued by deglycosylation of the mutant
F94A/K182Q/R184Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b. Mutant shows greatly impaired activity in the degradation of surface-bound C3b deposited on sheep erythrocytes
G170V
-
is expressed at low levels. Does degrade C4b and C3b
G243D
cofactor function of complement components C3b and Cb4 not affected
G261D
mutation in the complement factor I heavy chain associated with atypical hemolytic uremic syndrome, recombinant protein generated, activity tested
G71V
-
naturally occuring mutation, causes a failure in secretion of the enzyme
H165R
-
mutant is as efficiently expressed and secreted in human embryonic kidney cells as wild-type. Mutant cleaves the alpha'-chains of complement factor C4b and C3b more efficiently than wild-type in the presence of C4b-binding protein and factor H as cofactors in solution. Cleavage of complement factor C3b on the surface of sheep erythrocytes is similar to wild-type. In the presence of membrane cofactor protein mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) more efficiently than wild-type
H400L
-
mutation affects secretion, is expressed at low levels. Does degrade C4b and C3b
I322T
amino acid exchange in the serine protease domain, resulting in secreted proteins that lack cofactor function of complement components C3b and C4b
I339M
-
mutation affects secretion, is expressed at low levels
K124N
-
site-directed mutagenesis, altered kinetics compared to the wild-type
K124Q/R150Q/F151A/K152Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
K182N/R184S
-
site-directed mutagenesis, altered kinetics compared to the wild-type
K182Q/R184Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type. Mutant shows similar activity to wild-type in degradation of fluid-phase complement factor C4b or C3b and in the degradation of surface-bound C3b deposited on sheep erythrocytes
K326N/A328T
-
site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogue C3met
K458N/N460T
-
site-directed mutagenesis, altered kinetics compared to the wild-type
K51A/R62A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type, only mutant in the FI and membrane attack complex domain (FIMAC) which shows some activity in degradation of fluid-phase complement factor C4b or C3b
K51A/R62A/L73A/L76A/F82A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
K93Q/F94A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type. Compared to wild-type mutant shows decreased but not abolished activity in degradation of fluid-phase complement factor C4b or C3b. Mutant shows impaired activity in the degradation of surface-bound C3b deposited on sheep erythrocytes
L171N
-
site-directed mutagenesis, altered kinetics compared to the wild-type
L289x
-
deletion mutant (c.893delC) leading to a premature stop codon. Mutant protein is not secreted when expressed in human embryonic kidney cells
L73A/L76A/F82A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
M120V
-
mutant is as efficiently expressed in human embryonic kidney cells as wild-type, secretion is significantly lower compared to wild-type. Mutant cleaves the alpha'-chains of complement factor C4b and C3b more efficiently than wild-type in the presence of C4b-binding protein and factor H as cofactors in solution. Mutant cleaves complement factor C3b more efficiently in the presence of membrane cofactor protein in solution. Compared to wild-type mutant M120V shows enhanced cleavage of complement factor C3b on the surface of sheep erythrocytes. In the presence of membrane cofactor protein mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) more efficiently than wild-type
M220A/K221Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
N133S
-
mutant protein is not secreted when expressed in human embryonic kidney cells, mutant is sensitive to EndoH digestion, indicating that it does not reach the late Golgi compartment and is retained in the endoplasmic reticulum
N404T
-
site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogues C3met and C4met
P32A
-
mutant is as efficiently expressed and secreted in human embryonic kidney cells as wild-type. P32A mutant shows impaired function towards degradation of the alpha'-chains of complement factor C4b at the two highest concentrations and of the alpha'-chain of C3b at the highest concentration when factor H is used as cofactor. No significant impairment when complement receptor 1 and membrane cofactor protein 1 are used as cofactors. Compared to wild-type mutant P32A shows impaired cleavage of complement factor C3b on the surface of sheep erythrocytes. Mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) as efficiently as wild-type
Q210N/V212T
-
site-directed mutagenesis, altered kinetics compared to the wild-type
Q219N/K221S
-
site-directed mutagenesis, altered kinetics compared to the wild-type
Q232K
-
mutation affects secretion, is expressed in smaller amounts as the wild-type. Does degrade C4b and C3b
Q242N/K244S
-
site-directed mutagenesis, the mutation in the LDLr2 domain decreases the binding of the enzyme to substrate analogues C3met and C4met
Q257N/Q259S
-
site-directed mutagenesis, the mutation in the LDLr2 domain decreases the binding of the enzyme to substrate analogues C3met and C4met
Q336x
-
truncated mutant can be expressed, in vitro, at a level similar to that of the wild-type, but is not functional because it lacks the serine protease domain. Is not detected in serum of the patient
R130Q/R169Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
R150Q/F151A/K152Q
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type
R201S
-
present only in Far East populations with frequencies of about 0.03 in the main island of Japan and lower than 0.01 in Okinawa and Korea
R35N/I37T
-
site-directed mutagenesis, the mutation in the FIMAC domain impairs enzyme activity, which is rescued by deglycosylation of the mutant
R365N
-
site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogues C3met and C4met
R388H
cofactor function of complement components C3b and Cb4 not affected
R406H
-
present almost exclusively in East Asians and at highest frequencies in southern Chinese Han and Thais
R456x
-
point mutant leading to a premature stop codon. Mutant protein is not secreted when expressed in human embryonic kidney cells
R502L
-
must have arisen in a southeastern part of Asia and thereafter has spread to neighboring populations
R61N
-
site-directed mutagenesis, altered kinetics compared to the wild-type
S250L
-
mutation affects secretion, is expressed in smaller amounts as the wild-type. Cleaves C4b and C3b in the same manner as the wild-type
S561N/Y563T
-
site-directed mutagenesis, the mutation in the serine protease domain impairs enzyme activity, which is rescued by deglycosylation of the mutant
T520x
-
insertion mutant (c. 1610insAT) leading to a premature stop codon, mutant protein is not secreted when expressed in human embryonic kidney cells
T54N/V56T
-
site-directed mutagenesis, altered kinetics compared to the wild-type
V212A/L236A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b. Mutant shows no activity in the degradation of surface-bound C3b deposited on sheep erythrocytes
V252A/I267A
-
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b. Mutant shows no activity in the degradation of surface-bound C3b deposited on sheep erythrocytes
W468x
-
deletion mutant (c.1446-1450 delTTCAC) leading to a premature stop codon, mutant is as efficiently expressed in human embryonic kidney cells as wild-type but protein is not secreted
W528x
-
point mutant leading to a premature stop codon. Mutant protein is not secreted when expressed in human embryonic kidney cells
Y369S
-
patient heterozygous for a novel missense mutation in CFI. This polymorphism is within a functional domain. It is located in the 38 kDa chain of the protein within the serine protease domain that is linked by a disulfide bond to the noncatalytic heavy chain of factor I
D501N
amino acid exchange in the serine protease domain, resulting in secreted proteins that lack cofactor function of complement components C3b and C4b
D501N
-
mutant is as efficiently expressed and secreted in human embryonic kidney cells as wild-type, mutant does not degrade complement factor C4b or C3b. In contrast to wild-type mutant D501N does not cleave C3b alpha'chain on the surface of endothelial cells (HUVEV-cells)
D506V
-
leads to partial IF-deficiency
D506V
amino acid exchange in the serine protease domain, resulting in secreted proteins that lack cofactor function of complement components C3b and C4b
M120I
clinical data of aHUS-atients with complement factor I mutation summarized, cofactor function of complement components C3b and Cb4 not affected
M120I
clinical data of aHUS-patients with complemment factor I mutation summarized, cofactor function of complement components C3b and Cb4 not affected
R299W
amino acid exchange in the heavy chain, about 30% activity retained
R299W
-
mutant is as efficiently expressed in human embryonic kidney cells as wild-type, secretion is significantly lower compared to wild-type. Mutant cleaves the alpha'-chains of complement factor C4b and C3b as efficiently as wild-type in solution. Cleavage of complement factor C3b on the surface of sheep erythrocytes is similar to wild-type. In the presence of membrane cofactor protein mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) more efficiently than wild-type
W127X
-
stop-codon, leads to partial IF-deficiency
W127X
-
point mutant leading to a premature stop codon. Mutant protein is not secreted when expressed in human embryonic kidney cells
additional information
-
del 922C, leads to partial IF-deficiency
additional information
deletion mutant delTTCAC (1446-1450) analyzed, no secretion observed
additional information
-
mutations in the FIMAC, CD5, and LDLr1 domains do not decrease the binding of the enzyme to substrate analogues C3met or C4met
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Davis III, A.E.; Alper, C.A.
Factor I (C3b inactivator) the complement regulatory protease
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
553-558
1984
Cavia porcellus, Rattus norvegicus
-
brenda
Ekdahl, K.N.; Nilsson, U.R.; Nilsson, B.
Inhibition of factor I by diisopropylfluorophosphate. Evidence of conformational changes in factor I induced by C3b and additional studies on the specificity of factor I
J. Immunol.
144
4269-4274
1990
Homo sapiens
brenda
Medicus, R.G.; Melamed, J.; Arnaout, M.A.
Role of human factor I and C3b receptor in the cleavage of surface-bound C3bi molecules
Eur. J. Immunol.
13
465-470
1983
Homo sapiens
brenda
Kaidoh, T.; Gigli, I.
Phylogeny of regulatory proteins of the complement system. Isolation and characterization of a C4b/C3b inhibitor and a cofactor from sand bass plasma
J. Immunol.
142
1605-1613
1989
Paralabrax nebulifer
brenda
Hsiung, L.; Barclay, A.N.; Brandon, M.R.; Sim, E.; Porter, R.R.
Purification of human C3b inactivator by monoclonal-antibody affinity chromatography
Biochem. J.
203
293-298
1982
Homo sapiens
brenda
Crossley, L.G.
C3b inactivator and beta1H
Methods Enzymol.
80
112-124
1981
Homo sapiens
brenda
Nagasawa, S.; Ichihara, C.; Stroud, R.M.
Cleavage of C4b by C3b inactivator: production of a nicked form of C4b, C4b', as an intermediate cleavage product of C4b by C3b inactivator
J. Immunol.
125
578-582
1980
Homo sapiens
brenda
Fujita, T.; Nussenzweig, V.
The role of C4-binding protein and beta1H in proteolysis of C4b and C3b
J. Exp. Med.
150
267-276
1979
Homo sapiens
brenda
Gaither, T.A.; Hammer, C.H.; Frank, M.M.
Studies of the molecular mechanisms of C3b inactivation and a simplified assay of beta1H and the C3b inactivator (C3bINA)
J. Immunol.
123
1195-1204
1979
Homo sapiens
brenda
Schlaf, G.; Rothermel, E.; Oppermann, M.; Schieferdecker, H.L.; Jungermann, K.
Rat complement factor I: molecular cloning, sequencing and expression in tissue and isolated cells
Immunology
94
464-474
1999
Rattus norvegicus
brenda
Minta, J.O.; Wong, M.J.; Kozak, C.A.; Kunnath-Muglia, L.M.; Goldberger, G.
cDNA Cloning, sequencing and chromosomal assignment of the gene for mouse complement factor I (C3b/C4b inactivator): Identification of a species specific divergent segment in factor I
Mol. Immunol.
33
101-112
1996
Mus musculus
brenda
Kunnath-Muglia, L.M.; Chang, G.H.; Sim, R.B.; Day, A.J.; Ezekowitz, R.A.B.
Characterization of Xenopus laevis complement factor I structure - conservation of modular structure except for an unusual insert not present in human factor
Mol. Immunol.
30
1249-1256
1993
Xenopus laevis
brenda
DiScipio, R.G.
The fractionation of human plasma proteins
Protein Expr. Purif.
5
178-186
1994
Homo sapiens
brenda
Van den Berg, C.W.; Perez de la Lastra, J.M.; Llanes, D.; Morgan, B.P.
Purification and characterization of the pig analogue of human membrane cofactor protein (CD46/MCP)
J. Immunol.
158
1703-1709
1997
Homo sapiens, Sus scrofa
brenda
Ekdahl, K.N.; Nilsson, B.
Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase
J. Immunol.
154
6402-6510
1995
Homo sapiens
-
brenda
Cunnion, K.M.; Hair, P.S.; Buescher, E.S.
Cleavage of complement C3b to iC3b on the surface of Staphylococcus aureus is mediated by serum complement factor I
Infect. Immun.
72
2858-2863
2004
Homo sapiens
brenda
Tsiftsoglou, S.A.; Sim, R.B.
Human complement factor I does not require cofactors for cleavage of synthetic substrates
J. Immunol.
173
367-375
2004
Homo sapiens
brenda
Tsiftsoglou, S.A.; Willis, A.C.; Li, P.; Chen, X.; Mitchell, D.A.; Rao, Z.; Sim, R.B.
The catalytically active serine protease domain of human complement factor I
Biochemistry
44
6239-6249
2005
Homo sapiens
brenda
Kavanagh, D.; Kemp, E.J.; Mayland, E.; Winney, R.J.; Duffield, J.S.; Warwick, G.; Richards, A.; Ward, R.; Goodship, J.A.; Goodship, T.H.
Mutations in complement factor I predispose to development of atypical hemolytic uremic syndrome
J. Am. Soc. Nephrol.
16
2150-2155
2005
Homo sapiens
brenda
Cunnion, K.M.; Buescher, E.S.; Hair, P.S.
Serum complement factor I decreases Staphylococcus aureus phagocytosis
J. Lab. Clin. Med.
146
279-286
2005
Homo sapiens
brenda
Tsiftsoglou, S.A.; Arnold, J.N.; Roversi, P.; Crispin, M.D.; Radcliffe, C.; Lea, S.M.; Dwek, R.A.; Rudd, P.M.; Sim, R.B.
Human complement factor I glycosylation: structural and functional characterisation of the N-linked oligosaccharides
Biochim. Biophys. Acta
1764
1757-1766
2006
Homo sapiens (P05156), Homo sapiens
brenda
Rose, K.L.; Paixao-Cavalcante, D.; Fish, J.; Manderson, A.P.; Malik, T.H.; Bygrave, A.E.; Lin, T.; Sacks, S.H.; Walport, M.J.; Cook, H.T.; Botto, M.; Pickering, M.C.
Factor I is required for the development of membranoproliferative glomerulonephritis in factor H-deficient mice
J. Clin. Invest.
118
608-618
2008
Mus musculus (Q61129)
brenda
Nilsson, S.C.; Karpman, D.; Vaziri-Sani, F.; Kristoffersson, A.C.; Salomon, R.; Provot, F.; Fremeaux-Bacchi, V.; Trouw, L.A.; Blom, A.M.
A mutation in factor I that is associated with atypical hemolytic uremic syndrome does not affect the function of factor I in complement regulation
Mol. Immunol.
44
1835-1844
2007
Homo sapiens (P05156)
brenda
Timar, K.K.; Junnikkala, S.; Dallos, A.; Jarva, H.; Bhuiyan, Z.A.; Meri, S.; Bos, J.D.; Asghar, S.S.
Human keratinocytes produce the complement inhibitor factor I: Synthesis is regulated by interferon-gamma
Mol. Immunol.
44
2943-2949
2007
Homo sapiens (P05156), Homo sapiens
brenda
Okroj, M.; Hsu, Y.F.; Ajona, D.; Pio, R.; Blom, A.M.
Non-small cell lung cancer cells produce a functional set of complement factor I and its soluble cofactors
Mol. Immunol.
45
169-179
2008
Homo sapiens (P05156)
brenda
Kavanagh, D.; Richards, A.; Noris, M.; Hauhart, R.; Liszewski, M.K.; Karpman, D.; Goodship, J.A.; Fremeaux-Bacchi, V.; Remuzzi, G.; Goodship, T.H.; Atkinson, J.P.
Characterization of mutations in complement factor I (CFI) associated with hemolytic uremic syndrome
Mol. Immunol.
45
95-105
2008
Homo sapiens (P05156)
brenda
Chan, M.R.; Thomas, C.P.; Torrealba, J.R.; Djamali, A.; Fernandez, L.A.; Nishimura, C.J.; Smith, R.J.; Samaniego, M.D.
Recurrent atypical hemolytic uremic syndrome associated with factor I mutation in a living related renal transplant recipient
Am. J. Kidney Dis.
53
321-326
2009
Homo sapiens
brenda
Fagerness, J.A.; Maller, J.B.; Neale, B.M.; Reynolds, R.C.; Daly, M.J.; Seddon, J.M.
Variation near complement factor I is associated with risk of advanced AMD
Eur. J. Hum. Genet.
17
100-104
2009
Homo sapiens
brenda
Nilsson, S.C.; Trouw, L.A.; Renault, N.; Miteva, M.A.; Genel, F.; Zelazko, M.; Marquart, H.; Muller, K.; Sjoeholm, A.G.; Truedsson, L.; Villoutreix, B.O.; Blom, A.M.
Genetic, molecular and functional analyses of complement factor I deficiency
Eur. J. Immunol.
39
310-323
2009
Homo sapiens
brenda
Yuasa, I.; Nakagawa, M.; Umetsu, K.; Harihara, S.; Matsusue, A.; Nishimukai, H.; Fukumori, Y.; Saitou, N.; Park, K.S.; Jin, F.; Lucotte, G.; Chattopadhyay, P.K.; Henke, L.; Henke, J.
Molecular basis of complement factor I (CFI) polymorphism: one of two polymorphic suballeles responsible for CFI A is Japanese-specific
J. Hum. Genet.
53
1016-1021
2008
Homo sapiens
brenda
Wang, J.; Ohno-Matsui, K.; Yoshida, T.; Kojima, A.; Shimada, N.; Nakahama, K.; Safranova, O.; Iwata, N.; Saido, T.C.; Mochizuki, M.; Morita, I.
Altered function of factor I caused by amyloid beta: implication for pathogenesis of age-related macular degeneration from Drusen
J. Immunol.
181
712-720
2008
Homo sapiens, Mus musculus
brenda
Hair, P.S.; Ward, M.D.; Semmes, O.J.; Foster, T.J.; Cunnion, K.M.
Staphylococcus aureus clumping factor A binds to complement regulator factor I and increases factor I cleavage of C3b
J. Infect. Dis.
198
125-133
2008
Homo sapiens
brenda
Ponce-Castro, I.M.; Gonzalez-Rubio, C.; Delgado-Cervino, E.M.; Abarrategui-Garrido, C.; Fontan, G.; Sanchez-Corral, P.; Lopez-Trascasa, M.
Molecular characterization of Complement Factor I deficiency in two Spanish families
Mol. Immunol.
45
2764-2771
2008
Homo sapiens
brenda
Nakahata, K.; Matsunami, K.; Kobayashi, C.; Omori, T.; Xu, H.; Firdawes, S.; Fukuzawa, M.; Miyagawa, S.
Analysis of the serine protease function of porcine factor I produced by liver cells for xenotransplantation
Transpl. Immunol.
19
30-36
2008
Sus scrofa, Homo sapiens (P05156), Homo sapiens
brenda
Nilsson, S.C.; Kalchishkova, N.; Trouw, L.A.; Fremeaux-Bacchi, V.; Villoutreix, B.O.; Blom, A.M.
Mutations in complement factor I as found in atypical hemolytic uremic syndrome lead to either altered secretion or altered function of factor I
Eur. J. Immunol.
40
172-185
2010
Homo sapiens
brenda
Abernathy, J.W.; Lu, J.; Liu, H.; Kucuktas, H.; Liu, Z.
Molecular characterization of complement factor I reveals constitutive expression in channel catfish
Fish Shellfish Immunol.
27
529-534
2009
Ictalurus punctatus (C9D6Z5), Ictalurus punctatus
brenda
Hair, P.S.; Echague, C.G.; Sholl, A.M.; Watkins, J.A.; Geoghegan, J.A.; Foster, T.J.; Cunnion, K.M.
Clumping factor A interaction with complement factor I increases C3b cleavage on the bacterial surface of Staphylococcus aureus and decreases complement-mediated phagocytosis
Infect. Immun.
78
1717-1727
2010
Homo sapiens
brenda
Shin, D.H.; Webb, B.M.; Nakao, M.; Smith, S.L.
Characterization of shark complement factor I gene(s): genomic analysis of a novel shark-specific sequence
Mol. Immunol.
46
2299-2308
2009
Ginglymostoma cirratum (B0LCZ7), Ginglymostoma cirratum (B0LCZ8), Ginglymostoma cirratum (B0LCZ9), Ginglymostoma cirratum (B0LD00), Ginglymostoma cirratum
brenda
Ennis, S.; Gibson, J.; Cree, A.; Collins, A.; Lotery, A.
Support for the involvement of complement factor I in age-related macular degeneration
Eur. J. Hum. Genet.
18
15-16
2010
Homo sapiens
brenda
Anastasiou, V.; Mikrou, A.; Papanastasiou, A.; Zarkadis, I.
The molecular identification of factor H and factor I molecules in rainbow trout provides insights into complement C3 regulation
Fish Shellfish Immunol.
31
491-499
2011
Oncorhynchus mykiss (E7BAR3), Oncorhynchus mykiss
brenda
Roversi, P.; Johnson, S.; Caesar, J.J.; McLean, F.; Leath, K.J.; Tsiftsoglou, S.A.; Morgan, B.P.; Harris, C.L.; Sim, R.B.; Lea, S.M.
Structural basis for complement factor I control and its disease-associated sequence polymorphisms
Proc. Natl. Acad. Sci. USA
108
12839-12844
2011
Homo sapiens
brenda
Sanchez-Gallego, J.I.; Groeneveld, T.W.; Krentz, S.; Nilsson, S.C.; Villoutreix, B.O.; Blom, A.M.
Analysis of binding sites on complement factor I using artificial N-linked glycosylation
J. Biol. Chem.
287
13572-13583
2012
Homo sapiens
brenda
Broderick, L.; Gandhi, C.; Mueller, J.L.; Putnam, C.D.; Shayan, K.; Giclas, P.C.; Peterson, K.S.; Aceves, S.S.; Sheets, R.M.; Peterson, B.M.; Newbury, R.O.; Hoffman, H.M.; Bastian, J.F.
Mutations of complement factor I and potential mechanisms of neuroinflammation in acute hemorrhagic leukoencephalitis
J. Clin. Immunol.
33
162-171
2013
Homo sapiens
brenda
Johnson, J.; Borisevich, V.; Rockx, B.; Parks, G.
A novel factor I activity in Nipah virus inhibits human complement pathways through cleavage of C3b
J. Virol.
89
989-998
2015
Nipah henipavirus
brenda
Malm, S.; Jusko, M.; Eick, S.; Potempa, J.; Riesbeck, K.; Blom, A.M.
Acquisition of complement inhibitor serine protease factor I and its cofactors C4b-binding protein and factor H by Prevotella intermedia
PLoS ONE
7
e34852
2012
Homo sapiens
brenda
Okroj, M.; Holmquist, E.; Nilsson, E.; Anagnostaki, L.; Jirstroem, K.; Blom, A.M.
Local expression of complement factor I in breast cancer cells correlates with poor survival and recurrence
Cancer Immunol. Immunother.
64
467-478
2015
Homo sapiens
brenda
Xiang, J.; Li, X.; Chen, Y.; Lu, Y.; Yu, M.; Chen, X.; Zhang, W.; Zeng, Y.; Sun, L.; Chen, S.; Sha, Z.
Complement factor I from flatfish half-smooth tongue (Cynoglossus semilaevis) exhibited anti-microbial activities
Dev. Comp. Immunol.
53
199-209
2015
Cynoglossus semilaevis (A0A0H4CX09), Cynoglossus semilaevis
brenda
Kumar, J.; Yadav, V.; Phulera, S.; Kamble, A.; Gautam, A.; Panwar, H.; Sahu, A.
Species specificity of vaccinia virus complement control protein for the bovine classical pathway is governed primarily by direct interaction of its acidic residues with factor I
J. Virol.
91
e00668-17
2017
Bos taurus, Homo sapiens
brenda