PPAF3_HOLDI
ID PPAF3_HOLDI Reviewed; 351 AA.
AC Q8I6K0;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Phenoloxidase-activating factor 3 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:17287215};
DE AltName: Full=Prophenoloxidase-activating factor III {ECO:0000303|PubMed:12185078};
DE AltName: Full=Serine protease-like protein PPAF-3 {ECO:0000305};
DE Contains:
DE RecName: Full=Phenoloxidase-activating factor 3 light chain {ECO:0000305};
DE Contains:
DE RecName: Full=Phenoloxidase-activating factor 3 heavy chain {ECO:0000305};
DE Flags: Precursor;
GN Name=PPAF3 {ECO:0000305|PubMed:12185078};
GN Synonyms=PPAF-III {ECO:0000303|PubMed:12185078};
OS Holotrichia diomphalia (Korean black chafer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Melolonthinae; Holotrichia.
OX NCBI_TaxID=33394 {ECO:0000312|EMBL:BAC15604.1};
RN [1] {ECO:0000312|EMBL:BAC15604.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 217-224, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=12185078; DOI=10.1074/jbc.m205508200;
RA Kim M.S., Baek M.J., Lee M.H., Park J.W., Lee S.Y., Soderhall K., Lee B.L.;
RT "A new easter-type serine protease cleaves a masquerade-like protein during
RT prophenoloxidase activation in Holotrichia diomphalia larvae.";
RL J. Biol. Chem. 277:39999-40004(2002).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=17287215; DOI=10.1074/jbc.m611556200;
RA Piao S., Kim S., Kim J.H., Park J.W., Lee B.L., Ha N.C.;
RT "Crystal structure of the serine protease domain of prophenoloxidase
RT activating factor-I.";
RL J. Biol. Chem. 282:10783-10791(2007).
CC -!- FUNCTION: Serine endopeptidase which, by cleaving prophenoloxidase
CC activating factor PPAF2, is required for the activation of the
CC prophenoloxidase cascade probably following the recognition of
CC pathogen-derived products. {ECO:0000269|PubMed:12185078,
CC ECO:0000269|PubMed:17287215}.
CC -!- ACTIVITY REGULATION: Cleavage of PPAF2 is Ca(2+)-independent
CC (PubMed:12185078). Inhibited by heparin (PubMed:17287215).
CC {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:17287215}.
CC -!- SUBUNIT: In the active form, heterodimer of a light chain and a heavy
CC chain; disulfide-linked (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12185078}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078}.
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 -!- PTM: Proteolytically cleaved. {ECO:0000269|PubMed:12185078}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
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DR EMBL; AB079666; BAC15604.1; -; mRNA.
DR AlphaFoldDB; Q8I6K0; -.
DR SMR; Q8I6K0; -.
DR MEROPS; S01.204; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunity; Innate immunity; Metal-binding; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..96
FT /note="Phenoloxidase-activating factor 3 light chain"
FT /evidence="ECO:0000305"
FT /id="PRO_5004308145"
FT CHAIN 97..351
FT /note="Phenoloxidase-activating factor 3 heavy chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443523"
FT DOMAIN 22..73
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 97..350
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 299
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9GRW0"
FT SITE 96..97
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 23..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 33..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 39..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DISULFID 89..224
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT DISULFID 127..143
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT DISULFID 167..176
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT DISULFID 268..285
FT /evidence="ECO:0000250|UniProtKB:O97366"
FT DISULFID 295..326
FT /evidence="ECO:0000250|UniProtKB:O97366"
SQ SEQUENCE 351 AA; 37925 MW; 2A7F0BDFC52D78E5 CRC64;
MWLSLVILGV ASAIVNVSTQ ESCTTPNGET ATCLPIESCK IFWDYVVTSG ADPEINSFLR
ASLCRQGNYV VCCGSTLKFN SALPDRTECG LQDDFKVLGG EDTDLGEYPW MALLQQTKTS
GAKSFGCGGS LISDRYVLTA AHCVVSSSYT VTMVRLGEWD LRATQDCVGS GSYQYCSPPP
QDIGIESITS HPNYEKSSRG VFNDIALIRL ARPVNRNKYV QPICLPLPTE RTPVGENLLV
AGWGATETKA QSDKKQKLKL PVTDLPACKT LYAKHNKIIN DKMICAGGLK GKDSCKGDSG
GPLFGQTGAG NAQFYIEGIV SYGAICGTEG FPAIYTRVSD HLDWIKQNVR V
