ID   MAST_ANTFM              Reviewed;          14 AA.
AC   P0C022;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Eumenine mastoparan-AF {ECO:0000303|PubMed:10775751};
DE            Short=EMP-AF {ECO:0000303|PubMed:10775751};
DE   AltName: Full=Af-113 {ECO:0000303|PubMed:11006592};
OS   Anterhynchium flavomarginatum micado (Solitary wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Eumeninae; Anterhynchium.
OX   NCBI_TaxID=329991;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-14, SYNTHESIS, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11006592;
RX   DOI=10.1002/1097-0231(20001015)14:19<1828::aid-rcm101>3.0.co;2-g;
RA   Hisada M., Konno K., Itagaki Y., Naoki H., Nakajima T.;
RT   "Advantages of using nested collision induced dissociation/post-source
RT   decay with matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry: sequencing of novel peptides from wasp venom.";
RL   Rapid Commun. Mass Spectrom. 14:1828-1834(2000).
RN   [2]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10775751; DOI=10.1016/s0041-0101(00)00083-0;
RA   Konno K., Hisada M., Naoki H., Itagaki Y., Kawai N., Miwa A., Yasuhara T.,
RA   Morimoto Y., Nakata Y.;
RT   "Structure and biological activities of eumenine mastoparan-AF (EMP-AF), a
RT   new mast cell degranulating peptide in the venom of the solitary wasp
RT   (Anterhynchium flavomarginatum micado).";
RL   Toxicon 38:1505-1515(2000).
RN   [3]
RP   SYNTHESIS, FUNCTION, AND MINIMAL INHIBITORY CONCENTRATION.
RX   PubMed=15317499; DOI=10.1111/j.1399-3011.2004.00173.x;
RA   dos Santos Cabrera M.P., de Souza B.M., Fontana R., Konno K., Palma M.S.,
RA   de Azevedo W.F. Jr., Neto J.R.;
RT   "Conformation and lytic activity of eumenine mastoparan: a new
RT   antimicrobial peptide from wasp venom.";
RL   J. Pept. Res. 64:95-103(2004).
RN   [4]
RP   REVIEW.
RX   PubMed=27096870; DOI=10.3390/toxins8040114;
RA   Konno K., Kazuma K., Nihei K.;
RT   "Peptide toxins in solitary wasp venoms.";
RL   Toxins 8:114-114(2016).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=11053843; DOI=10.1107/s0907444900009719;
RA   Canduri F., Delatorre P., Fadel V., Lorenzi C.C.B., Pereira J.H.,
RA   Olivieri J.R., Ruggiero Neto J., Konno K., Palma M.S., Yamane T.,
RA   de Azevedo W.F. Jr.;
RT   "Crystallization and preliminary X-ray diffraction analysis of a eumenine
RT   mastoparan toxin: a new class of mast-cell degranulating peptide in the
RT   wasp venom.";
RL   Acta Crystallogr. D 56:1434-1436(2000).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=11342062; DOI=10.1016/s0167-4838(00)00192-8;
RA   Delatorre P., Olivieri J.R., Ruggiero Neto J., Lorenzi C.C.B., Canduri F.,
RA   Fadel V., Konno K., Palma M.S., Yamane T., de Azevedo W.F. Jr.;
RT   "Preliminary cryocrystallography analysis of an eumenine mastoparan toxin
RT   isolated from the venom of the wasp Anterhynchium flavomarginatum micado.";
RL   Biochim. Biophys. Acta 1545:372-376(2001).
CC   -!- FUNCTION: Mast cell degranulating peptide. Also permeates anionic
CC       liposomes. Has little hemolytic activity. Has an amphiphilic alpha-
CC       helix conformation. Shows broad-spectrum antimicrobial activity against
CC       the Gram-positive bacteria S.aureus ATCC 6538 (MIC=5 ug/ml),
CC       S.saprophyticus CS (MIC=5 ug/ml), S.epidermidis CS (MIC=5 ug/ml),
CC       B.subtilis CCT 2471 (MIC=40 ug/ml), and the Gram-negative bacteria
CC       E.coli CCT 1371 (MIC=20 ug/ml), E.coli ATCC 25922 (MIC=50 ug/ml), and
CC       P.aeruginosa ATCC 15442 (MIC=20 ug/ml). Blocks the lobster
CC       neuromuscular transmission. Induces the depolarization of the muscle
CC       membrane. {ECO:0000269|PubMed:10775751, ECO:0000269|PubMed:15317499}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane. Note=Assumes an
CC       amphipathic alpha-helical conformation in a lipid environment. Forms a
CC       membrane channel in the prey (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=1523; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10775751};
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:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; 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   Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Mast cell degranulation; Membrane; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Target cell membrane; Target membrane;
KW   Toxin.
FT   PEPTIDE         1..14
FT                   /note="Eumenine mastoparan-AF"
FT                   /id="PRO_0000044052"
FT   MOD_RES         14
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:11006592"
SQ   SEQUENCE   14 AA;  1524 MW;  C8404A1270F45E3D CRC64;
     INLLKIAKGI IKSL