MASP2_POLPI
ID MASP2_POLPI Reviewed; 14 AA.
AC P84915;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Venom protein 13a {ECO:0000303|PubMed:15150833};
DE Short=VP13a {ECO:0000305|PubMed:15150833};
DE AltName: Full=Polybia-MP-II {ECO:0000303|PubMed:19463874};
DE AltName: Full=Polybia-MPII {ECO:0000305};
OS Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Epiponini; Polybia.
OX NCBI_TaxID=291283;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT LEU-14, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15150833; DOI=10.1002/rcm.1452;
RA de Souza B.M., Marques M.R., Tomazela D.M., Eberlin M.N., Mendes M.A.,
RA Palma M.S.;
RT "Mass spectrometric characterization of two novel inflammatory peptides
RT from the venom of the social wasp Polybia paulista.";
RL Rapid Commun. Mass Spectrom. 18:1095-1102(2004).
RN [2]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT
RP LEU14, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=19463874; DOI=10.1016/j.peptides.2009.05.008;
RA de Souza B.M., da Silva A.V., Resende V.M., Arcuri H.A.,
RA Dos Santos Cabrera M.P., Ruggiero Neto J., Palma M.S.;
RT "Characterization of two novel polyfunctional mastoparan peptides from the
RT venom of the social wasp Polybia paulista.";
RL Peptides 30:1387-1395(2009).
RN [3]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=30974767; DOI=10.3390/toxins11040216;
RA das Neves R.C., Mortari M.R., Schwartz E.F., Kipnis A.,
RA Junqueira-Kipnis A.P.;
RT "Antimicrobial and antibiofilm effects of peptides from venom of social
RT wasp and scorpion on multidrug-resistant Acinetobacter baumannii.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: Antimicrobial peptide (PubMed:19463874, PubMed:30974767). Is
CC active against both Gram-negative and -positive bacteria
CC (Staphylococcus aureus (MIC=2 uM), Mycobacterium abscessus subsp.
CC massiliense, S.aureus (EC(50)=1.83 uM), Escherichia coli (MIC=5 uM),
CC Pseudomonas aeruginosa (MIC=38 uM), Bacillus cereus (MIC=5 uM), and the
CC multidrug-resistant bacterium A.baumannii), and fungi (Candida albicans
CC (EC(50)=12.9 uM, EC(90)=15.3 uM) and Cryptococcus neoformans (EC(50)=11
CC uM, EC(90)=22.7 uM)) (By similarity) (PubMed:19463874,
CC PubMed:30974767). Inhibits biofilm formation of A.baumannii and
CC Staphylococcus spp. bacteria (PubMed:30974767). Mycobacteria cell shape
CC and cell wall integrity are not altered after exposure to the peptide
CC (6.25 uM) (By similarity). Has low hemolytic activity (MIC=50 uM)
CC (PubMed:15150833, PubMed:19463874) (By similarity). Is also cytotoxic
CC to mouse peritoneal macrophages (EC(50)=13.19 uM) (By similarity). Also
CC causes moderate mast cell degranulation (ED(50)=80 uM) and exhibits
CC chemotactic activity for polymorphonucleated leukocytes (PMNL)
CC (PubMed:15150833, PubMed:19463874). Shows antibacterial activity
CC against multidrug-resistant A.baumannii adherence and biofilm formation
CC on vascular stents, preventing its formation and treating mature
CC biofilm (PubMed:30974767). In vivo, shows antistaphylococcal activity
CC (S.aureus) with a decline bacterial load after 6 days of topical
CC treatment (By similarity). {ECO:0000250|UniProtKB:P0DQT3,
CC ECO:0000269|PubMed:15150833, ECO:0000269|PubMed:19463874,
CC ECO:0000269|PubMed:30974767}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15150833,
CC ECO:0000269|PubMed:19463874}. Target cell membrane
CC {ECO:0000305|PubMed:19463874}. Note=Forms an alpha-helical membrane
CC channel in the prey. {ECO:0000305|PubMed:19463874}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15150833}.
CC -!- MASS SPECTROMETRY: Mass=1612.07; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15150833};
CC -!- BIOTECHNOLOGY: Could be used to treat biofilm-resistant agents such as
CC A.baumannii and Staphylococcus spp. coated on the surfaces of implanted
CC medical devices, such as vascular stents.
CC {ECO:0000269|PubMed:30974767}.
CC -!- MISCELLANEOUS: The primary structure of this mature peptide is
CC identical to that of Polybia-MPII from Pseudopolybia vespiceps testacea
CC (AC P0DQT3). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC {ECO:0000255}.
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DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB.
DR InterPro; IPR013214; Mastoparan_peptide.
DR Pfam; PF08251; Mastoparan_2; 1.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Chemotaxis; Cytolysis;
KW Direct protein sequencing; Fungicide; Hemolysis; Immunity; Innate immunity;
KW Mast cell degranulation; Membrane; Secreted; Target cell membrane;
KW Target membrane.
FT PEPTIDE 1..14
FT /note="Venom protein 13a"
FT /evidence="ECO:0000269|PubMed:15150833"
FT /id="PRO_0000248506"
FT MOD_RES 14
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:15150833"
SQ SEQUENCE 14 AA; 1614 MW; 2209239FD56ABE38 CRC64;
INWLKLGKMV IDAL
