O97366 · PPAF1_HOLDI
- ProteinPhenoloxidase-activating factor 1
- GenePPAF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.
Activity regulation
Protein stability and endopeptidase activity are calcium dependent (PubMed:17287215).
First cleavage on prophenoloxidase PPO1 and PPO2 is not dependent on calcium; however, cleavage of PPO1 and PPO2 to their active forms is dependent on calcium and on the presence of PPAF2 and PPAF3 (PubMed:12185078).
Cleavage of PPAF2 is inhibited by calcium (PubMed:11012672, PubMed:12185078).
Inhibited by ethylenediaminetetraacetic acid (EDTA), p-nitrophenyl-p'-guanido-benzoate, diisopropylphosphorofluoridate (iPr2PF) and p-(Amidinophenyl)methanesulfonyl fluoride (p-APMSF) (PubMed:17287215, PubMed:9652393).
First cleavage on prophenoloxidase PPO1 and PPO2 is not dependent on calcium; however, cleavage of PPO1 and PPO2 to their active forms is dependent on calcium and on the presence of PPAF2 and PPAF3 (PubMed:12185078).
Cleavage of PPAF2 is inhibited by calcium (PubMed:11012672, PubMed:12185078).
Inhibited by ethylenediaminetetraacetic acid (EDTA), p-nitrophenyl-p'-guanido-benzoate, diisopropylphosphorofluoridate (iPr2PF) and p-(Amidinophenyl)methanesulfonyl fluoride (p-APMSF) (PubMed:17287215, PubMed:9652393).
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 109-110 | Cleavage | ||||
Sequence: KI | ||||||
Active site | 155 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 175 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 177 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 180 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 183 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 220 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 315 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | endopeptidase activity | |
Molecular Function | peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | innate immune response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePhenoloxidase-activating factor 1
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Coleoptera > Polyphaga > Scarabaeiformia > Scarabaeidae > Melolonthinae > Holotrichia
Accessions
- Primary accessionO97366
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MKQVHFFILWFFVLNLYSIKAQA | ||||||
Chain | PRO_5004160790 | 24-109 | Phenoloxidase-activating factor 1 light chain | |||
Sequence: GCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCCGSSASYQPPPTSASIRNRRPELLPNDCGYQVEADK | ||||||
Disulfide bond | 25↔73 | |||||
Sequence: CRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVC | ||||||
Disulfide bond | 35↔64 | |||||
Sequence: CVPINNCKILYDSVLTSDPEVIRFLRASQC | ||||||
Disulfide bond | 41↔74 | |||||
Sequence: CKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCC | ||||||
Disulfide bond | 101↔240 | Interchain (between light and heavy chains) | ||||
Sequence: CGYQVEADKILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVC | ||||||
Chain | PRO_0000443316 | 110-365 | Phenoloxidase-activating factor 1 heavy chain | |||
Sequence: ILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLLAERANQQFFLEGLVSFGATCGTEGWPGIYTKVGKYRDWIEGNIRP | ||||||
Glycosylation | 131 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 140↔156 | |||||
Sequence: CGGSLINNRYIVTAAHC | ||||||
Disulfide bond | 184↔191 | |||||
Sequence: CYGAVRVC | ||||||
Disulfide bond | 284↔301 | |||||
Sequence: CAKTFGAAGVRVRSSQLC | ||||||
Disulfide bond | 311↔340 | |||||
Sequence: CGGDSGGPLLAERANQQFFLEGLVSFGATC |
Post-translational modification
Cleaved following the recognition of pathogen-derived products, probably by a lysyl endopeptidase.
Keywords
- PTM
PTM databases
Expression
Developmental stage
Expressed in larva (at protein level).
Interaction
Subunit
In the active form, heterodimer of a light chain and a heavy chain; disulfide-linked (Probable).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-74 | Clip | ||||
Sequence: GCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCC | ||||||
Domain | 110-364 | Peptidase S1 | ||||
Sequence: ILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLLAERANQQFFLEGLVSFGATCGTEGWPGIYTKVGKYRDWIEGNIR |
Domain
The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure (By similarity).
The clip domain is necessary for regulating the zymogen activation (PubMed:16362048).
The clip domain is necessary for regulating the zymogen activation (PubMed:16362048).
Sequence similarities
Belongs to the peptidase S1 family. CLIP subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length365
- Mass (Da)40,195
- Last updated1999-05-01 v1
- ChecksumEC69F6093923F4C5
Keywords
- Technical term