ID   EUMER_EUMRB             Reviewed;          15 AA.
AC   P0CJ36;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Eumenitin-R {ECO:0000303|PubMed:21549739};
OS   Eumenes rubrofemoratus (Solitary wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Eumeninae; Eumenes.
OX   NCBI_TaxID=1035770;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND CIRCULAR DICHROISM.
RC   TISSUE=Venom;
RX   PubMed=21549739; DOI=10.1016/j.toxicon.2011.04.014;
RA   Rangel M., Dos Santos Cabrera M.P., Kazuma K., Ando K., Wang X., Kato M.,
RA   Nihei K.I., Hirata I.Y., Cross T.J., Garcia A.N., Faquim-Mauro E.L.,
RA   Franzolin M.R., Fuchino H., Mori-Yasumoto K., Sekita S., Kadowaki M.,
RA   Satake M., Konno K.;
RT   "Chemical and biological characterization of four new linear cationic
RT   alpha-helical peptides from the venoms of two solitary eumenine wasps.";
RL   Toxicon 57:1081-1092(2011).
RN   [2]
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).
CC   -!- FUNCTION: Linear cationic alpha-helical peptide that acts as
CC       antimicrobial peptide by forming pore in membrane. Has antibacterial
CC       activities against both Gram-positive and Gram-negative strains. Has
CC       more potent activities against the yeast C.albicans. Shows moderate
CC       mast cell degranulation and leishmanicidal activities. Has a very low
CC       hemolytic activity. {ECO:0000269|PubMed:21549739}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21549739}. Target
CC       cell membrane {ECO:0000269|PubMed:21549739}. 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       {ECO:0000269|PubMed:21549739}.
CC   -!- MASS SPECTROMETRY: Mass=1623.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21549739};
CC   -!- SIMILARITY: Belongs to the MCD family. Eumenitin subfamily.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW   Ion transport; Mast cell degranulation; Membrane; Secreted;
KW   Target cell membrane; Target membrane; Transmembrane; Transport.
FT   PEPTIDE         1..15
FT                   /note="Eumenitin-R"
FT                   /evidence="ECO:0000269|PubMed:21549739"
FT                   /id="PRO_0000411087"
SQ   SEQUENCE   15 AA;  1624 MW;  49340CF644E26B4F CRC64;
     LNLKGLIKKV ASLLN