MASTA_POLDO
ID MASTA_POLDO Reviewed; 17 AA.
AC P0C1M6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Dominulin-A;
OS Polistes dominula (European paper wasp) (Vespa dominula).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Polistini; Polistes.
OX NCBI_TaxID=743375;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SYNTHESIS,
RP AMIDATION AT LEU-17, MASS SPECTROMETRY, AND MINIMAL INHIBITORY
RP CONCENTRATION.
RC TISSUE=Cuticle, and Venom;
RX PubMed=16446098; DOI=10.1016/j.jasms.2005.11.017;
RA Turillazzi S., Mastrobuoni G., Dani F.R., Moneti G., Pieraccini G.,
RA la Marca G., Bartolucci G., Perito B., Lambardi D., Cavallini V.,
RA Dapporto L.;
RT "Dominulin A and B: two new antibacterial peptides identified on the
RT cuticle and in the venom of the social paper wasp Polistes dominulus using
RT MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap.";
RL J. Am. Soc. Mass Spectrom. 17:376-383(2006).
CC -!- FUNCTION: Shows antimicrobial activity against the Gram-positive
CC bacteria B.subtilis ATCC 6633 (MIC=2 ug/ml), and the Gram-negative
CC bacteria E.coli JM109 (MIC=8 ug/ml).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16446098}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. This peptide is also
CC found on female cuticle and nest paper. The venom could be the source
CC of these peptides, which could be spread all over the cuticle by the
CC frequent grooming movements of the female wasps.
CC {ECO:0000269|PubMed:16446098}.
CC -!- MASS SPECTROMETRY: Mass=1854.08; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16446098};
CC -!- MASS SPECTROMETRY: Mass=1854.11; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16446098};
CC -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0C1M6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Secreted.
FT PEPTIDE 1..17
FT /note="Dominulin-A"
FT /id="PRO_0000246012"
FT MOD_RES 17
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:16446098"
SQ SEQUENCE 17 AA; 1856 MW; DB9214E855ACDCEF CRC64;
INWKKIAEVG GKILSSL