Ha, Byung Hak Kim, Kyung Hee Yoo, Hee Min Lee, Weontae Kim, Eunice EunKyeong 2024-01-20T03:33:38Z 2024-01-20T03:33:38Z 2021-09-04 2016-08-05 0006-291X https://pubs.kist.re.kr/handle/201004/123795 Ubiquitin-fold modifier 1 (Ufm1) specific protease (UfSP) is a novel cysteine protease that activates Ufm1 from its precursor by processing the C-terminus to expose the conserved Gly necessary for substrate conjugation and de-conjugates Ufm1 from the substrate. There are two forms: UfSP1 and UfSP2, the later with an additional domain at the N-terminus. Ufm1 and both the conjugating and deconjugating enzymes are highly conserved. However, in Caenorhabditis elegans there is one UfSP which has extra 136 residues at the N terminus compared to UfSP2. The crystal structure of cUfSP reveals that these additional residues display a MPN fold while the rest of the structure mimics that of UfSP2. The MPN domain does not have the metalloprotease activity found in some MPN-domain containing protein, rather it is required for the recognition and deufmylation of the substrate of cUfSP, U1BP1. In addition, the MPN domain is also required for localization to the endoplasmic reticulum. (C) 2016 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE STRUCTURAL BASIS UFM1 The MPN domain of Caenorhabditis elegans UfSP modulates both substrate recognition and deufmylation activity Article 10.1016/j.bbrc.2016.05.143 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.476, no.4, pp.450 - 456 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 476 4 450 456 scie scopus 000379886500042 2-s2.0-84971667887 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article STRUCTURAL BASIS UFM1 UfSP Ufm1 MPN domain Deufmylation Crystal structure