{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McCartney CE"],"funding":["Government of Canada Canadian Institutes of Health Research","CIHR"],"pagination":["17716-17730"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6240860"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(46)"],"pubmed_abstract":["Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit-containing calpain-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain. It also has two unique insertion sequences (ISs) not found in the other calpains: IS1 within calpain-3's protease core and IS2 just prior to the penta-EF-hand domain. Production of either native or recombinant full-length calpain-3 to characterize the function of these ISs is challenging. Therefore, here we used recombinant rat calpain-2 as a stable surrogate and inserted IS1 into its equivalent position in the protease core. As it does in calpain-3, "],"journal":["The Journal of biological chemistry"],"pubmed_title":["Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide."],"pmcid":["PMC6240860"],"funding_grant_id":["MOP74681","MOP 74681"],"pubmed_authors":["Davies PL","Campbell RL","Ye Q","McCartney CE"],"additional_accession":[]},"is_claimable":false,"name":"Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.","description":"Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit-containing calpain-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain. It also has two unique insertion sequences (ISs) not found in the other calpains: IS1 within calpain-3's protease core and IS2 just prior to the penta-EF-hand domain. Production of either native or recombinant full-length calpain-3 to characterize the function of these ISs is challenging. Therefore, here we used recombinant rat calpain-2 as a stable surrogate and inserted IS1 into its equivalent position in the protease core. As it does in calpain-3, ","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Nov","modification":"2026-04-29T03:32:05.161Z","creation":"2021-02-20T04:41:18Z"},"accession":"S-EPMC6240860","cross_references":{"pubmed":["30254072"],"doi":["10.1074/jbc.ra118.004803","10.1074/jbc.RA118.004803"]}}