Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown. The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form. [PIN+], also known as [RNQ+], is the prion form of RNQ1 (PubMed:10678178). [PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils (PubMed:17097676). [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (PubMed:10678178). Present with 1140 molecules/cell in log phase SD medium.