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a new protein superfamily tppp-like proteins一个新的蛋白质总科tppp-like蛋白质
A New Protein Superfamily: TPPP-Like Proteins
Ferenc Orosz*
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
Abstract
The introduction of the term ‘Tubulin Polymerization Promoting Protein (TPPP)-like proteins’ is suggested. They constitute a
eukaryotic protein superfamily, characterized by the presence of the p25alpha domain (Pfam05517, IPR008907), and named
after the first identified member, TPPP/p25, exhibiting microtubule stabilizing function. TPPP-like proteins can be grouped
on the basis of two characteristics: the length of their p25alpha domain, which can be long, short, truncated or partial, and
the presence or absence of additional domain(s). TPPPs, in the strict sense, contain no other domains but one long or short
p25alpha one (long- and short-type TPPPs, respectively). Proteins possessing truncated p25alpha domain are first described
in this paper. They evolved from the long-type TPPPs and can be considered as arthropod-specific paralogs of long-type
TPPPs. Phylogenetic analysis shows that the two groups (long-type and truncated TPPPs) split in the common ancestor of
arthropods. Incomplete p25alpha domains can be found in multidomain TPPP-like proteins as well. The various subfamilies
occur with a characteristic phyletic distribution: e. g., animal genomes/proteomes contain almost without exception long-
type TPPPs; the multidomain apicortins occur almost exclusively in apicomplexan parasites. There are no data about the
physiological function of these proteins except two human long-type TPPP paralogs which are involved in developmental
processes of the brain and the musculoskeletal system, respectively. I predict that the superfamily members containing long
or partial p25alpha domain are often intrinsically disordered proteins, while those with short or truncated domain(s) are
structurally ord
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