{PDOC50192}
{PS50192; T_SNARE}
{BEGIN}
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* t-SNARE coiled-coil homology domain profile *
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The process  of  vesicular  membrane  fusion  in eukaryotic cells depends on a
conserved fusion  machinery  called  SNARE (soluble N-ethylmaleimide-sensitive
factor (NSF)  attachment  protein (SNAP) receptors). In the process of vesicle
docking, proteins  present  on  the  vesicle  (v-SNARE)  have to bind to their
counterpart  on the target membrane (t-SNARE)  to form a core complex that can
then recruit  the soluble proteins NSF and SNAP. This so called fusion complex
can then  disassemble  after  ATP  hydrolysis  mediated by the ATPase NSF in a
process that leads to membrane fusion and the release of the vesicle contents.
t-SNAREs consist  of  two different families of proteins: the type II integral
membrane proteins  syntaxins and SNAP-25 (synaptosome-associated protein of 25
kDa), which is anchored in the plasma membrane by attached lipids and does not
span the membrane [1].

The N- and C-terminal coiled-coil domains of members of the SNAP-25 family and
the most  C-terminal  coiled-coil domain of the syntaxin family are related to
each other  and  form  a  new homology domain of approximately 60 amino acids.
This domain  is  also  found  in  other  known  proteins involved in vesicular
membrane traffic, some of which belong to different protein families [1]:

 - Yeast SFT1, UFE1, BET1, VAM7 and YDR468c proteins.
 - Mammalian TSL-4 proteins.

The profile  we  developed  covers  the  entire  t-SNARE  coiled-coil homology
domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2002 / First entry.

[ 1] Weimbs T., Low S.H., Chapin S.J., Mostov K.E., Bucher P., Hofmann K.
     "A conserved domain is present in different families of vesicular
     fusion proteins: a new superfamily."
     Proc. Natl. Acad. Sci. U.S.A. 94:3046-3051(1997).
     PubMed=9096343

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