{PDOC51306}
{PS51306; ASD1}
{PS51307; ASD2}
{BEGIN}
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* ASD1 and ASD2 domains profiles *
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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  [1-3].  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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2007 / First entry.

[ 1] Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.
     "Differential actin-dependent localization modulates the
     evolutionarily conserved activity of Shroom family proteins."
     J. Biol. Chem. 281:20542-20554(2006).
     PubMed=16684770; DOI=10.1074/jbc.M512463200
[ 2] Yoder M., Hildebrand J.D.
     "Shroom4 (Kiaa1202) is an actin-associated protein implicated in
     cytoskeletal organization."
     Cell Motil. Cytoskeleton 64:49-63(2007).
     PubMed=17009331; DOI=10.1002/cm.20167
[ 3] Hildebrand J.D., Soriano P.
     "Shroom, a PDZ domain-containing actin-binding protein, is required
     for neural tube morphogenesis in mice."
     Cell 99:485-497(1999).
     PubMed=10589677

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{END}