page_title: Cordon-bleu protein
section_title: Structure
hierarchical_section_title: Cordon-bleu protein / Structure
caption_attribution_description: English: Structure of Cordon-bleu protein with characteristic domains.
context_page_description: Protein cordon-bleu is a protein that in humans is encoded by the COBL gene.
  The Cordon-bleu protein was first described in 2007 Cobl was demonstrated to be a brain-enriched, Wiskott-Aldrich Homology 2 WH2 domain-based actin nucleator playing a pivotal role in morphogenetic processes in the vertebrate central nervous system that give rise to the complex dendritic arbor of neuronal cells
  The Cobl gene was originally identified in lacZ-gene-trap experiments in mice. Cobl mRNA was detected as early as at day 7.5 post-coitum in the gastrula organizer and extended towards the axial midline at E8. The organizer is a small group of embryonal cells that organizes the entire body plan because it gives rise to the axial midline – an important source of patterning and morphogenesis cues.
  The human COBL gene encodes a 1261-amino acid protein with a mass of about 136 kDa. The mouse protein is 1337 amino acids long. The cobl gene in mice and human gives rise to a variety of putative splice variants, which, however, have not yet been analyzed at the protein level. Cobl genes seem to be restricted to vertebrates.
context_section_description: An important functional part of this actin-nucleating protein is the C-terminus, which contains 3 Wiskott-Aldrich syndrome protein (WASp) homology 2 (WH2) domains. WH2 domains are able to associate with actin monomers to funnel them into actin filament formation processes. Cobl in humans contains three WH2 domains located at the C-terminus (the first WH2 domain, WH2.1, lies between 1109 and 1129, WH2.2 between  1149 and 1169 and WH2.3 between 1237 and 1257), that are responsible for forming an "actin nucleus" composed of 3 actin monomers from which an actin filament can be further elongated. The cobl-actin-nucleus is thought to remain at the pointed end of the emerging filament leaving the barbed end free for rapid polymerization. 
  Other critical functional parts are the N-terminal Cobl Homology domain, which can also be found in the ancestor of Cobl, Cobl-like - a protein that is also expressed highly in the nervous system and able to give rise to actin filaments by a mechanism different to Cobl, yet, using in part similar associated components and molecular mechanisms. Cobl Homology domains contain three motifs following the consensus KrRAPpPP (first described as "KRAP" motif of unknown function by Caroll et al., 2003), which represent syndapin I binding sites
  The polypeptide also contains several further proline-rich sequences, which e.g. bind the SH3 domain of Abp1 and PRMT2. Also binding sites for profilin-actin heterodimers have been suggested, selected Ser residues are phosphorylated and two Arginines in the second WH2 domain, which is considered the pace maker of the actin nucleation process were detected to be methylated.
  In humans there are 5 isoforms of Cobl generated though alternative splicing.
caption: Motifs and domains in Cordon-bleu protein.
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