MASP3_POLPI
ID MASP3_POLPI Reviewed; 14 AA.
AC P84914;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Venom protein 13b {ECO:0000303|PubMed:15150833};
DE Short=VP13b {ECO:0000305|PubMed:15150833};
DE AltName: Full=Polybia-MP-III {ECO:0000303|PubMed:19463874};
DE AltName: Full=Polybia-MPIII {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, SUBCELLULAR LOCATION, AMIDATION AT LEU-14, AND
RP 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).
CC -!- FUNCTION: Antimicrobial peptide (PubMed:19463874). Is active against
CC both Gram-negative and -positive bacteria (Escherichia coli (MIC=38
CC uM), Pseudomonas aeruginosa (MIC=310 uM), Staphylococcus aureus (MIC=19
CC uM), and Bacillus cereus (MIC=38 uM)) (PubMed:19463874). Also causes
CC moderate mast cell degranulation (ED(50)=100 uM) and low hemolysis
CC (MIC=50 uM) (PubMed:15150833, PubMed:19463874). Exhibits chemotactic
CC activity for polymorphonucleated leukocytes (PMNL) (PubMed:15150833,
CC PubMed:19463874). {ECO:0000269|PubMed:15150833,
CC ECO:0000269|PubMed:19463874}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15150833,
CC ECO:0000269|PubMed:19463874}. Target cell membrane
CC {ECO:0000305|PubMed:19463874}. Note=Forms amphipathic alpha-helical
CC conformations under membrane-mimetic conditions.
CC {ECO:0000305|PubMed:19463874}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15150833}.
CC -!- MASS SPECTROMETRY: Mass=1658.60; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15150833};
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IDA:UniProtKB.
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; Chemotaxis; Cytolysis; Direct protein sequencing;
KW Mast cell degranulation; Membrane; Secreted; Target cell membrane;
KW Target membrane; Toxin.
FT PEPTIDE 1..14
FT /note="Venom protein 13b"
FT /evidence="ECO:0000269|PubMed:15150833"
FT /id="PRO_0000248507"
FT MOD_RES 14
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:15150833"
SQ SEQUENCE 14 AA; 1661 MW; 221633991DC8BE38 CRC64;
IDWLKLGKMV MDVL