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
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convertase
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macular
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properdin
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uremic
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cell-bound
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c3d
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fluid-phase
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glomerulonephritis
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complement-mediated
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opsonization
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medicine
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i-mediated
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eculizumab
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alpha\'-chain
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c4-binding
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c4bp
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microangiopathic
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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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Subunits
Subunits on EC 3.4.21.45 - complement factor I
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dimer
heterodimer
additional information
x * 69230, mature protein, calculated from amino acid sequence
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1 * 38000 + 1 * 50000, non-catalytic 50000 Da subunit is disulfide-linked to the 38000 Da catalytic subunit
dimer
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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
heterodimer
composed of two disulfide linked chains, each carrying three N-linked oligosaccharide chains, 25-27% N-glycosylation, 55% disialylated structures for the heavy chain and 62% disialylated structures for the light chain identified, 40% monosialylated structures for the heavy chain and 35% monosialylated structures for light chains identified, A2G2S2 identified as the dominant type of glycan on both chains, biantennary structure with chains terminating in sialic acid linked to galactose, deduced from glycan characterization
CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site. The light chain of trout CFI comprises the serine protease domain, which contains the catalytic triad, His380-Asp429-Ser525 residues, human CFI numbering, as well as the Asp519 residue located at the bottom of the specificity pocket. All these residues are identical by composition and position in all species tested
additional information
-
CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site. The light chain of trout CFI comprises the serine protease domain, which contains the catalytic triad, His380-Asp429-Ser525 residues, human CFI numbering, as well as the Asp519 residue located at the bottom of the specificity pocket. All these residues are identical by composition and position in all species tested