The following proteins have been shown to be evolutionary related [1,2,3]:
Epimorphin (or syntaxin 2), a mammalian mesenchymal protein which plays an
essential role in epithelial morphogenesis.
Syntaxin 1A (also known as antigen HPC-1) and syntaxin 1B which are
synaptic proteins which may be involved in docking of synaptic vesicles at
presynaptic active zones.
Syntaxin 3.
Syntaxin 4, which is potentially involved in docking of synaptic vesicles
at presynaptic active zones.
Syntaxin 5, which mediates endoplasmic reticulum to golgi transport.
Syntaxin 6, which is involved in intracellular vesicle trafficking.
Syntaxin 7.
Yeast PEP12 (or VPS6) which is required for the transport of proteases to
the vacuole.
Yeast SED5 which is required for the fusion of transport vesicles with the
Golgi complex.
Yeast SSO1 and SSO2 which are required for vesicle fusion with the plasma
membrane.
Yeast VAM3, which is required for vacuolar assembly.
Arabidopsis thaliana protein KNOLLE which may be involved in cytokinesis.
Caenorhabditis elegans hypothetical proteins F35C8.4, F48F7.2, F55A11.2 and
T01B11.3.
The above proteins share the following characteristics: a size ranging from
30 Kd to 40 Kd; a C-terminal extremity which is highly hydrophobic and is
probably involved in anchoring the protein to the membrane; a central, well
conserved region, which seems to be in a coiled-coil conformation.
The pattern specific for this family is based on the most conserved region of
the coiled coil domain.
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