The Shroom (Shrm) protein family is found only in animals. Proteins of this family are predicted to be utilized in multiple morphogenic and developmental processes across animal phyla to regulate cells shape or intracellular architecture in an actin and myosin-dependent manner [1]. While the founding member of the Shrm family is Shrm1 (formerly Apx), it appears that this protein is found only in Xenopus [2]. In mice and humans, the Shrm family of proteins consists of:

• Shrm2 (formerly Apxl), a protein involved in the morphogenesis, maintenance, and/or function of vascular endothelial cells.
• Shrm3 (formerly Shroom), a protein necessary for neural tube closure in vertebrate development as defiency in Shrm results in exencephaly and spina bifida. Shrm3 is also conserved in some invertebrates, as orthologs can be found in sea urchin and Ciona.
• Shrm4, a regulator of cytoskeletal architecture that may play an important role in vertebrate development. It is implicated in X-linked mental retardation in humans.

This protein family is based on the conservation of a specific arrangement of an N-terminal PDZ domain (see <PDOC50106>), a centrally positionned sequence motif termed ASD1 (Apx/Shrm Domain 1) and a C-terminally positioned motif termed ASD2 [1,2,3]. Shrm2 and Shrm3 contain all three domains, while Shrm4 contains the PDZ and ASD2 domains, but lacks a discernable ASD1 element. To date, the ASD1 and ASD2 elements have only been found in Shrm-related proteins and do not appear in combination with other conserved domains. ASD1 is required for targeting to actin, while ASD2 is capable of eliciting an actomyosin based constriction event [1,2].

ASD2 is the most highly conserved sequence element shared by Shrm1, Shrm2, Shrm3, and Shrm4. It possesses a well conserved series of leucine residues that exhibit spacing consistent with that of a leucine zipper motif [1].

The profiles we developed cover the entire ASD1 and ASD2 domains.