ID   MASP2_PARVS             Reviewed;          14 AA.
AC   P0DQT3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Polybia-MPII {ECO:0000303|PubMed:28108242};
OS   Parachartergus vespiceps testaceus (Wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Epiponini; Parachartergus; Parachartergus vespiceps.
OX   NCBI_TaxID=2893768;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SYNTHESIS, AND AMIDATION
RP   AT LEU-14.
RC   TISSUE=Venom;
RX   PubMed=28108242; DOI=10.1016/j.ijantimicag.2016.11.013;
RA   Silva J.C., Neto L.M., Neves R.C., Goncalves J.C., Trentini M.M.,
RA   Mucury-Filho R., Smidt K.S., Fensterseifer I.C., Silva O.N., Lima L.D.,
RA   Clissa P.B., Vilela N., Guilhelmelli F., Silva L.P., Rangel M., Kipnis A.,
RA   Silva-Pereira I., Franco O.L., Junqueira-Kipnis A.P., Bocca A.L.,
RA   Mortari M.R.;
RT   "Evaluation of the antimicrobial activity of the mastoparan Polybia-MPII
RT   isolated from venom of the social wasp Pseudopolybia vespiceps testacea
RT   (Vespidae, Hymenoptera).";
RL   Int. J. Antimicrob. Agents 49:167-175(2017).
RN   [2]
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:28108242, PubMed:30974767). Is
CC       active against both Gram-negative and Gram-positive bacteria
CC       (Staphylococcus aureus (MIC=2 uM), Mycobacterium abscessus subsp.
CC       massiliense, and S.aureus (EC(50)=1.83 uM), Escherichia coli (MIC=5
CC       uM), Pseudomonas aeruginosa (MIC=38 uM), Bacillus cereus (MIC=5 uM),
CC       and the multidrug-resistant bacterium A.baumannii), and fungi (Candida
CC       albicans (EC(50)=12.9 uM, EC(90)=15.3 uM) and Cryptococcus neoformans
CC       (EC(50)=11 uM, EC(90)=22.7 uM)) (PubMed:28108242, PubMed:30974767).
CC       Inhibits biofilm formation of A.baumannii and Staphylococcus spp.
CC       bacteria (PubMed:30974767). Mycobacteria cell shape and cell wall
CC       integrity are not altered after exposure to the peptide (6.25 uM)
CC       (PubMed:28108242, PubMed:30974767). Has low hemolytic activity (MIC=50
CC       uM) (PubMed:28108242) (By similarity). Is also cytotoxic to mouse
CC       peritoneal macrophages (EC(50)=13.19 uM) (PubMed:28108242). Also causes
CC       moderate mast cell degranulation (ED(50)=80 uM) and exhibits
CC       chemotactic activity for polymorphonucleated leukocytes (PMNL) (By
CC       similarity). In vivo, shows antistaphylococcal activity (S.aureus) with
CC       a decline bacterial load after 6 days of topical treatment
CC       (PubMed:28108242). {ECO:0000250|UniProtKB:P84915,
CC       ECO:0000269|PubMed:28108242, ECO:0000269|PubMed:30974767}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28108242}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P84915}. Note=Forms an alpha-
CC       helical membrane channel in the prey. {ECO:0000250|UniProtKB:P84915}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:28108242}.
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 VP13a from Polybia paulista (AC P84915).
CC       {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; IEA:UniProtKB-SubCell.
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: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   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="Polybia-MPII"
FT                   /evidence="ECO:0000269|PubMed:28108242"
FT                   /id="PRO_0000455166"
FT   MOD_RES         14
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:28108242"
SQ   SEQUENCE   14 AA;  1614 MW;  2209239FD56ABE38 CRC64;
     INWLKLGKMV IDAL