ID   CRBL_VESCR              Reviewed;          13 AA.
AC   P01518;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Crabrolin;
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-13.
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).
RN   [2]
RP   SYNTHESIS, AND ANTIMICROBIAL ACTIVITY.
RX   PubMed=9273892; DOI=10.1111/j.1399-3011.1997.tb01173.x;
RA   Krishnakumari V., Nagaraj R.;
RT   "Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide
RT   from the venom of the European hornet, Vespa crabro, and its analogs.";
RL   J. Pept. Res. 50:88-93(1997).
CC   -!- FUNCTION: Mast cell degranulating peptide. Induces the chemotaxis of
CC       neutrophils. Has antimicrobial and hemolytic activity.
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   PIR; A01781; JZVHP1.
DR   PDB; 6TWG; NMR; -; A=1-13.
DR   PDBsum; 6TWG; -.
DR   SMR; P01518; -.
DR   TCDB; 1.C.32.3.1; the amphipathic peptide mastoparan (mastoparan) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; 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   3D-structure; Amidation; Antibiotic; Antimicrobial; Chemotaxis; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Mast cell degranulation; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Crabrolin"
FT                   /id="PRO_0000044045"
FT   MOD_RES         13
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:6206053"
FT   HELIX           3..12
FT                   /evidence="ECO:0007829|PDB:6TWG"
SQ   SEQUENCE   13 AA;  1497 MW;  515EF8FCEA8D2407 CRC64;
     FLPLILRKIV TAL