Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP) family members 2 and 3; WASF2 (WAS protein family, member 2), This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) members 2 (WIPF2; also known as WIRE/WICH) and 3 (WIPF3). WIPF2 may be an important regulator of the actin cytoskeleton. It binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. Pathogenic properties of Shigella flexneri, a causative agent of intestinal infections worldwide, rely on its ability to invade the human colon where it spreads from cell to cell; WIPF2 has been shown to promote this via its contribution to the efficiency of actin-based motility in the cytosol and the resolution of the membrane protrusions into vacuoles. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1207110578  32 EAKGRGALLSDICKGAKLKKTTGVNDRSAP 61
Cdd:cd22077     1 EQKGRNALLADIQKGARLKKVTQINDRSAP 30

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP) family members 2 and 3; WASF2 (WAS protein family, member 2), This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) members 2 (WIPF2; also known as WIRE/WICH) and 3 (WIPF3). WIPF2 may be an important regulator of the actin cytoskeleton. It binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. Pathogenic properties of Shigella flexneri, a causative agent of intestinal infections worldwide, rely on its ability to invade the human colon where it spreads from cell to cell; WIPF2 has been shown to promote this via its contribution to the efficiency of actin-based motility in the cytosol and the resolution of the membrane protrusions into vacuoles. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1207110578  32 EAKGRGALLSDICKGAKLKKTTGVNDRSAP 61
Cdd:cd22077     1 EQKGRNALLADIQKGARLKKVTQINDRSAP 30

Wiskott Aldrich syndrome homology region 2; Wiskott Aldrich syndrome homology region 2 / actin-binding motif

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gi 1207110578   35 GRGALLSDICKGAKLKKT 52
Cdd:smart00246   1 ARSALLAQIRQGKKLKKV 18

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP) family members 2 and 3; WASF2 (WAS protein family, member 2), This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP) members 2 (WIPF2; also known as WIRE/WICH) and 3 (WIPF3). WIPF2 may be an important regulator of the actin cytoskeleton. It binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. Pathogenic properties of Shigella flexneri, a causative agent of intestinal infections worldwide, rely on its ability to invade the human colon where it spreads from cell to cell; WIPF2 has been shown to promote this via its contribution to the efficiency of actin-based motility in the cytosol and the resolution of the membrane protrusions into vacuoles. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1207110578  32 EAKGRGALLSDICKGAKLKKTTGVNDRSAP 61
Cdd:cd22077     1 EQKGRNALLADIQKGARLKKVTQINDRSAP 30

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP). Human WIP protein is proline rich and has high sequence similarity to yeast protein verprolin (included in this model). WIP forms complexes with WASP/N-WASP and modulates their function in vivo. It is involved in the regulation of endocytosis and participates in several cellular processes, some of which are relevant in cancer and may be dependent on different oncogenic stimuli. WIP interacts directly with mammalian actin-binding protein-1 (mABP1) via the SH3 domain during platelet-derived growth factor (PDGF)-mediated dorsal ruffle formation. WIP family includes members 1 (WAS/WASL-interacting protein family member 1) or WIPF1), 2 (WIPF2) and 3 (WIPF3). Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival. WIPF2 may be an important regulator of the actin cytoskeleton. WIPF2 binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta. In yeast, verprolin is involved in cytoskeletal organization and cellular growth. It may exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins, such as profilin, or via proteins possessing SH3 domains.

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                  ....*....|....*....|....*....|
gi 1207110578  32 EAKGRGALLSDICKGAKLKKTTgVNDRSAP 61
Cdd:cd22064     1 EQKGRGALLGDIRKGMKLKKTV-TNDRSAP 29

Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif), and similar proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) as well as thymosin-beta (Tbeta; also called beta-thymosin or betaT) domains that are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. These WH2/betaT peptides are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions; the betaT shares a more extended and conserved C-terminal half than WH2. These single or repeated domains are found in actin-binding proteins (ABPs) such as the hematopoietic-specific protein WASP, its ubiquitously expressed ortholog neural-WASP (N-WASP), WASP-interacting protein (WAS/WASL-interacting protein family members 1 and 2), and WASP-family verprolin homologous protein (WAVE/SCAR) isoforms: WAVE1, WAVE2, and WAVE3. Also included are the WH2 domains found in inverted formin FH2 domain-containing protein (INF2), Cordon bleu (Cobl) protein, vasodilator-stimulated phosphoprotein (VASP) homology protein and actobindin (found in amoebae). These ABPs are commonly multidomain proteins that contain signaling domains and structurally conserved actin-binding motifs, the most important being the WH2 domain motif through which they bind actin in order to direct the location, rate, and timing for actin assembly in the cell into different structures, such as filopodia, lamellipodia, stress fibers, and focal adhesions. The WH2 domain motif is one of the most abundant actin-binding motifs in Wiskott-Aldrich syndrome proteins (WASPs) where they activate Arp2/3-dependent actin nucleation and branching in response to signals mediated by Rho-family GTPases. The thymosin beta (Tbeta) domains in metazoans act in cells as major actin-sequestering peptides; their complex with monomeric ATP-actin (G-ATP-actin) cannot polymerize at either filament (F-actin) end.

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gi 1207110578  35 GRGALLSDICKGAKLKKTT 53
Cdd:cd21762     4 DRSALLSDIRKGKKLKKTV 22