HTRA2_DROAN
ID HTRA2_DROAN Reviewed; 426 AA.
AC B3LVG7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Serine protease HTRA2, mitochondrial {ECO:0000250|UniProtKB:Q9VFJ3};
DE EC=3.4.21.108;
DE AltName: Full=High temperature requirement protein A2 {ECO:0000250|UniProtKB:Q9VFJ3};
DE Flags: Precursor;
GN Name=HtrA2 {ECO:0000250|UniProtKB:Q9VFJ3}; ORFNames=GF17480;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV41495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV41495.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Serine protease that shows proteolytic activity against a
CC non-specific substrate beta-casein. Promotes or induces cell death
CC either by direct binding to and inhibition of BIRC proteins (also
CC called inhibitor of apoptosis proteins, IAPs), leading to an increase
CC in caspase activity, or by a BIRC inhibition-independent, caspase-
CC independent and serine protease activity-dependent mechanism. Can
CC antagonize antiapoptotic activity of th by directly inducing the
CC degradation of th (By similarity). {ECO:0000250|UniProtKB:Q9VFJ3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of non-polar aliphatic amino-acids at the P1
CC position, with a preference for Val, Ile and Met. At the P2 and P3
CC positions, Arg is selected most strongly with a secondary preference
CC for other hydrophilic residues.; EC=3.4.21.108;
CC -!- SUBUNIT: Interacts with th/DIAP1 (via BIR 2 domain).
CC {ECO:0000250|UniProtKB:Q9VFJ3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q9VFJ3}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9VFJ3};
CC Single-pass membrane protein {ECO:0000255}. Note=Predominantly present
CC in the intermembrane space. Released into the cytosol following
CC apoptotic stimuli, such as UV treatment. The extramitochondrial protein
CC does not diffuse throughout the cytosol but stays near the
CC mitochondria. {ECO:0000250|UniProtKB:Q9VFJ3}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000255}.
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DR EMBL; CH902617; EDV41495.1; -; Genomic_DNA.
DR RefSeq; XP_001952912.1; XM_001952877.2.
DR AlphaFoldDB; B3LVG7; -.
DR SMR; B3LVG7; -.
DR STRING; 7217.FBpp0120672; -.
DR EnsemblMetazoa; FBtr0122180; FBpp0120672; FBgn0094498.
DR GeneID; 6500264; -.
DR KEGG; dan:6500264; -.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_6_0_1; -.
DR InParanoid; B3LVG7; -.
DR OMA; DTRHFDY; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; B3LVG7; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016006; C:Nebenkern; IEA:EnsemblMetazoa.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:EnsemblMetazoa.
DR GO; GO:0007005; P:mitochondrion organization; IEA:EnsemblMetazoa.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:EnsemblMetazoa.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF17820; PDZ_6; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Apoptosis; Hydrolase; Membrane; Mitochondrion; Protease;
KW Reference proteome; Serine protease; Transit peptide; Transmembrane;
KW Transmembrane helix; Zymogen.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 31..78
FT /evidence="ECO:0000255"
FT /id="PRO_0000382181"
FT CHAIN 79..426
FT /note="Serine protease HTRA2, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
FT /id="PRO_0000382182"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 329..414
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 30..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..306
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT MOTIF 79..82
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
SQ SEQUENCE 426 AA; 46723 MW; 88F5B3C086209FDC CRC64;
MALRGSHRLD DFIRRCSALT LFHSQAPSRR VSHCGRDRRQ QQDPPGQGRQ EQQESGGGHW
SRFGWRSLIR FFVPFSLGAV ASSLVIKREE LTPTITAKAM SGRRRDFNFI ADVVAGCADS
VVYIEIKDTR HFDYFSGQPI TASNGSGFII EQNGLILTNA HVVINKPHTM VQVRLSDGRT
FPATIEDVDQ TSDLATLRIQ VSNLSVMRLG KSSTLRSGEW VVALGSPLAL SNTVTAGVIS
STQRASQELG LRNRDINYLQ TDAAITFGNS GGPLVNLDGE AIGVNSMKVT AGISFAIPID
YVKVFLERAA ERRKKGAAYK TGYPVKRYMG ITMLTLTPDI LFELKSRSQN MPSNLTHGVL
VWKVIVGSPA HSGGLQPGDI VTHINKKEIK NSSDVYDALA DNSKHLDIVI LRGVKQMHVT
ITPEDP
