HTRA2_DROVI
ID HTRA2_DROVI Reviewed; 421 AA.
AC B4LY58;
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=GJ24448;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW67946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW67946.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH940650; EDW67946.1; -; Genomic_DNA.
DR RefSeq; XP_002054426.1; XM_002054390.2.
DR AlphaFoldDB; B4LY58; -.
DR SMR; B4LY58; -.
DR STRING; 7244.FBpp0238865; -.
DR EnsemblMetazoa; FBtr0240373; FBpp0238865; FBgn0211528.
DR GeneID; 6630732; -.
DR KEGG; dvi:6630732; -.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; B4LY58; -.
DR OMA; DTRHFDY; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; B4LY58; -.
DR Proteomes; UP000008792; 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 ?..73
FT /evidence="ECO:0000255"
FT /id="PRO_0000382197"
FT CHAIN 74..421
FT /note="Serine protease HTRA2, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
FT /id="PRO_0000382198"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 324..409
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 138..301
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT MOTIF 74..77
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
SQ SEQUENCE 421 AA; 45903 MW; 64B176C0F5F67CB7 CRC64;
MALRSINKLE VFLKRYSAPT LYYCSNKSAH GATNGIGTDD SNNNYNNNNK NKNGYTGFSW
RSVIRFFVPF SLGALASTMV AQREELTPTI SARALSGRRR EFNFIADVVA GCADSVVYIE
IKDTRHFDYF SGQPITASNG SGFVIEQNGL ILTNAHVVIN KPNTMVQVRL SDGRTFPATI
EDVDQTSDLA TLRIQVNNLS VMKLGKSSTL RSGEWVVALG SPLALSNTVT AGVISSTQRA
SQELGLRNRD INYLQTDAAI TFGNSGGPLV NLDGEAIGVN SMKVTAGISF AIPIDYVKVF
LERAAARRRK GSAYKTGYPV KRYMGITMLT LTPDILFELK SRTQNMPNTL SHGVLVWKVI
VGSPAHSGGL QPGDIVTHIN KKEIKNSSDV YDALADGKKE LDIVILRGVK QMRVTITPED
P
