DESI1

Official Full Name

desumoylating isopeptidase 1

Organism

Homo sapiens

GeneID

27351

Background

Enables importin-alpha family protein binding activity and long-chain fatty acyl-CoA hydrolase activity. Involved in protein export from nucleus and regulation of proteasomal ubiquitin-dependent protein catabolic process. Located in cytosol. Part of protein-containing complex. [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

POST; DESI2; DeSI-1; PPPDE2; FAM152B; D15Wsu75e; DJ347H13.4;

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Detailed Information

Post-translational modifications of small ubiquitin-like modifiers (SUMOs) can be reversed by SENPs, the first known class of de-SUMOylating enzymes. Recently, a new de-SUMOylating enzyme, DeSI-1, has been identified, which differs from SENPs and belongs to the putative deubiquitinating isopeptidase PPPDE superfamily.

Structure of Desi1

Mouse DeSI-1 is almost identical to human DeSI-1, with a sequence identity of 97.0%. DeSI-1 monomer can be characterized as a hybrid α/β-fold composed of six β-strands and six α-helices. The five β-strands (β1-β5) form a highly curved central β-sheet, which is stacked by a pair of antiparallel α-helices (α2 and α3) and surrounded by α1 and α4. The existing crystal structure of human DeSI-1 is not a full-length protein but a truncated protein lacking the 20 residues at the C-terminus. In the structure of the truncated protein, human DeSI-1(1-148) is a homodimer. In the dimeric structure of human DeSI-1(1-148), there is a prominent surface groove between the two subunits, and each of the two opposite sides of the groove contains two residues that are invariant in the PPPDE family of proteins: Cys108 and His38 are located on α3 and β2, respectively.

Function of Desi1

The modification of proteins by ubiquitin and SUMO (ubiquitin-like minor modifiers) is a dynamic and reversible process. Similar to the ubiquitin pathway, in the ubiquitin pathway, deubiquitinating enzymes act to remove ubiquitin from the ubiquitin adduct. The protease family is able to remove SUMO intact from the substrate. To date, only one SUMO-specific protease family has been described: the enkephalin-specific proteases (SENP). A new de-SUMO-chemistry enzyme, which has been named DeSI-1 (de-SUMO-chemistry isopeptidase 1). A new transcriptional repressor, BZEL, serves as a substrate for DeSI-1, which catalyzes the de-SUMOization of BZEL but not its deubiquitination. Furthermore, the SENP substrates PML and ΔNp63 were not de-SUMOylated by DeSI-1, suggesting that SENP and DeSI enzymes recognize different substrates.

References:

Shin EJ, Shin HM, Nam E, et al. DeSUMOylating isopeptidase: a second class of SUMO protease. EMBO Rep. 2012;13(4):339-346. doi:10.1038/embor.2012.3
Suh HY, Kim JH, Woo JS, et al. Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily. Proteins. 2012;80(8):2099-2104. doi:10.1002/prot.24093

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