title: Nuclear import sequence identification in hOAS3 protein.
abstract: OBJECTIVE
  The OAS proteins are characterized by their capacity to synthesize 2',5'-linked phosphodiester bonds to polymerize ATP into oligomers of adenosine. OAS3, belonging to OASs gene family, synthesizes dimeric 2-5A that binds to RNase L with low affinity and produces 2-5A oligomers shorter than the tri-tetramer 2-5As produced by other family members.
  
  
  METHODS
  For these studies, we used the open source tools cNLS Mapper, PredictProtein and COMPARTMENTS for the nuclear localization signal prediction, UCSF Chimera for molecular graphics and analyses, The Human Protein Atlas to confirm with the IF the OAS3 cell localization and Ensembl Variation Table to identify the presence of putative single nucleotide polymorphisms in the NLS sequence identification.
  
  
  RESULTS
  The analysis of OAS3 protein sequence (NP_006178.2) displayed a putative nuclear localization signal (cNLS Mapper score 8 and PP 100 %), identified by 11 and 5 amino acids (LQRQL KRPRP V) located in the outer portion ready to interact with the importin α/β. Furthermore, we showed that in all cells lines available in the Human Protein Atlas subcell section, the OAS3 was mainly localized in the cytoplasm and nucleus, but not in the nucleoli. We identify six known variant SNPs mapping in the nuclear import sequence, but only three were associated with a missense variation (rs781335794, rs750458641, rs550465943) and were able to strongly reduce the cNLS score.
  
  
  CONCLUSIONS
  The catalytically inactive domain of human OAS3 has a potential nuclear import function, susceptible to SNPs, which could determine their roles in the viral infection and IFNs response.
authors.affiliation: Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
authors.forename: Lucia
authors.initials: L
authors.lastname: Malaguarnera
authors.affiliation: Department of Clinical and Molecular Biomedicine, Division of Infectious Diseases at the University of Catania, Catania, Italy.
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Nunnari
authors.affiliation: Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy. mdirosa@unict.it.|Department of Clinical and Molecular Biomedicine, Division of Infectious Diseases at the University of Catania, Catania, Italy. mdirosa@unict.it.
authors.forename: Michelino
authors.identifier: http://orcid.org/0000-0002-1837-9325
authors.initials: M
authors.lastname: Di Rosa
mesh_terms: D015088:2',5'-Oligoadenylate Synthetase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D019913:Nuclear Localization Signals; D020641:Polymorphism, Single Nucleotide; D000072417:Protein Domains / Q000235:genetics*; D020539:Sequence Analysis, Protein
chemical_list: D019913:Nuclear Localization Signals; D015088:2',5'-Oligoadenylate Synthetase; C577439:OAS3 protein, human
keywords: NLS; Nuclear localization signals; OAS3; SNP; UCSF Chimera; cNLS Mapper