{PDOC51070}
{PS51070; SHD}
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* Stonin homology domain (SHD) profile *
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Human stonins,  like  their  Drosophila  homologue stoned B are supposed to be
endocytotic proteins  involved  in  clathrin-mediated endocytosis at synapses.
The two   human   stonins,  as  well  as  their  Drosophila  melanogaster  and
Caenorhabditis elegans  homologues,  exhibit a modular structure consisting of
an N-terminal  proline-  and  serine-rich  domain,  a  central stonin homology
domain (SHD),  and a C-terminal domain homologous to the signal-binding domain
of the mu subunits of adaptor protein (AP) complexes (mu-homology domain) (see
<PDOC51072>). The  ~140 amino-acid SHD domain  has not been described in other
proteins and  may thus be unique to members of the stonin family. Its function
is not yet known [1,2].

The profile we developed covers the entire SHD domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2005 / First entry.

[ 1] Martina J.A., Bonangelino C.J., Aguilar R.C., Bonifacino J.S.
     "Stonin 2: an adaptor-like protein that interacts with components of
     the endocytic machinery."
     J. Cell Biol. 153:1111-1120(2001).
     PubMed=11381094
[ 2] Walther K., Diril M.K., Jung N., Haucke V.
     "Functional dissection of the interactions of stonin 2 with the
     adaptor complex AP-2 and synaptotagmin."
     Proc. Natl. Acad. Sci. U.S.A. 101:964-969(2004).
     PubMed=14726597; DOI=10.1073/pnas.0307862100

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