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The potent immunomodulatory, anti-inflammatory and procoagulant properties of theprotein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have beenpreviously found to be modulated by a supramolecular monomer-trimer equilibrium.More structural details that integrate experimental data into a predictive frameworkhave recently been reported. Unfortunately, homology modelling and fold-recognitionstrategies were not successful in creating a theoretical model of the structuralorganization of SV-IV. It was inferred that the global structure of SV-IV is not similarto any protein of known three-dimensional structure. Reversing the classical approachto the sequence-structure-function paradigm, in this paper we report on novelinformation obtained by comparing physicochemical parameters of SV-IV with twodatasets made of intrinsically unfolded and ideally globular proteins. In addition, wehave analysed the SV-IV sequence by several publicly available disorder-orientedpredictors. Overall, disorder predictions and a re-examination of existing experimentaldata strongly suggest that SV-IV needs large plasticity to efficiently interact with thedifferent targets that characterize its multifaceted biological function and should betherefore better classified as an intrinsically disordered protein.

Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle