InterPro : IPR017904

Name  ADF/Cofilin/Destrin Short Name  ADF/Cofilin/Destrin
Type  Family Description  The actin-depolymerising factor homology (ADF-H) domain is an ~150-amino acid motif that is present in three phylogenetically distinct classes of eukaryotic actin-binding proteins [, , ]:ADF/cofilins, which include ADF, cofilin, destrin, actophorin, coactosin, depactin and glia maturation factors (GMFs) beta and gamma. ADF/cofilins are small actin-binding proteins composed of a single ADF-H domain. They bind both actin-monomers and filaments and promote rapid filament turnover in cells by depolymerising/fragmenting actin filaments. ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin monomersTwinfilins, which are actin monomer-binding proteins that are composed of two ADF-H domainsAbp1/Drebrins, which are relatively large proteins composed of an N-terminal ADF-H domain followed by a variable region and a C-terminal SH3 domain. Abp1/Drebrins interact only with actin filaments and do not promote filament depolymerisation or fragmentationAlthough these proteins are biochemically distinct and play different roles in actin dynamics, they all appear to use the ADF-H domain for their interactions with actin.The ADF-H domain consists of a six-stranded mixed beta-sheet in which the four central strands (beta2-beta5) are anti-parallel and the two edge strands (beta1 and beta6) run parallel with the neighbouring strands. The sheet is surrounded by two alpha-helices on each side [, , ].This entry represents a subgroup containing the ADF-H domain and found in ADF proteins, cofilins and destrins.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR027234 Cofilin 1 Cofilin_1 Family
IPR029924 Destrin Dstn Family

0 Contains

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Paavilainen VO Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin. 2002 J Biol Chem 277 43089-95
Liu L Crystal structure of human coactosin-like protein. 2004 J Mol Biol 344 317-23
Lappalainen P The ADF homology (ADF-H) domain: a highly exploited actin-binding module. 1998 Mol Biol Cell 9 1951-9
Liu LX Structure and expression of a novel filarial gene for glia maturation factor. 1997 Gene 186 1-5

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)