HTRA2_DROMO
ID HTRA2_DROMO Reviewed; 430 AA.
AC B4K835;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GI24802;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW15389.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW15389.1};
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; CH933806; EDW15389.1; -; Genomic_DNA.
DR RefSeq; XP_001999928.2; XM_001999892.2.
DR AlphaFoldDB; B4K835; -.
DR SMR; B4K835; -.
DR STRING; 7230.FBpp0174019; -.
DR EnsemblMetazoa; FBtr0175527; FBpp0174019; FBgn0147524.
DR GeneID; 6573869; -.
DR KEGG; dmo:Dmoj_GI24802; -.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_6_0_1; -.
DR InParanoid; B4K835; -.
DR OMA; DTRHFDY; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; B4K835; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP ?..82
FT /evidence="ECO:0000255"
FT /id="PRO_0000382187"
FT CHAIN 83..430
FT /note="Serine protease HTRA2, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
FT /id="PRO_0000382188"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 333..418
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 30..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..310
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT MOTIF 83..86
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
SQ SEQUENCE 430 AA; 46847 MW; CC005C22257F61F5 CRC64;
MALRSINKLN VFVKRCATTL LYCRHKSAPS ALNTNSASSP TSTNSSRNNN NKNEDDNRNN
KNGFSGYSWR SAIRFFVPFS LGALASTMVA QREELTPTIS ARTLNGRRRE FNFIADVVAG
CADSVVYIEI KDTRHFDYFS GQPITASNGS GFVIEQNGLI LTNAHVVINK PNTMVQVRLS
DGRTFPATIE DVDQTSDLAT LRIQVNNLSV MKLGKSSTLR SGEWVVALGS PLALSNTVTA
GVISSTQRAS QELGLRNRDI NYLQTDAAIT FGNSGGPLVN LDGEAIGVNS MKVTAGISFA
IPIDYVKVFL ERAAARRKKG SAYKTGYPVK RYMGITMLTL TPDILFELKS RTQNMPNTLS
HGVLVWKVIV GSPAHSGGLQ PGDIVTHINK KEIKNSSDVY DALADGKKEL DIVILRGVKQ
MRVTITPEDP
