P0C1Q4 · MASTI_POLPI
- ProteinPolybia-mastoparan-I
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Antimicrobial and chemotactic peptide for polymorphonucleated leukocytes (PMNL) (PubMed:16129513).
Potent antimicrobial peptide against Gram-positive bacteria B.subtilis CCT 2576 (MIC=4 ug/ml), and S.aureus ATCC 6538 (MIC=15 ug/ml) and Gram-negative bacteria E.coli ATCC 25922 (MIC=8 ug/ml) and P.aeruginosa ATCC 15422 (MIC=8 ug/ml) (PubMed:16129513).
Has low cytotoxicity to normal (non-cancer) cells (Probable) (PubMed:18328599, PubMed:22630563).
Exhibits preferential interaction with anionic lipid vesicles over zwitterionic ones, which is further impaired by the presence of cholesterol (PubMed:18328599, PubMed:22630563).
In vivo, blood biochemical parameters after mice injection suggest that the peptide induces acute renal failure, hemolysis, rhabdomyolysis, and hepatic necrosis (PubMed:20600424).
The death of mice is probably due to acute renal failure resulting from rhabdomyolysis and intravascular hemolysis (PubMed:20600424).
Importantly, the peptide is more toxic to cancer cell lines (Jurkat, K-562) than to primary non-cancer cells (human primary lymphocytes) (Probable) (PubMed:22630563).
Its toxicity is related to the induction of necrosis (PubMed:19233550, PubMed:22630563).
Shows a pore-like activity on Jurkat cells with several bilayer compositions: the highest average conductance is found in bilayers formed by phosphatidylcholine or a mixture of phosphatidylcholine and phosphatidylserine (70:30) (PubMed:22630563).
Shows a membranolytic activity on human glioblastoma multiforme cells (brain tumor cells) that leads to cell necrosis (PubMed:28965321).
Selectively inhibits the proliferation of prostate and bladder cancer cell lines, as well as the associated endothelial cells (PubMed:18328599).
Is effective against multidrug resistant leukemic cells (PubMed:19233550).
In vivo, shows anticancer activity when tested on sarcoma xenograft tumors (PubMed:20600424).
Potent antimicrobial peptide against Gram-positive bacteria B.subtilis CCT 2576 (MIC=4 ug/ml), and S.aureus ATCC 6538 (MIC=15 ug/ml) and Gram-negative bacteria E.coli ATCC 25922 (MIC=8 ug/ml) and P.aeruginosa ATCC 15422 (MIC=8 ug/ml) (PubMed:16129513).
Has low cytotoxicity to normal (non-cancer) cells (Probable) (PubMed:18328599, PubMed:22630563).
Exhibits preferential interaction with anionic lipid vesicles over zwitterionic ones, which is further impaired by the presence of cholesterol (PubMed:18328599, PubMed:22630563).
In vivo, blood biochemical parameters after mice injection suggest that the peptide induces acute renal failure, hemolysis, rhabdomyolysis, and hepatic necrosis (PubMed:20600424).
The death of mice is probably due to acute renal failure resulting from rhabdomyolysis and intravascular hemolysis (PubMed:20600424).
Importantly, the peptide is more toxic to cancer cell lines (Jurkat, K-562) than to primary non-cancer cells (human primary lymphocytes) (Probable) (PubMed:22630563).
Its toxicity is related to the induction of necrosis (PubMed:19233550, PubMed:22630563).
Shows a pore-like activity on Jurkat cells with several bilayer compositions: the highest average conductance is found in bilayers formed by phosphatidylcholine or a mixture of phosphatidylcholine and phosphatidylserine (70:30) (PubMed:22630563).
Shows a membranolytic activity on human glioblastoma multiforme cells (brain tumor cells) that leads to cell necrosis (PubMed:28965321).
Selectively inhibits the proliferation of prostate and bladder cancer cell lines, as well as the associated endothelial cells (PubMed:18328599).
Is effective against multidrug resistant leukemic cells (PubMed:19233550).
In vivo, shows anticancer activity when tested on sarcoma xenograft tumors (PubMed:20600424).
Miscellaneous
Negative results: causes no or weak hemolysis to rat and mice erythrocytes and has no mast cell degranulation activity at physiological concentrations.
The analog MPI-1, which has a C-terminal thioamide (CS-NH2) instead of the C-terminal amide (CO-NH2), suppress the growth of sarcoma xenograft tumors (S180) with a higher potency than the wild-type peptide. Has also a higher hemolytic activity, a remarkable improved stability to enzymatic degradation, a higher hydrophobicity, and a higher ability to bind protein. Surprisingly, this analog has a lower ability to kill mice than the wild-type peptide when intraperitoneally injected.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | other organism cell membrane | |
Biological Process | chemotaxis | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | defense response to Gram-positive bacterium | |
Biological Process | innate immune response | |
Biological Process | positive regulation of chemotaxis |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePolybia-mastoparan-I
- Short namesPolybia-MP-I ; Polybia-MPI
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Vespoidea > Vespidae > Polistinae > Epiponini > Polybia
Accessions
- Primary accessionP0C1Q4
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Note: Has an amphipathic alpha-helical conformation in a lipid environment (Probable). May disrupt lipid membranes by forming pore-like structure (Probable).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 7 | Decrease in both antitumor activity and content of alpha-helix conformation. | ||||
Sequence: L → P | ||||||
Mutagenesis | 8 | Decrease in both antitumor activity and content of alpha-helix conformation. | ||||
Sequence: D → P | ||||||
Mutagenesis | 9 | Decrease in both antitumor activity and content of alpha-helix conformation. | ||||
Sequence: A → P |
PTM/Processing
Features
Showing features for peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Peptide | PRO_0000247263 | 1-14 | Polybia-mastoparan-I | |||
Sequence: IDWKKLLDAAKQIL | ||||||
Modified residue | 14 | Leucine amide | ||||
Sequence: L |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.