OSM_OSMRU
ID OSM_OSMRU Reviewed; 17 AA.
AC P0CD70;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Osmin;
OS Osmia rufa (Red mason bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Megachilidae; Megachilinae; Osmia.
OX NCBI_TaxID=1437190;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, AMIDATION AT VAL-17, AND
RP SYNTHESIS.
RC TISSUE=Venom;
RX PubMed=19109988; DOI=10.1016/j.toxicon.2008.12.011;
RA Stocklin R., Favreau P., Thai R., Pflugfelder J., Bulet P., Mebs D.;
RT "Structural identification by mass spectrometry of a novel antimicrobial
RT peptide from the venom of the solitary bee Osmia rufa (hymenoptera:
RT megachilidae).";
RL Toxicon 55:20-27(2010).
CC -!- FUNCTION: Synthetic peptide exhibits hemolytic activities (less than
CC melittin) and inhibits bacterial (M.luteus and E.coli) and fungal
CC (F.oxysporum) growth at micromolar concentrations. A synthetic peptide
CC with a free C-terminus shows weaker hemolytic, antibacterial and
CC antifungal activities. {ECO:0000269|PubMed:19109988}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=1924.20; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19109988};
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 AlphaFoldDB; P0CD70; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW Fungicide; Hemolysis; Secreted; Toxin.
FT PEPTIDE 1..17
FT /note="Osmin"
FT /id="PRO_0000391364"
FT MOD_RES 17
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:19109988"
SQ SEQUENCE 17 AA; 1926 MW; 84184CCE1E83C64D CRC64;
GFLSALKKYL PIVLKHV