Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar proteins; This family contains beta-thymosin (betaT; also called thymosin beta or Tbeta) domain which is similar to the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2). Proteins in the beta-thymosin family are small peptides that act as actin monomer (G-actin) sequestering factors. They bind to G-actin into a 1:1 complex, rendering G-actin resistant to polymerization into filaments (F-actin). Thymosin beta 4 (Tbeta4 or TB4) and beta10 (Tbeta10) are minor variants of betaT that bind skeletal muscle actin and inhibit actin polymerization. Thymosin beta4 can also bind to polymerized F-actin. The roles of beta-thymosins also appear to extend beyond G-actin sequestration. Thymosin beta4 has also been linked to a number of additional biological events, including angiogenesis, wound healing, inflammation, and intracellular signaling through kinase activation. Research on thymosin beta10 in breast cancer cells has suggested a relationship with actin cytoskeletal remodeling and cell motility. In addition, thymosins beta4, beta10, and beta15 are highly expressed in several tumor cells, and these have been associated with a higher metastatic potential, possibly due to their function in cell proliferation.

                         10        20        30
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gi 1174821524  3 DKPDLSEVEKFDRSKLKKTNTEEKNTLPSKE 33
Cdd:cd22059    1 AENLKSQLEGFDKSKLKKTETQEKNPLPSKE 31

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in beta-Thymosin, and similar proteins; This family contains beta-thymosin (betaT; also called thymosin beta or Tbeta) domain which is similar to the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2). Proteins in the beta-thymosin family are small peptides that act as actin monomer (G-actin) sequestering factors. They bind to G-actin into a 1:1 complex, rendering G-actin resistant to polymerization into filaments (F-actin). Thymosin beta 4 (Tbeta4 or TB4) and beta10 (Tbeta10) are minor variants of betaT that bind skeletal muscle actin and inhibit actin polymerization. Thymosin beta4 can also bind to polymerized F-actin. The roles of beta-thymosins also appear to extend beyond G-actin sequestration. Thymosin beta4 has also been linked to a number of additional biological events, including angiogenesis, wound healing, inflammation, and intracellular signaling through kinase activation. Research on thymosin beta10 in breast cancer cells has suggested a relationship with actin cytoskeletal remodeling and cell motility. In addition, thymosins beta4, beta10, and beta15 are highly expressed in several tumor cells, and these have been associated with a higher metastatic potential, possibly due to their function in cell proliferation.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 1174821524  3 DKPDLSEVEKFDRSKLKKTNTEEKNTLPSKE 33
Cdd:cd22059    1 AENLKSQLEGFDKSKLKKTETQEKNPLPSKE 31