| IED ID | IndEnz0002006291 |
| Enzyme Type ID | protease006291 |
| Protein Name |
Serine protease HTRA2, mitochondrial EC 3.4.21.108 High temperature requirement protein A2 DmHtrA2 HtrA2 Omi stress-regulated endoprotease dOmi Cleaved into: Serine protease HTRA2, mitochondrial, long; Serine protease HTRA2, mitochondrial, short |
| Gene Name | HtrA2 Omi/HtrA2 CG8464 |
| Organism | Drosophila melanogaster (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 melanogaster (Fruit fly) |
| Enzyme Sequence | MALRGSHRLEVIFKRCIASPVLHSHAANRRSSQLAIKEGDPNSNGNSGQYQQNGEQKEKGWRRLVRFFVPFSLGAVVSAAIIQREDLTPTIAASKMTGRRRDFNFIADVVAGCADSVVYIEIKDTRHFDYFSGQPITASNGSGFIIEQNGLILTNAHVVINKPHTMVQVRLSDGRTFPATIEDVDQTSDLATLRIQVNNLSVMRLGKSSTLRSGEWVVALGSPLALSNTVTAGVISSTQRASQELGLRNRDINYLQTDAAITFGNSGGPLVNLDGEAIGVNSMKVTAGISFAIPIDYVKVFLERAAEKRKKGSAYKTGYPVKRYMGITMLTLTPDILFELKSRSQNMPSNLTHGVLVWKVIVGSPAHSGGLQPGDIVTHINKKEIKNSSDVYDALADNSKTLDIVILRGVKQMHVTITPEDP |
| Enzyme Length | 422 |
| Uniprot Accession Number | Q9VFJ3 |
| 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:0000269|PubMed:18259196 |
| 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. {ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:17557079, ECO:0000269|PubMed:18259196}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Domain (1); Motif (2); Mutagenesis (6); Propeptide (1); Region (2); Transit peptide (1); Transmembrane (1) |
| Keywords | Apoptosis;Direct protein sequencing;Hydrolase;Membrane;Mitochondrion;Protease;Reference proteome;Serine protease;Transit peptide;Transmembrane;Transmembrane helix;Ubl conjugation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:18259196}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18259196}; Single-pass membrane protein {ECO:0000255}. Note=Predominantly present in the intermembrane space (PubMed:17397804, PubMed:18259196). Released into the cytosol following apoptotic stimuli, such as UV treatment (PubMed:17397804). The extramitochondrial protein does not diffuse throughout the cytosol but stays near the mitochondria (PubMed:17397804). {ECO:0000269|PubMed:17397804, ECO:0000269|PubMed:18259196}. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated by th, thereby antagonizing induced cell death.; PTM: Autoproteolytically cleaved into active forms in the mitochondria. {ECO:0000269|PubMed:17557079, ECO:0000269|PubMed:18259196}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14605208; 16998822; 17645804; 17996400; 19118185; 19182545; 19282869; 20220848; 20371351; 20950655; 21074052; 21441212; 21512585; 22494833; 22496853; 23024178; 23071443; 23523076; 24099009; 24998521; 25062361; 25312911; 25687947; 25708988; 25848931; 26160069; 26870755; 26896675; 27502471; 27848260; 27960592; 28211869; 28809158; 28945745; 29360576; 30545438; 31722958; 31837423; 32357532; 32444642; 33827210; 33863891; 34216545; 34244144; 34463269; |
| Motif | MOTIF 75..78; /note="IAP-binding"; /evidence="ECO:0000255, ECO:0000269|PubMed:18259196"; MOTIF 94..97; /note="IAP-binding"; /evidence="ECO:0000255, ECO:0000269|PubMed:18259196" |
| Gene Encoded By | |
| Mass | 46,000 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.108; |