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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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.45 - complement factor I
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glycoprotein
proteolytic modification
CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site
side-chain modification
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the first GlcNAc residue of each of the six N-linked glycosylation sites is ordered and visible in the electron density, crystallization data
glycoprotein
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factor I is a multidomain acute phase glycoprotein, that is N-glycosylated at six positions (25-27%, w/w) with heavily sialylated biantennary glycans. Three-dimensional overview of the glycosylation sites. Deglycosylation by endoglycosidases, profile overview
glycoprotein
sequence contains three potential N-glycosylation sites
glycoprotein
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N-glycosylation sites are Asn-73, 421, 493 and 535, and a O-glycosylation sites is Thr-36. Has little species-specificity like human 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
side-chain modification
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carbohydrate content is at least 10.7% w/w, not including neuraminic acid, with 7.2% hexose and 3.2% glucosamine
side-chain modification
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most of the six potential N-glycosylation acceptance sites are utilized in the mouse protein