ID   CRBL_VESMA              Reviewed;          13 AA.
AC   P17232;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   02-JUN-2021, entry version 49.
DE   RecName: Full=Vespid chemotactic peptide M;
DE            Short=VESCP-M;
DE            Short=Ves-CP-M;
OS   Vespa mandarinia (Asian giant hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7446;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT LEU-13.
RC   TISSUE=Venom;
RA   Yasuhara T., Nakajima T., Fukuda K., Tsukamoto Y., Mori M., Kitada C.,
RA   Fujino M.;
RL   (In) Munekata E. (eds.);
RL   Peptide chemistry 1983, pp.185-190, Protein Research Foundation, Osaka
RL   (1984).
CC   -!- FUNCTION: Mast cell degranulating peptide. Induces the chemotaxis of
CC       neutrophils.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the MCD family. Crabrolin subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Chemotaxis; Direct protein sequencing; Mast cell degranulation;
KW   Secreted.
FT   PEPTIDE         1..13
FT                   /note="Vespid chemotactic peptide M"
FT                   /id="PRO_0000044047"
FT   MOD_RES         13
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   13 AA;  1384 MW;  2650402B9DF92338 CRC64;
     FLPIIGKLLS GLL