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    <!-- http://purl.obolibrary.org/obo/RO_0002233 -->

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    <!-- http://purl.obolibrary.org/obo/RO_0002234 -->

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    <!-- 
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    <!-- http://purl.obolibrary.org/obo/HINO_0006577 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0006577">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Complement factor I</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0006585 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0006585">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">iC3b</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0006587 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0006587">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Complement factor I:Cell surface:FH,FHR3:C3b</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0006719 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0006719">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">FH, FHR-3</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0008634 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0008634">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Factor I inactivates Factor H-boundC3b</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/INO_0000040"/>
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        </rdfs:subClassOf>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Jupe, S, 2010-10-26</rdfs:comment>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">EC Number: 3.4.21</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Jupe, S, 2010-11-01</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Following the displacement of Bb from C3bBb, Factor I cleaves Factor H-bound C3b producing iC3b, which remains bound to the membrane. The majority of the C3b alpha chain is retained as two fragments which are tethered to the beta chain by disulphide bonds. iC3b is proteolytically inactive and cannot contribute to the complement cascade process, though it still contributes to opsonization.</rdfs:comment>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed3848661</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed6219696</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 43977371</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ReactomeREACT_118841</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Bradley, DT, 2012-02-13</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Fraczek, LA, 2012-02-13</rdfs:comment>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/INO_0000040 -->

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    <!-- http://purl.obolibrary.org/obo/UniProt_P01024 -->

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