ID A0A182XY18_ANOST Unreviewed; 440 AA.
AC A0A182XY18;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
OS Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI01104-PA, ECO:0000313|Proteomes:UP000076408};
RN [1] {ECO:0000313|Proteomes:UP000076408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA Sharakhov I.V., Tu Z.;
RT "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT stephensi.";
RL Genome Biol. 15:459-459(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASTEI01104-PA}
RP IDENTIFICATION.
RC STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI01104-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182XY18; -.
DR STRING; 30069.A0A182XY18; -.
DR EnsemblMetazoa; ASTEI01104-RA; ASTEI01104-PA; ASTEI01104.
DR VEuPathDB; VectorBase:ASTE005467; -.
DR VEuPathDB; VectorBase:ASTEI01104; -.
DR VEuPathDB; VectorBase:ASTEI20_035223; -.
DR OMA; IMSPEGY; -.
DR Proteomes; UP000076408; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
SQ SEQUENCE 440 AA; 48540 MW; 29770CE409F1EF30 CRC64;
MIKVHPAKTM YCCALRRSAS IFQHRWLVGV HLSAHHSSRP IQTTKQHHDD GRHEQGKHRR
FGTTMALTGV FGLLAYKQTL SNDEQHKSRR HSWSLWPTVG AKTNADTTTK RSQRKDFNFI
ADAVEISAPA VVYLEIRDRQ HVDFFTREPL TVSTGSGFII ESDGLILTNA HVVVSKPHTM
VTVKLPDGRT FPGYVEHVDP ASDLATVRVH CNNLPTMKLG QSADLRTGEW VVALGSPLAL
NNTVTAGVIS TTQRPSQELG LRGKDINYIQ TDAAITFGNS GGPLVNLDGE AIGINSMKVT
PGISFAIPID HAKEFLRKIN ESPAGTDRRA AGDAHTYRRY IGITMLTLTP EILSELQQRN
HKFPPSVRGG VLVWKVIQGS PAYSGGLQPG DIITHINGKE IKNSSDVYEL LLEQDKKLSI
SIYRGQQLTT VHVFPEDTTA
//
