ID   MAST_VESCR              Reviewed;          14 AA.
AC   P01516;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Mastoparan-C;
OS   Vespa crabro (European hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7445;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT LEU-14.
RC   TISSUE=Venom;
RX   PubMed=6206053; DOI=10.1016/s0021-9258(18)90935-x;
RA   Argiolas A., Pisano J.J.;
RT   "Isolation and characterization of two new peptides, mastoparan C and
RT   crabrolin, from the venom of the European hornet, Vespa crabro.";
RL   J. Biol. Chem. 259:10106-10111(1984).
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; A01779; QMVHP2.
DR   TCDB; 1.C.32.1.5; 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.
DR   InterPro; IPR013213; Mastoparan.
DR   Pfam; PF08249; Mastoparan; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Mast cell degranulation; Secreted.
FT   PEPTIDE         1..14
FT                   /note="Mastoparan-C"
FT                   /id="PRO_0000044059"
FT   MOD_RES         14
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:6206053"
SQ   SEQUENCE   14 AA;  1508 MW;  550C0ECA1D6AB1D7 CRC64;
     LNLKALLAVA KKIL