ID   MAST_VESBA              Reviewed;          14 AA.
AC   P21654;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   02-JUN-2021, entry version 47.
DE   RecName: Full=Mastoparan-B;
OS   Vespa basalis (Hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7444;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT LEU-14.
RC   TISSUE=Venom;
RX   PubMed=2006909; DOI=10.1042/bj2740453;
RA   Lo C.-L., Hwang L.-L.;
RT   "Structure and biological activities of a new mastoparan isolated from the
RT   venom of the hornet Vespa basalis.";
RL   Biochem. J. 274:453-456(1991).
CC   -!- FUNCTION: Mast cell degranulating peptide. Activates G proteins that
CC       couple to phospholipase C.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC       {ECO:0000305}.
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DR   PIR; S14336; S14336.
DR   TCDB; 1.C.32.1.7; the amphipathic peptide mastoparan (mastoparan) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Mast cell degranulation; Secreted.
FT   PEPTIDE         1..14
FT                   /note="Mastoparan-B"
FT                   /id="PRO_0000044058"
FT   MOD_RES         14
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:2006909"
SQ   SEQUENCE   14 AA;  1613 MW;  D35944CA193A19A2 CRC64;
     LKLKSIVSWA KKVL