Ubiquitin carboxyl-terminal hydrolase isozyme L3
Function
Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3'', and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
Sequence Similarities
Belongs to the peptidase C12 family.
Tissue Specificity
Highly expressed in heart, skeletal muscle, and testis.
Cellular localization
- Cytoplasm
Alternative names
Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, Ubiquitin thioesterase L3, UCHL3