ID A0A154PIY5_DUFNO Unreviewed; 425 AA.
AC A0A154PIY5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Serine protease HTRA2, mitochondrial {ECO:0000256|ARBA:ARBA00016929};
DE EC=3.4.21.108 {ECO:0000256|ARBA:ARBA00013033};
DE AltName: Full=High temperature requirement protein A2 {ECO:0000256|ARBA:ARBA00029644};
DE Flags: Fragment;
GN ORFNames=WN55_02531 {ECO:0000313|EMBL:KZC11170.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC11170.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC11170.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC11170.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC11170.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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/Diap1 by directly inducing the
CC degradation of th/Diap1. {ECO:0000256|ARBA:ARBA00035606}.
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 Evidence={ECO:0000256|ARBA:ARBA00001760};
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004375}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004375}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004304}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; KQ434902; KZC11170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A154PIY5; -.
DR STRING; 178035.A0A154PIY5; -.
DR EnsemblMetazoa; XM_015577656.1; XP_015433142.1; LOC107189181.
DR Proteomes; UP000076502; Unassembled WGS sequence.
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 CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 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 PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KZC11170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 308..405
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT NON_TER 425
FT /evidence="ECO:0000313|EMBL:KZC11170.1"
SQ SEQUENCE 425 AA; 47072 MW; 5B3C56F4B811B418 CRC64;
MAAPLLRLPR TVFKKNQFQY KQVSVFLFVN HFSGIKSFHT RPQKQRTFNK NTKEILAYTF
LFSGLSYIWY NLRNDSDNGN RKQFSLTPKV AAKSINVLDI NHNRDKYNFI ADVVEISAPS
VVYIEIKDNK RFDYFTGKPI TASNGSGFVV QSDGLILTNA HVVVNKPNTT VKVRLYDGNT
YTGIVEDVDM HSDLATVRIN KTNLPVMKLG NSSNIRPGEF VVAIGSPLAL SNTITSGVVS
SVNRQSEELG LYNKQMGYIQ TDAAITFGNS GGPLVNLNGE AIGINAMKVT PGISFAIPID
HAKEFLKKAD MRRKSKGTHS SLTIPKNRYL GVTMLSLTPN LLFELQQRLE GIPQNIRHGV
LICKVIVGSP AHLGGLQSGD IITHVNDEPV LNALNIYKAI ETSKDLKLTV VRGVQVLQLR
IEPED
//
