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. 2018 May 28;9:1180. doi: 10.3389/fimmu.2018.01180

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Copyright © 2018 Caneparo, Landolfo, Gariglio and De Andrea.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Domain organization of the IFN-inducible protein 16 (IFI16). From the N- to the C-terminal (left to right), IFI16 comprises a pyrin domain (PYD) involved in protein–protein interactions, a linker region containing four nuclear localization signal motifs (NLS) and two hematopoietic interferon-inducible nuclear protein with 200-amino-acid repeats (HIN200) domains, which is an hallmark of the absent in melanoma 2-like receptors/PYHIN proteins. The HIN200 domains include two tandem b-barrels, known as oligonucleotide–oligosaccharide-binding (OB) fold, which allow DNA docking in a non-sequence-specific manner. They are separated by serine/threonine/proline-rich (S/T/P) repeats, which are regulated by alternative mRNA splicing. The numbers represent the amino acid positions based on NCBI Reference Sequence NP_005522.2.