Detail Information for IndEnz0002015845
IED ID IndEnz0002015845
Enzyme Type ID protease015845
Protein Name Metacaspase-2
EC 3.4.22.-
TbMCA2

Cleaved into: Large subunit p20; Small subunit p10
Gene Name MCA2
Organism Trypanosoma brucei brucei
Taxonomic Lineage cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Trypanozoon Trypanosoma brucei Trypanosoma brucei brucei
Enzyme Sequence MCSLITQLCDAGQLADYVGLGWLNAVSSQPYLVQALGLQPPPRRVDVDAAFRDAEGLHGHQPWVATPLPGRTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKGFKQVPQLSASKAIDLDQTFSLTEMFSVDRSVQ
Enzyme Length 347
Uniprot Accession Number Q8T8E7
Absorption
Active Site ACT_SITE 158; /evidence=ECO:0000250|UniProtKB:Q08601; ACT_SITE 213; /evidence=ECO:0000250|UniProtKB:Q585F3
Activity Regulation ACTIVITY REGULATION: Activated by Ca(2+). In response to calcium binding, the 280-loop, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site. The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme. Proteolytic cleavage is required for catalytic activity towards large protein substrates. {ECO:0000250|UniProtKB:Q585F3}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.22.-
Enzyme Function FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues. {ECO:0000250|UniProtKB:Q585F3}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (3); Metal binding (4); Propeptide (1); Region (1); Site (3)
Keywords Autocatalytic cleavage;Calcium;Endosome;Hydrolase;Metal-binding;Protease;Thiol protease;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Recycling endosome {ECO:0000305|PubMed:16507595}.
Modified Residue
Post Translational Modification PTM: Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates. After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (By similarity). In vivo, the unprocessed enzyme appears to be the predominant form (PubMed:16507595). {ECO:0000250|UniProtKB:Q585F3, ECO:0000269|PubMed:16507595}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 37,794
Kinetics
Metal Binding METAL 173; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 189; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 190; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 220; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3
Rhea ID
Cross Reference Brenda