ID   EUME_EUMRU              Reviewed;          15 AA.
AC   P0C931;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   29-SEP-2021, entry version 23.
DE   RecName: Full=Eumenitin {ECO:0000303|PubMed:16762455, ECO:0000303|PubMed:18206199};
DE   AltName: Full=Er-12 {ECO:0000303|PubMed:11006592};
OS   Eumenes rubronotatus (Solitary wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Eumeninae; Eumenes.
OX   NCBI_TaxID=539890;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, AND IDENTIFICATION BY 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, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   SYNTHESIS.
RC   TISSUE=Venom;
RX   PubMed=16762455; DOI=10.1016/j.peptides.2006.04.013;
RA   Konno K., Hisada M., Naoki H., Itagaki Y., Fontana R., Rangel M.,
RA   Oliveira J.S., dos Santos Cabrera M.P., Neto J.R., Hide I., Nakata Y.,
RA   Yasuhara T., Nakajima T.;
RT   "Eumenitin, a novel antimicrobial peptide from the venom of the solitary
RT   eumenine wasp Eumenes rubronotatus.";
RL   Peptides 27:2624-2631(2006).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=18206199; DOI=10.1016/j.toxicon.2007.11.023;
RA   Arcisio-Miranda M., dos Santos Cabrera M.P., Konno K., Rangel M.,
RA   Procopio J.;
RT   "Effects of the cationic antimicrobial peptide eumenitin from the venom of
RT   solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge
RT   and pore formation activity.";
RL   Toxicon 51:736-745(2008).
CC   -!- FUNCTION: Cationic linear alpha-helical antimicrobial peptide that
CC       binds preferentially to charged lipid membranes as compared with
CC       zwitterionic ones. It exhibits inhibitory activity against both Gram-
CC       positive and Gram-negative bacteria, and moderately stimulates
CC       degranulation from the rat peritoneal mast cells. Does not show
CC       hemolytic activity. May play a role in preventing infection by
CC       microorganisms during prey consumption by their larvae.
CC       {ECO:0000269|PubMed:16762455, ECO:0000269|PubMed:18206199}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16762455}. Target
CC       cell membrane {ECO:0000269|PubMed:16762455}. Note=Assumes an
CC       amphipathic alpha-helical conformation in a lipid environment. Forms a
CC       membrane channel in the prey.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=1644.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16762455};
CC   -!- SIMILARITY: Belongs to the MCD family. Eumenitin subfamily.
CC       {ECO:0000305}.
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DR   TCDB; 1.C.32.2.2; the amphipathic peptide mastoparan (mastoparan) family.
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:0006811; P:ion transport; 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; Ion transport;
KW   Mast cell degranulation; Membrane; Secreted; Target cell membrane;
KW   Target membrane; Transmembrane; Transport.
FT   PEPTIDE         1..15
FT                   /note="Eumenitin"
FT                   /id="PRO_0000370686"
SQ   SEQUENCE   15 AA;  1645 MW;  50235DF644E26B4F CRC64;
     LNLKGIFKKV ASLLT