|Protein Name||Cofilin -1|
|Ref Sequence Id||NP_001015655.1|
|Amino Acid Lenth||166|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Protein Function||Regulates actin cytoskeleton dynamics; Important for normal progress through mitosis and normal cytokinesis; Plays a role in the regulation of cell morphology and cytoskeletal organization; required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation; Required for neural tube morphogenesis and neural crest cell migration|
|Biochemical Properties||Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity; presence of special ADF-H domain in its structure; The ADF-H domains can directly or indirectly interact with actin cytoskeleton and provide its remodeling ; interacts with HSPH1 and LIMK1. ; binds and severs F-actin in a pH dependent manner; below pH 7.0 cofilin binds to F-actin in a 1:1 molar ratio of cofilin to actin monomer in the filament; above pH 7.0 cofilin will sever actin filaments and bind actin monomer in a 1:1 molar ratio.|
|Significance in milk||Upregulated in intramammary infection during S. uberis challenge|
|PTMs||Cofilin oxidation leads to formation of intramolecular disulfide bonds and to dephosphorylation at Ser3 ; phosphorylation at Ser3 for role in actin filament dynamics|
|Significance of PTMs||cofilin requires dephosphorylation of an N-terminal serine and deprotonation of a C-terminal histidine for increased activity|
|Bibliography||1. Mudaliar, M., Tassi, R., Thomas, F. C., McNeilly, T. N., Weidt, S. K., McLaughlin, M., … Zadoks, R. N. (2016). Mastitomics, the integrated omics of bovine milk in an experimental model of Streptococcus uberis mastitis: 2. Label-free relative quantitative proteomics. Molecular BioSystems, 12(9), 2748–2761. https://doi.org/10.1039/c6mb00290k. |
2. Klemke, M., Wabnitz, G. H., Funke, F., Funk, B., Kirchgessner, H., & Samstag, Y. (2008). Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions. Immunity, 29(3), 404–413. https://doi.org/10.1016/j.immuni.2008.06.016.
3. Klamt, F., Zdanov, S., Levine, R. L., Pariser, A., Zhang, Y., Zhang, B., … Shacter, E. (2009). Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nature Cell Biology, 11(10), 1241–1246. https://doi.org/10.1038/ncb1968.