ID   MAS2B_EUMPO             Reviewed;          63 AA.
AC   D1MEI8;
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 2b {ECO:0000303|PubMed:20096300};
DE            Short=EpVP2b {ECO:0000303|PubMed:20096300};
DE            Short=VP2b {ECO:0000312|EMBL:ACZ37394.1};
DE   AltName: Full=Eumenine mastoparan VP2b {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], AND PROBABLE AMIDATION AT LEU-62.
RC   TISSUE=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).
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:P0CJ38}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20096300}. Target
CC       cell membrane {ECO:0000250|UniProtKB:P0CJ38}. 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   -!- MISCELLANEOUS: May be a minor component of E.pomiformis venom.
CC       {ECO:0000305|PubMed:20096300}.
CC   -!- SIMILARITY: Belongs to the MCD family. Mastoparan subfamily.
CC       {ECO:0000305}.
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DR   EMBL; GU136233; ACZ37394.1; -; 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_0000453661"
FT   PEPTIDE         49..62
FT                   /note="Venom peptide 2b"
FT                   /evidence="ECO:0000305|PubMed:20096300"
FT                   /id="PRO_5003024564"
FT   MOD_RES         62
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000305|PubMed:20096300"
SQ   SEQUENCE   63 AA;  6495 MW;  BF921EF19AF35E23 CRC64;
     MRGTSFILFA VVVILGFLHG NAEPLANPEP SANPDPLANP DPLANPEAFD LLGLVKSVVS
     ALG