CAHS proteins are cytosolic heat soluble proteins that seem to contribute to the anhydrobiosis in tardigrades, but their specific mechanisms are yet to be identified (PubMed:28306513, PubMed:33545053). It is possible that protection during anhydrobiosis might occur via the stabilization of vitrifying small molecules such as sugars, but not via the direct glass transition of CAHS proteins themselves (Probable). Expression is highly induced during desiccation (PubMed:28306513). CAHS proteins contain 2 repeats of 19-mer peptides designated as CAHS-motifs that comprise each two octapeptides connected by a tripeptide (PubMed:22937162). Affects slightly survival under dry conditions but does not affect survival under frozen conditions (PubMed:28306513). Trehalose, a disaccharide essential for several organisms to survive drying, is detected at low levels or not at all in some tardigrade species, indicating that tardigrades possess potentially novel mechanisms for surviving desiccation involving tardigrade-specific intrinsically disordered proteins (TDPs) (PubMed:28306513). Belongs to the Cytosolic-abundant heat soluble protein (CAHS) family. It was suggested that CAHS proteins were intrinsically unstructured and show heat-dependent glass transition, which contributes to the vitrification of cells, and this further leads to desiccation tolerance (PubMed:28306513). However, more recent studies led to the conclusion that there was no evidence supporting glass transition of CAHS proteins to be contributing to the glass transition of the whole tardigrade (PubMed:33545053).