ID   MASTB_VESMG             Reviewed;          13 AA.
AC   P0C1M5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Mastoparan-like peptide 12b;
OS   Vespa magnifica (Hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=202807;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND MINIMAL INHIBITORY CONCENTRATION.
RC   TISSUE=Venom;
RX   PubMed=16330062; DOI=10.1016/j.toxicon.2005.10.015;
RA   Xu X., Li J., Lu Q., Yang H., Zhang Y., Lai R.;
RT   "Two families of antimicrobial peptides from wasp (Vespa magnifica)
RT   venom.";
RL   Toxicon 47:249-253(2006).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, AND AMIDATION AT LEU-13.
RX   PubMed=17046111; DOI=10.1016/j.peptides.2006.09.003;
RA   Xu X., Yang H., Yu H., Li J., Lai R.;
RT   "The mastoparanogen from wasp.";
RL   Peptides 27:3053-3057(2006).
CC   -!- FUNCTION: Mast cell degranulating peptide. Has little hemolytic
CC       activity. Shows antimicrobial activity against the Gram-negative
CC       bacteria E.coli ATCC 25922 (MIC=15 ug/ml), the Gram-positive bacteria
CC       S.aureus ATCC 2592 (MIC=3.7 ug/ml) and the fungus C.albicans ATCC 2002
CC       (MIC=7.5 ug/ml). {ECO:0000269|PubMed:17046111}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=1483.9; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:16330062};
CC   -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Fungicide; Hemolysis; Mast cell degranulation; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Mastoparan-like peptide 12b"
FT                   /id="PRO_0000246011"
FT   MOD_RES         13
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:17046111"
SQ   SEQUENCE   13 AA;  1486 MW;  1DE4C7A49AB0DDD0 CRC64;
     INWKGIAAMK KLL