A variety of extracellular proteins from eukaryotes have been found to be
evolutionary related. They have been termed cysteine-rich secretory proteins
(CRISP). Some relevant members of this family are:
Rodent sperm-coating glycoprotein (SCP), also known as acidic epididymal
glycoprotein (AEG) . This protein is thought to be involved in sperm
maturation . It is a protein of about 220 residues and probably contains
eight disulfide bonds.
Mammalian testis-specific protein Tpx-1 . Tpx-1 is highly related to
Mammalian glioma pathogenesis-related protein (GliPR).
Lizard helothermine, a toxin that blocks ryanodine receptors.
Venom allergen 5 (Ag5) from vespid wasps and venom allergen 3 (Ag3) from
fire ants. These proteins are potent allergens and are the main cause of
allergic reactions to stings from insects of the hymenoptera family .
Ag5/3 are proteins of about 200 residues and contain four disulfide bonds.
Plant pathogenesis proteins of the PR-1 family . These proteins are
synthesized during pathogen infection or other stress-related responses.
They are proteins of about 130 to 140 residues and probably contain three
Proteins Sc7 and Sc14 from the basidomycete fungus Schizophyllum commune.
These extracellular proteins are loosely associated with fruit body hyphal
walls . Sc7/14 are proteins of about 180 residues and probably contain
two disulfide bonds.
Ancylostoma secreted protein from dog hookworm.
Yeast hypothetical proteins YJL078c, YJL079c and YKR013w.
The exact function of these proteins is not yet known. As signature patterns,
we selected two conserved regions located in their C-terminal half. The second
signature contains a cysteine which is known to be involved in a disulfide
bond in Ag5.
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