EUME1_EUMPO
ID EUME1_EUMPO Reviewed; 63 AA.
AC D1MEI6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Venom peptide 1 {ECO:0000303|PubMed:20096300};
DE Short=EpVP1 {ECO:0000303|PubMed:20096300};
DE Short=VP1 {ECO:0000312|EMBL:ACZ37392.1};
DE AltName: Full=Eumenitin VP1 {ECO:0000305};
DE Flags: Precursor;
OS Eumenes pomiformis (Potter wasp) (Vespa pomiformis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Eumeninae; Eumenes.
OX NCBI_TaxID=693051;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20096300; DOI=10.1016/j.toxicon.2010.01.004;
RA Baek J.H., Lee S.H.;
RT "Differential gene expression profiles in the venom gland/sac of Eumenes
RT pomiformis (Hymenoptera: Eumenidae).";
RL Toxicon 55:1147-1156(2010).
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:0000250|UniProtKB:P0CJ36}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20096300}. Target
CC cell membrane {ECO:0000250|UniProtKB:P0CJ36}. Note=Assumes an
CC amphipathic alpha-helical conformation in a lipid environment.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:20096300}.
CC -!- MASS SPECTROMETRY: Mass=1610.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20096300};
CC -!- SIMILARITY: Belongs to the MCD family. Eumenitin 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 EMBL; GU136231; ACZ37392.1; -; mRNA.
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:0019835; P:cytolysis; 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 Amidation; Antibiotic; Antimicrobial; Cytolysis; Fungicide; Ion transport;
KW Mast cell degranulation; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane; Transmembrane; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /evidence="ECO:0000305|PubMed:20096300"
FT /id="PRO_0000453659"
FT PEPTIDE 49..63
FT /note="Venom peptide 1"
FT /evidence="ECO:0000269|PubMed:20096300"
FT /id="PRO_5003025094"
SQ SEQUENCE 63 AA; 6546 MW; FC582451B3B5984C CRC64;
MRGTSFILFA VVVILGFLHA NAEPLANPAP LANPDPLANA DPLADPEAIN LKGLIKKVAS
LLT