HTRA2_DROER
ID HTRA2_DROER Reviewed; 422 AA.
AC B3P3J9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=GG21285;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV48887.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV48887.1};
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; CH954181; EDV48887.1; -; Genomic_DNA.
DR RefSeq; XP_001979929.1; XM_001979893.2.
DR AlphaFoldDB; B3P3J9; -.
DR SMR; B3P3J9; -.
DR STRING; 7220.FBpp0139831; -.
DR EnsemblMetazoa; FBtr0141339; FBpp0139831; FBgn0113464.
DR GeneID; 6552632; -.
DR KEGG; der:6552632; -.
DR eggNOG; KOG1320; Eukaryota.
DR HOGENOM; CLU_020120_6_0_1; -.
DR OMA; DTRHFDY; -.
DR OrthoDB; 630723at2759; -.
DR PhylomeDB; B3P3J9; -.
DR Proteomes; UP000008711; 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; Serine protease;
KW Transit peptide; Transmembrane; Transmembrane helix; Zymogen.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 18..74
FT /evidence="ECO:0000255"
FT /id="PRO_0000382183"
FT CHAIN 75..422
FT /note="Serine protease HTRA2, mitochondrial"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
FT /id="PRO_0000382184"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 325..410
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 24..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..302
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT MOTIF 75..78
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT MOTIF 94..97
FT /note="IAP-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 25..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O43464"
FT ACT_SITE 266
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9VFJ3"
SQ SEQUENCE 422 AA; 45845 MW; AE3E47A90BE794D1 CRC64;
MALRGSHRLQ VILKRCIASP LFHSHAPNRR SSQPAIKGGE PNSNGNSGHD QQNGERKGKG
WRRLVSFFVP FSLGAVVSAA VIKREDFTPT IAASKMTGRR RDFNFIADVV AGCADSVVYI
EIKDTRHFDY FSGQPITASN GSGFIIEQNG LILTNAHVVI NKPHTMVQVR LSDGRTFPAT
IEDVDQTSDL ATLRIQVNNL SVMRLGKSST LRSGEWVVAL GSPLALSNTV TAGVISSTQR
ASQELGLRNR DINYLQTDAA ITFGNSGGPL VNLDGEAIGV NSMKVTAGIS FAIPIDYVKV
FLERAAEKRK KGSAYKTGYP VKRYMGITML TLTPDILFEL KSRSQNMPSN LTHGVLVWKV
IVGSPAHSGG LQPGDIVTHI NKKEIKNSSD VYDALADNSK NLDIVILRGV KQMHVTITPE
DP
