<rdf:RDF
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:ns1="http://metadb.riken.jp/db/SciNetS_rib125i/"
    xmlns:ns5="http://metadb.riken.jp/db/SciNetS_rib124i/"
    xmlns:rdfs="http://www.w3.org/2000/01/rdf-schema#"
    xmlns:ns4="http://creativecommons.org/ns#"
    xmlns:ns3="http://database.riken.jp/sw/item/">
  <ns1:crib125s1i rdf:about="http://metadb.riken.jp/db/SciNetS_rib125i/crib125s1rib125u8397i">
    <ns1:prib125u2i xml:lang="en">The N-terminal predicted helical stretch of the insulin receptortyrosine kinase substrate p53 (IRSp53) is an evolutionaryconserved F-actin bundling domain involved in filopodiumformation. The domain has been named IMD after the IRSp53 andmissing in metastasis (MIM) proteins in which it occurs.Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1and is SH3-independent [1].</ns1:prib125u2i>
    <ns1:prib125u1i xml:lang="en">IRSp53/MIM homology domain</ns1:prib125u1i>
    <ns1:prib125s1i rdf:resource="http://metadb.riken.jp/db/SciNetS_rib124i/crib124s1rib124u13606i"/>
    <ns4:attributionURL rdf:resource="http://pfam.sanger.ac.uk/family?acc=PF08397"/>
    <rdfs:seeAlso rdf:resource="http://database.riken.jp/sw/item/crib125s1rib125u8397i"/>
    <rdfs:label xml:lang="en">IMD</rdfs:label>
  </ns1:crib125s1i>
</rdf:RDF>