ID   PFAF2_GALME             Reviewed;         303 AA.
AC   A0A6J1W8N1; C0HLY7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Phenoloxidase-activating factor 2 {ECO:0000303|PubMed:34443685};
DE            Short=PFAF2 {ECO:0000305};
DE   AltName: Full=Prophenoloxidase-activating factor II {ECO:0000250|UniProtKB:Q9GRW0};
DE   Flags: Fragment;
GN   Name=LOC113510063 {ECO:0000312|RefSeq:XP_026749280.1};
OS   Galleria mellonella (Greater wax moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Pyralidae; Galleriinae; Galleria.
OX   NCBI_TaxID=7137 {ECO:0000312|Proteomes:UP000504614};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Calla B., Robertson H.M., Grozinger C.M., Robinson G.E., Dolezal A.G.,
RA   Swale T., Shiue L., Berenbaum M.R.;
RT   "Genome sequence of Galleria mellonella, the greater wax moth.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 36-55, FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=34443685; DOI=10.3390/molecules26165097;
RA   Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P.,
RA   Skrzypiec K., Cytrynska M.;
RT   "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in
RT   the Insect Model Host Galleria mellonella.";
RL   Molecules 26:5097-5097(2021).
CC   -!- FUNCTION: Binds and activates processed prophenoloxidases PPO1 and PPO2
CC       and thus is involved in the activation of the prophenoloxidase cascade
CC       probably following the recognition of pathogen-derived products (By
CC       similarity). Binds the A.niger cell wall component alpha-1,3-glucan, a
CC       fungal pathogen-associated molecular pattern (PAMP) that activates the
CC       host immune response (PubMed:34443685). {ECO:0000250|UniProtKB:Q9GRW0,
CC       ECO:0000269|PubMed:34443685}.
CC   -!- SUBUNIT: Heterodimer. {ECO:0000250|UniProtKB:Q9GRW0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34443685}.
CC       Note=Secreted in the hemolymph. {ECO:0000269|PubMed:34443685}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in last instar larvae.
CC       {ECO:0000269|PubMed:34443685}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Lacks the conserved Ser residue within the catalytic triad
CC       which is replaced by a Gly residue, probably resulting in a loss of
CC       proteolytic activity. {ECO:0000305}.
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DR   EMBL; RBWF02003166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_026749280.1; XM_026893479.1.
DR   Proteomes; UP000504614; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Reference proteome; Secreted.
FT   CHAIN           <1..303
FT                   /note="Phenoloxidase-activating factor 2"
FT                   /id="PRO_0000455043"
FT   DOMAIN          36..292
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        173..247
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        206..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        237..268
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|RefSeq:XP_026749280.1"
SQ   SEQUENCE   303 AA;  33807 MW;  0C8BB44E571C3CA6 CRC64;
     PDRRPPEDPI TPPPPTKEEQ RAGCGWRNEN GVGFRIIGDK DGEAKFGEFP WMVAILKIEP
     VNDQDPEGQK LNVYVGGGSL IHPQVVLTAA HYVATAKTLR VRAGEWDTQT TKEIYPYQDR
     DVTHKEIHKD FNKGNLFYDI ALLFLSQPME MAPNVGVVCL PPRNERAEAG TRCFASGWGK
     DKFGKEGRYQ VILKKVEVPV VDRNTCQDQL RKTRLGRHFM LHSSFMCAGG EPGRDTCRGD
     GGSPLVCPIQ YEKGRYVQSG IVAWGIGCGE DRTPGVYVDV GNLRDWIDDK VAGRGIEPTV
     YTY