ID A0A195EE27_9HYME Unreviewed; 433 AA.
AC A0A195EE27;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
GN ORFNames=ALC57_04235 {ECO:0000313|EMBL:KYN23361.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN23361.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN23361.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN23361.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN23361.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-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; KQ979039; KYN23361.1; -; Genomic_DNA.
DR RefSeq; XP_018358708.1; XM_018503206.1.
DR AlphaFoldDB; A0A195EE27; -.
DR STRING; 471704.A0A195EE27; -.
DR GeneID; 108758326; -.
DR OrthoDB; 2159919at2759; -.
DR Proteomes; UP000078492; 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:KYN23361.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 326..421
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 433 AA; 47482 MW; 62B9F37CFB384CF7 CRC64;
MASSWSLVRW TCLARASNSN ISRLATFVFA KQHAGTRTFH SHQQQQQHLQ HGRTIFSDGA
RRLLTCTAFV AATSLGYALY NWRDNIRQGI KSLIVPIPSV RAISLSDGNQ KRDKFNFIAD
AVEVSAPAVV YIEIRDGSRV DYFSGKPILT SNGSGFIISQ DGLILTNAHV VANKPHTAMK
IQVRLHDGST YSGTVEDIDL QSDLATVRIN KTNLPTMKLG SSANLRPGEF VVAIGAPLNL
SNTITSGIVS SVNRPSQELG INSRNMGLIQ TDAAITFGNS GGPLVNLNGE AIGINSMKVT
SGISFAIPID YAKEFLKKGE LRKKNKDVLH KDTPRRRYMG ITMQTLTPEI LNEMQQYYDY
TNVRHGVLVW KVMVGSPAYI AGLKPGDIVT HANGESVLDS SNIYKILEQP GTINLQILRK
GQTLYIQVDP EDV
//
