{PDOC00433}
{PS00500; THYMOSIN_B4}
{BEGIN}
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* Thymosin beta-4 family signature *
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Thymosin beta-4  [1] is a  polypeptide of  43 amino  acid residues which plays
an important  role  in  the  organization of the cytoskeleton. It binds to and
sequesters actin   monomers   (G   actin)   and   therefore   inhibits   actin
polymerization.

The sequence of thymosin beta-4 is extremely  well  conserved  in  mammals and
amphibians.  A number of peptides closely related to thymosin beta-4 are known
to exist:  thymosin beta-9 (and beta-8) in bovine and pig, thymosin beta-10 in
man and rat, thymosin beta-11 and beta-12 in trout and human Nb thymosin beta.

As a  signature  pattern  for this family, we selected  a stretch of 12 highly
conserved residues located  in the central part of the thymosin beta proteins.
This region,    rich    in   charged  residues, lies between two alpha-helical
regions and is involved in the binding of actin.

-Consensus pattern: L-[KR]-K-T-[DENT]-T-x(2)-K-N-[PT]-L.
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2002 / Pattern and text revised.

[ 1] Huff T., Mueller C.S.G., Otto A.M., Netzker R., Hannappel E.
     "beta-Thymosins, small acidic peptides with multiple functions."
     Int. J. Biochem. Cell Biol. 33:205-220(2001).
     PubMed=11311852

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