Cofilin-1

Basic Information
Short Name	Cofilin-1, p18
UNP ID	P23528
Organism	Homo sapiens
Cys Site	Cys139
Family/Domain	Cofilin/tropomyosin-type actin-binding protein, Actin-binding proteins ADF family
Known Ligand	Ligand list
Function Type	Structural protein

Summary

Protein Function

Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.
One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration.

Cys Function & Property

Molecules covalent bind with Cys139 would disrupt the interface between Cofilin1 and actin.

• Hydrophobic property:

• SASA：

Cys139: 36.275 A^2

Protein Sequence

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
EKLGGSAVIS LEGKPL

Structural Information

• Known structures with covalent ligands:
  

Unknown

• Protein structure:

Related Pathway

• Axon guidance
  
• Fc gamma R-mediated phagocytosis
  
• Regulation of actin cytoskeleton
  
• Pertussis
  
• Human immunodeficiency virus 1 infection
  

Experimental Evidence

Mass Spectrometry, Tryptic Digest

Reference

1. Gabrielsen M, Schuldt M, Munro J, et al. Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target[J]. Cell Communication and Signaling, 2013, 11(1): 58. 23945128