PPAE1_SPOLT
ID PPAE1_SPOLT Reviewed; 374 AA.
AC Q49QW1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Phenoloxidase-activating enzyme 1 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|RuleBase:RU363034, ECO:0000269|PubMed:19557749};
DE AltName: Full=Prophenoloxidase-activating enzyme 1 {ECO:0000303|PubMed:19557749};
DE AltName: Full=Serine protease PPAE1 {ECO:0000305};
DE Short=Slppae1 {ECO:0000303|PubMed:19557749};
DE Flags: Precursor;
GN Name=PPAE1 {ECO:0000303|PubMed:19557749, ECO:0000312|EMBL:AAW24480.1};
OS Spodoptera litura (Asian cotton leafworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=69820 {ECO:0000312|EMBL:AAW24480.1};
RN [1] {ECO:0000312|EMBL:AAW24480.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND PTM.
RC TISSUE=Hemocyte {ECO:0000303|PubMed:19557749};
RX PubMed=19557749; DOI=10.1002/arch.20323;
RA Arora N., Hoque M.E., Rajagopal R., Sachdev B., Bhatnagar R.K.;
RT "Expression, purification, and characterization of pro-phenoloxidase-
RT activating serine protease from Spodoptera litura.";
RL Arch. Insect Biochem. Physiol. 72:61-73(2009).
CC -!- FUNCTION: Serine protease which, by cleaving and activating
CC prophenoloxidase (PPO1) after immune challenge, plays an essential role
CC in the melanization immune response to wounding.
CC {ECO:0000305|PubMed:19557749}.
CC -!- ACTIVITY REGULATION: Inhibited by aprotenin. Not inhibited by EDTA,
CC PMSF or leupeptin. {ECO:0000269|PubMed:19557749}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU366078,
CC ECO:0000269|PubMed:19557749}. Note=Secreted in the hemolymph.
CC {ECO:0000269|PubMed:19557749}.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes.
CC {ECO:0000269|PubMed:19557749}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae.
CC {ECO:0000269|PubMed:19557749}.
CC -!- INDUCTION: Upon physical injury. Up-regulated 5-fold after 6 hours and
CC 15-fold after 18 hours of injury. {ECO:0000269|PubMed:19557749}.
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236,
CC ECO:0000255|RuleBase:RU366078}.
CC -!- PTM: Activated by the removal of the N-terminal inhibitory propeptide.
CC {ECO:0000305|PubMed:19557749}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236, ECO:0000255|RuleBase:RU366078}.
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DR EMBL; AY677081; AAW24480.1; -; mRNA.
DR AlphaFoldDB; Q49QW1; -.
DR SMR; Q49QW1; -.
DR MEROPS; S01.427; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1640.30; -; 1.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Hydrolase; Metal-binding; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..120
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9V3Z2"
FT /id="PRO_0000450806"
FT CHAIN 121..374
FT /note="Phenoloxidase-activating enzyme 1"
FT /evidence="ECO:0000250|UniProtKB:Q9V3Z2"
FT /id="PRO_5023968796"
FT DOMAIN 21..74
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 121..370
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 83..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT DISULFID 22..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 32..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 38..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 151..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 292..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 317..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 374 AA; 40896 MW; C2187FCEFE57E711 CRC64;
MWKSLVFFVS ALIWSFGSSQ DCTTPTGSRS NCVSLYQCQP LYNAFEQRPL PTHVVSYLGR
SQCGFEGYVP RVCCGPLPEE QEATSARPTQ APTQGSSDVF PEDSSPAPRN QCGIDTTGDR
VYGGTITDLD EFPWMALLGY RTKKGTTSYQ CGGVLVNHRY ILTAAHCITG AIEQAVGTLI
TVRLGEYDTQ QDVDCIDSVC ADRPQEIRVA SAYPHPGYSD KNKNRQDDIG IVRLATRAAY
TYYVQPICLI DNRARLDTGS DVYVAGWGKT LNGRNSPIKL KLNLPIFNKQ ECDDKHRGEV
LSSVQICAGG VFAEDACRGD SGGPLMKKTP NGIWEVVGVV SFGYGCGRDG WPGVYTSVAR
YIDWIQNTIA SSNV
