Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle.
The potent immunomodulatory, anti-inflammatory and procoagulant properties of protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have previously been found to be modulated by a supramolecular monomer-trimer equilibrium. More structural details that integrate experimental data into a predictive framework have recently been reported. Unfortunately, homology modelling and fold-recognition strategies were not successful in creating a theoretical model of the structural organization of SV-IV. It was inferred that the global structure of SV-IV is not similar to that of any protein of known three-dimensional structure. Reversing the classical approach to the sequence-structure-function paradigm, in this paper we report novel information obtained by comparing the physicochemical parameters of SV-IV with two datasets composed of intrinsically unfolded and ideally globular proteins. In addition, we analyse the SV-IV sequence by several publicly available disorder-oriented predictors. Overall, disorder predictions and a re-examination of existing experimental data strongly suggest that SV-IV needs large plasticity to efficiently interact with the different targets that characterize its multifaceted biological function, and should therefore be better classified as an intrinsically disordered protein.
Vilasi
Silvia
S
Dipartimento di Biochimica e Biofisica, Naples, Italy.
Ragone
Raffaele
R
D000595:Amino Acid Sequence; D000728:Androgens / Q000378:metabolism*; D000818:Animals; D019295:Computational Biology; D030562:Databases, Protein; D008297:Male; D008969:Molecular Sequence Data; D051381:Rats; D029607:Seminal Vesicle Secretory Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020539:Sequence Analysis, Protein
D000728:Androgens; D029607:Seminal Vesicle Secretory Proteins; C101178:Svs4 protein, rat