Q9V3Z2 · SER7_DROME
- ProteinSerine protease 7
- GeneSp7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids391 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine protease that, by cleaving and activating prophenoloxidase (PPO1) after immune challenge, plays an essential role in the melanization immune response to septic wounding (PubMed:16256951, PubMed:16322759, PubMed:16861233, PubMed:19071960, PubMed:24260243).
May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea (PubMed:16322759, PubMed:18854145, PubMed:24260243).
Important for the innate immune response to fungi (PubMed:16861233).
Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway (PubMed:16861233).
May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A in the hemolymph and Spn77BA in the trachea (PubMed:16322759, PubMed:18854145, PubMed:24260243).
Important for the innate immune response to fungi (PubMed:16861233).
Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway (PubMed:16861233).
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 182 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 202 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 204 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 207 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 210 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 244 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 341 | Charge relay system | ||||
Sequence: S |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | metal ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | melanization defense response | |
Biological Process | positive regulation of melanization defense response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSerine protease 7
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9V3Z2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown is semi-pupal lethal, with 50% of pupae dying at the late pupal stage or during eclosion (PubMed:16861233).
Adults display impaired melanization at the site of septic infection (septic injury) using either Gram-negative or Gram-positive bacteria (PubMed:16256951, PubMed:16861233, PubMed:19071960).
Reduced survival, PPO1 activity and induction of the antimicrobial peptide Drs following septic injury using the fungus B.bassiana (PubMed:16256951, PubMed:16861233).
Septic injury with various bacteria reduces survival (L.monocytogenes, S.typhimurium and S.aureus) and in some cases decreases (E.faecelis) or increases bacterial growth (L.monocytogenes, S.typhimurium and B.cepacia). Aseptic injury reduces survival (PubMed:19071960).
Aseptic wounding has no effect on survival (PubMed:22227521).
Significant increase in survival after immune challenge with S.pneumoniae although there is no increase in melanization (PubMed:19071960).
No effect on the survival following infection with various bacteria (E.coli, B.cepacia and E.faecelis) (PubMed:19071960).
No induction of the antimicrobial peptides Drs and Dpt following infection with E.carotovora (PubMed:16861233).
Adults display impaired melanization at the site of septic infection (septic injury) using either Gram-negative or Gram-positive bacteria (PubMed:16256951, PubMed:16861233, PubMed:19071960).
Reduced survival, PPO1 activity and induction of the antimicrobial peptide Drs following septic injury using the fungus B.bassiana (PubMed:16256951, PubMed:16861233).
Septic injury with various bacteria reduces survival (L.monocytogenes, S.typhimurium and S.aureus) and in some cases decreases (E.faecelis) or increases bacterial growth (L.monocytogenes, S.typhimurium and B.cepacia). Aseptic injury reduces survival (PubMed:19071960).
Aseptic wounding has no effect on survival (PubMed:22227521).
Significant increase in survival after immune challenge with S.pneumoniae although there is no increase in melanization (PubMed:19071960).
No effect on the survival following infection with various bacteria (E.coli, B.cepacia and E.faecelis) (PubMed:19071960).
No induction of the antimicrobial peptides Drs and Dpt following infection with E.carotovora (PubMed:16861233).
PTM/Processing
Features
Showing features for signal, propeptide, disulfide bond, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MKSTRKVVGIFLATCLLPFTVLQNVAA | ||||||
Propeptide | PRO_0000438113 | 28-136 | Activation peptide | |||
Sequence: QGSCRNPNQKQGQCLSIYDCQSLLSVIQQSYVSPEDRTFLRNSQCLDGVGRQPYVCCTSDRSFGSQEATSAAPPPTTTSSSSRGQDGQAGLGNLLPSPPKCGPHSFSNK | ||||||
Disulfide bond | 31↔83 | |||||
Sequence: CRNPNQKQGQCLSIYDCQSLLSVIQQSYVSPEDRTFLRNSQCLDGVGRQPYVC | ||||||
Disulfide bond | 41↔72 | |||||
Sequence: CLSIYDCQSLLSVIQQSYVSPEDRTFLRNSQC | ||||||
Disulfide bond | 47↔84 | |||||
Sequence: CQSLLSVIQQSYVSPEDRTFLRNSQCLDGVGRQPYVCC | ||||||
Disulfide bond | 128↔264 | |||||
Sequence: CGPHSFSNKVYNGNDTAIDEFNWMALLEYVDNRGRRELSCGGSLINNRYVLTAAHCVIGAVETEVGHLTTVRLGEYDTSKDVDCIDDICNQPILQLGIEQATVHPQYDPANKNRIHDIALLRLDRPVVLNEYIQPVC | ||||||
Chain | PRO_5007718041 | 137-391 | Serine protease 7 | |||
Sequence: VYNGNDTAIDEFNWMALLEYVDNRGRRELSCGGSLINNRYVLTAAHCVIGAVETEVGHLTTVRLGEYDTSKDVDCIDDICNQPILQLGIEQATVHPQYDPANKNRIHDIALLRLDRPVVLNEYIQPVCLPLVSTRMAINTGELLVVSGWGRTTTARKSTIKQRLDLPVNDHDYCARKFATRNIHLISSQLCVGGEFYRDSCDGDSGGPLMRRGFDQAWYQEGVVSFGNRCGLEGWPGVYTRVADYMDWIVETIRP | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 167↔183 | |||||
Sequence: CGGSLINNRYVLTAAHC | ||||||
Disulfide bond | 211↔216 | |||||
Sequence: CIDDIC | ||||||
Disulfide bond | 310↔327 | |||||
Sequence: CARKFATRNIHLISSQLC | ||||||
Disulfide bond | 337↔366 | |||||
Sequence: CDGDSGGPLMRRGFDQAWYQEGVVSFGNRC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated after wounding. Levels are higher with septic wounding, using either Gram-negative or Gram-positive bacteria.
Developmental stage
First detected in stage 11 embryos, in cells close to the gnathal region. At stage 13, expressed in numerous cells that are dispersed throughout the embryo. During organogenesis predominantly expressed under the cuticle in the proventricular zone close to the hindgut. In L3 larvae, expressed in the lymph glands, the hematopoietic organ that flanks the dorsal vessel and in mature hemolymph crystal cells that appear in clusters attached to diverse organs.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-84 | Clip | ||||
Sequence: SCRNPNQKQGQCLSIYDCQSLLSVIQQSYVSPEDRTFLRNSQCLDGVGRQPYVCC | ||||||
Compositional bias | 91-115 | Polar residues | ||||
Sequence: GSQEATSAAPPPTTTSSSSRGQDGQ | ||||||
Region | 91-121 | Disordered | ||||
Sequence: GSQEATSAAPPPTTTSSSSRGQDGQAGLGNL | ||||||
Domain | 137-390 | Peptidase S1 | ||||
Sequence: VYNGNDTAIDEFNWMALLEYVDNRGRRELSCGGSLINNRYVLTAAHCVIGAVETEVGHLTTVRLGEYDTSKDVDCIDDICNQPILQLGIEQATVHPQYDPANKNRIHDIALLRLDRPVVLNEYIQPVCLPLVSTRMAINTGELLVVSGWGRTTTARKSTIKQRLDLPVNDHDYCARKFATRNIHLISSQLCVGGEFYRDSCDGDSGGPLMRRGFDQAWYQEGVVSFGNRCGLEGWPGVYTRVADYMDWIVETIR |
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.
Sequence similarities
Belongs to the peptidase S1 family. CLIP subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length391
- Mass (Da)43,128
- Last updated2000-05-01 v1
- Checksum3E1416F12EDF89F6
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 91-115 | Polar residues | ||||
Sequence: GSQEATSAAPPPTTTSSSSRGQDGQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF233093 EMBL· GenBank· DDBJ | AAF43410.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF54143.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAG22126.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAG22127.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY060475 EMBL· GenBank· DDBJ | AAL25514.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AY665379 EMBL· GenBank· DDBJ | AAT76546.1 EMBL· GenBank· DDBJ | mRNA | ||
BT128742 EMBL· GenBank· DDBJ | AEH59645.1 EMBL· GenBank· DDBJ | mRNA |