MAST1_VESVU
ID MAST1_VESVU Reviewed; 15 AA.
AC P0C1Q8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 02-JUN-2021, entry version 16.
DE RecName: Full=Mastoparan-V1;
OS Vespula vulgaris (Yellow jacket) (Wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespula.
OX NCBI_TaxID=7454;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=12759486; DOI=10.1159/000070431;
RA King T.P., Jim S.Y., Wittkowski K.M.;
RT "Inflammatory role of two venom components of yellow jackets (Vespula
RT vulgaris): a mast cell degranulating peptide mastoparan and phospholipase
RT A1.";
RL Int. Arch. Allergy Immunol. 131:25-32(2003).
CC -!- FUNCTION: Chemotactic peptide for polymorphonucleated leukocytes
CC (PMNL), but causing no hemolysis to erythrocytes and no mast cell
CC degranulation activity at physiological concentrations. Potent
CC antimicrobial peptide against Gram-positive and Gram-negative bacteria
CC (By similarity). {ECO:0000250}.
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 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:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Chemotaxis;
KW Direct protein sequencing; Mast cell degranulation; Secreted.
FT PEPTIDE 1..15
FT /note="Mastoparan-V1"
FT /id="PRO_0000247267"
FT MOD_RES 15
FT /note="Asparagine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 15 AA; 1758 MW; 93BBE82237A7FC68 CRC64;
INWKKIKSII KAAMN