ID   MAST_VESLE              Reviewed;          14 AA.
AC   P01514;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 79.
DE   RecName: Full=Mastoparan-L {ECO:0000303|PubMed:540362};
OS   Vespula lewisii (Korean yellow-jacket wasp) (Vespula flaviceps lewisii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespula.
OX   NCBI_TaxID=7452;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-14, AND SYNTHESIS.
RC   TISSUE=Venom;
RX   PubMed=540362; DOI=10.1248/cpb.27.1942;
RA   Hirai Y., Yasuhara T., Yoshida H., Nakajima T., Fujino M., Kitada C.;
RT   "A new mast cell degranulating peptide 'mastoparan' in the venom of Vespula
RT   lewisii.";
RL   Chem. Pharm. Bull. 27:1942-1944(1979).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=11168364; DOI=10.1046/j.1432-1033.2001.01880.x;
RA   Hori Y., Demura M., Iwadate M., Ulrich A.S., Niidome T., Aoyagi H.,
RA   Asakura T.;
RT   "Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in
RT   detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in
RT   oriented lipid bilayers.";
RL   Eur. J. Biochem. 268:302-309(2001).
CC   -!- FUNCTION: Mast cell degranulating peptide. Activates G proteins that
CC       couple to phospholipase C. May be able to switch from an in-plane to a
CC       transmembrane orientation in lipid bilayers.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane {ECO:0000305}.
CC       Note=Forms a membrane channel in the prey. {ECO:0000305}.
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; A01776; QMWAVV.
DR   PDB; 1D7N; NMR; -; A=1-14.
DR   PDB; 6DUL; NMR; -; A=1-14.
DR   PDB; 6DUU; NMR; -; A=1-14.
DR   PDBsum; 1D7N; -.
DR   PDBsum; 6DUL; -.
DR   PDBsum; 6DUU; -.
DR   BMRB; P01514; -.
DR   SMR; P01514; -.
DR   TCDB; 1.C.32.1.6; the amphipathic peptide mastoparan (mastoparan) family.
DR   EvolutionaryTrace; P01514; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   3D-structure; Amidation; Direct protein sequencing;
KW   Mast cell degranulation; Membrane; Secreted; Target cell membrane;
KW   Target membrane; Toxin; Transmembrane.
FT   PEPTIDE         1..14
FT                   /note="Mastoparan-L"
FT                   /evidence="ECO:0000269|PubMed:540362"
FT                   /id="PRO_0000044060"
FT   MOD_RES         14
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:540362"
FT   HELIX           4..11
FT                   /evidence="ECO:0007829|PDB:1D7N"
SQ   SEQUENCE   14 AA;  1480 MW;  CC0C0ECA1D7B00DD CRC64;
     INLKALAALA KKIL