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PROSITE documentation PDOC50192 [for PROSITE entry PS50192]

t-SNARE coiled-coil homology domain profile


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.

Last update:

April 2002 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

T_SNARE, PS50192; t-SNARE coiled-coil homology domain profile  (MATRIX)


1AuthorsWeimbs T. Low S.H. Chapin S.J. Mostov K.E. Bucher P. Hofmann K.
TitleA conserved domain is present in different families of vesicular fusion proteins: a new superfamily.
SourceProc. Natl. Acad. Sci. U.S.A. 94:3046-3051(1997).
PubMed ID9096343

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