{PDOC00297}
{PS51263; ADF_H}
{BEGIN}
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* ADF-H domain profile *
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The actin-depolymerizing  factor homology (ADF-H) domain is an ~150-amino acid
motif that is present in three phylogenetically distinct classes of eukaryotic
actin-binding proteins [1-3]:

 - 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  depolymerizing/fragmenting actin filaments. ADF/cofilins bind
   ADP-actin with  higher  affinity than ATP-actin and inhibit the spontaneous
   nucleotide exchange on actin monomers.
 - Twinfilins.  They  are  actin monomer-binding proteins that are composed of
   two ADF-H domains.
 - Abp1/Drebrins. They are relatively large proteins composed of an N-terminal
   ADF-H domain followed by a variable region and a C-terminal SH3 domain (see
   <PS50002>). Abp1/Drebrins  interact  only  with  actin filaments and do not
   promote filament depolymerization or fragmentation.

Although 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 neighboring strands. The sheet is
surrounded by two alpha-helices on each side (see <PDB:1COF>) [1,2,4].

The profile we developed covers the entire ADF-H domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2006 / Pattern removed, profile added and text revised.

[ 1] Lappalainen P., Kessels M.M., Cope M.J., Drubin D.G.
     "The ADF homology (ADF-H) domain: a highly exploited actin-binding
     module."
     Mol. Biol. Cell 9:1951-1959(1998).
     PubMed=9693358
[ 2] Paavilainen V.O., Merckel M.C., Falck S., Ojala P.J., Pohl E.,
     Wilmanns M., Lappalainen P.
     "Structural conservation between the actin monomer-binding sites of
     twinfilin and actin-depolymerizing factor (ADF)/cofilin."
     J. Biol. Chem. 277:43089-43095(2002).
     PubMed=12207032; DOI=10.1074/jbc.M208225200
[ 3] Liu L.X., Xu H., Weller P.F., Shi A., Debnath I.
     "Structure and expression of a novel filarial gene for glia maturation
     factor."
     Gene 186:1-5(1997).
     PubMed=9047337
[ 4] Liu L., Wei Z., Wang Y., Wan M., Cheng Z., Gong W.
     "Crystal structure of human coactosin-like protein."
     J. Mol. Biol. 344:317-323(2004).
     PubMed=15522287; DOI=10.1016/j.jmb.2004.09.036

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