CRBLF_VESMG
ID CRBLF_VESMG Reviewed; 13 AA.
AC P0C1M2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Vespid chemotactic peptide 5f;
DE Short=VCP 5f;
OS Vespa magnifica (Hornet).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespa.
OX NCBI_TaxID=202807;
RN [1]
RP PROTEIN SEQUENCE, AND MINIMAL INHIBITORY CONCENTRATION.
RC TISSUE=Venom;
RX PubMed=16330062; DOI=10.1016/j.toxicon.2005.10.015;
RA Xu X., Li J., Lu Q., Yang H., Zhang Y., Lai R.;
RT "Two families of antimicrobial peptides from wasp (Vespa magnifica)
RT venom.";
RL Toxicon 47:249-253(2006).
CC -!- FUNCTION: Mast cell degranulating peptide (By similarity). Has little
CC hemolytic activity. Shows antimicrobial activity against the Gram-
CC negative bacteria E.coli ATCC 25922 (MIC=30 ug/ml), the Gram-positive
CC bacteria S.aureus ATCC 2592 (MIC=10 ug/ml) and the fungus C.albicans
CC ATCC 2002 (MIC=25 ug/ml). {ECO:0000250}.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; 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 Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Fungicide; Hemolysis; Mast cell degranulation; Secreted.
FT PEPTIDE 1..13
FT /note="Vespid chemotactic peptide 5f"
FT /id="PRO_0000246008"
FT MOD_RES 13
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 13 AA; 1462 MW; 786D40390DFE4774 CRC64;
FLPIPRPILL GLL