3.4.21.45: complement factor I

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For detailed information about complement factor I, go to the full flat file.

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

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.45 complement factor I

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Results	in table
24	Activating Compound
30	AA Sequence
17	Application
1	CAS Registry Number
16	Cloned(Commentary)
13	Cofactor
1	Crystallization (Commentary)
357	Disease/ Diagnostics
1	Expression
10	General Information
1	General Stability
39	Inhibitors
20	KM Value [mM]
7	Localization
2	Metals/Ions
61	Molecular Weight [Da]
37	Natural Substrates/ Products (Substrates)
56	Organism
8	PDB ID
5	pH Optimum
1	pH Range
1	pH Stability
1	pI Value
12	Posttranslational Modification
79	Protein Variants
20	Purification (Commentary)
1	Reaction
1	Reaction Type
53	Reference
1	Renatured (Commentary)
74	Source Tissue
9	Specific Activity [micromol/min/mg]
3	Storage Stability
95	Substrates and Products (Substrate)
13	Subunits
53	Synonyms
12	Temperature Optimum [°C]
1	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.4.21.45 - complement factor I

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 2.7 A resolution. The shape of factor I is bilobal, with the heavy and light chains making up the two halves of a brick. The arrangement of the domains in the larger heavy-chain lobe forms a ring structure, with the N-terminal FIMAC domain contacting the C-terminal LDLRA domains. This contact is linked covalently by a disulfide bridge between Cys15 and Cys237. Mapping of disease-associated gene polymorphisms and mutations known to alter cofactor-assisted C3b/C4b cleavage by factor I onto the factor I structure implies allosteric regulation of light-chain activity by contact of the heavy chain. Modeling of the ternary complex of factor I, factor H, and C3b

Homo sapiens

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