Detail Information for IndEnz0002004120
IED ID IndEnz0002004120
Enzyme Type ID protease004120
Protein Name Serine protease HTRA2, mitochondrial
EC 3.4.21.108
High temperature requirement protein A2
Gene Name HtrA2 GM25850
Organism Drosophila sechellia (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila sechellia (Fruit fly)
Enzyme Sequence MALRGSHRLEVIFKRCIASPVLHSQAGNRRSSQLAIKGVDPNSNGNSGQYQQNGEHKEKGWRRLVRFFVPFSLGAAVSAAIIQREDLTPTIAASKMTGRRRDFNFIADVVAGCADSVVYIEIKDTRHFDYFSGQPITASNGSGFIIEQNGLILTNAHVVINKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVNNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRASQELGLRNRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTAGISFAIPIDYVKVFLERAAEKRKKGSAYKTGYPVKRYMGITMLTLTPDILFELKSRSQNMPSNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKTLDIVILRGVKQMHVTITPEDP
Enzyme Length 422
Uniprot Accession Number B4HEM8
Absorption
Active Site ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O43464; ACT_SITE 189; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O43464; ACT_SITE 266; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9VFJ3
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.; EC=3.4.21.108;
DNA Binding
EC Number 3.4.21.108
Enzyme Function FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Can antagonize antiapoptotic activity of th by directly inducing the degradation of th (By similarity). {ECO:0000250|UniProtKB:Q9VFJ3}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (1); Domain (1); Motif (2); Propeptide (1); Region (2); Transit peptide (1); Transmembrane (1)
Keywords Apoptosis;Hydrolase;Membrane;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q9VFJ3}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9VFJ3}; Single-pass membrane protein {ECO:0000255}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment. The extramitochondrial protein does not diffuse throughout the cytosol but stays near the mitochondria. {ECO:0000250|UniProtKB:Q9VFJ3}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 75..78; /note=IAP-binding; /evidence=ECO:0000255; MOTIF 94..97; /note=IAP-binding; /evidence=ECO:0000255
Gene Encoded By
Mass 45,927
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda