ID   TX14A_ODOMO             Reviewed;          68 AA.
AC   A0A348G5W0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=U-poneritoxin(01)-Om4a {ECO:0000250|UniProtKB:A0A348G5W2};
DE            Short=U-PONTX(01)-Om4a {ECO:0000250|UniProtKB:A0A348G5W2};
DE   AltName: Full=Pilosulin-like peptide 4 {ECO:0000312|EMBL:BBF97833.1};
DE            Short=PLP4 {ECO:0000303|PubMed:29027956};
DE   AltName: Full=Poneratoxin {ECO:0000305};
DE   Flags: Precursor;
OS   Odontomachus monticola (Trap-jaw ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Odontomachus.
OX   NCBI_TaxID=613454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=29027956; DOI=10.3390/toxins9100323;
RA   Kazuma K., Masuko K., Konno K., Inagaki H.;
RT   "Combined venom gland transcriptomic and venom peptidomic analysis of the
RT   predatory ant Odontomachus monticola.";
RL   Toxins 9:323-323(2017).
RN   [2]
RP   FUNCTION, MASS SPECTROMETRY, SYNTHESIS OF PEPTIDE WITH UNKNOWN TERMINAL
RP   RESIDUES, SUBUNIT, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=30658410; DOI=10.3390/toxins11010050;
RA   Tani N., Kazuma K., Ohtsuka Y., Shigeri Y., Masuko K., Konno K.,
RA   Inagaki H.;
RT   "Mass spectrometry analysis and biological characterization of the
RT   predatory ant Odontomachus monticola venom and venom sac components.";
RL   Toxins 11:0-0(2019).
CC   -!- FUNCTION: This homodimer composed of two cationic amphipathic alpha-
CC       helical peptides has antimicrobial activities against E.coli (MIC=3.1
CC       uM), S.aureus (MIC=3.1 uM), and S.cerevisiae (MIC=3.1 uM).It also shows
CC       histamine-releasing activity (66.4% at 10 uM) and a weak hemolytic
CC       activity (10.5% at 50 uM). {ECO:0000269|PubMed:30658410}.
CC   -!- SUBUNIT: Homo- or heterodimer with PLP7 (AC A0A348G6I9); disulfide-
CC       linked. {ECO:0000269|PubMed:29027956, ECO:0000269|PubMed:30658410}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29027956,
CC       ECO:0000269|PubMed:30658410}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29027956}.
CC   -!- PTM: Truncated sequences of this peptide have also been found in the
CC       venom. It is possible they have been cleaved in the venom.
CC       {ECO:0000305|PubMed:30658410}.
CC   -!- MASS SPECTROMETRY: Mass=3223.8; Method=Electrospray; Note=in reducing
CC       conditions, Monoisotopic mass.; Evidence={ECO:0000269|PubMed:30658410};
CC   -!- MASS SPECTROMETRY: Mass=6331.6; Method=Electrospray; Note=Homodimer,
CC       Monoisotopic mass.; Evidence={ECO:0000269|PubMed:29027956,
CC       ECO:0000269|PubMed:30658410};
CC   -!- MASS SPECTROMETRY: Mass=6349.6; Method=Electrospray; Note=Heterodimer,
CC       Monoisotopic mass.; Evidence={ECO:0000269|PubMed:30658410};
CC   -!- SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily.
CC       {ECO:0000305}.
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DR   EMBL; FX985497; BBF97833.1; -; mRNA.
DR   AlphaFoldDB; A0A348G5W0; -.
DR   SMR; A0A348G5W0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Antibiotic; Antimicrobial; Cytolysis; Disulfide bond; Fungicide; Hemolysis;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..39
FT                   /evidence="ECO:0000305|PubMed:29027956"
FT                   /id="PRO_0000447073"
FT   PEPTIDE         40..68
FT                   /note="U-poneritoxin(01)-Om4a"
FT                   /evidence="ECO:0000269|PubMed:30658410"
FT                   /id="PRO_5016599850"
FT   DISULFID        60
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:29027956,
FT                   ECO:0000269|PubMed:30658410"
SQ   SEQUENCE   68 AA;  7320 MW;  697D6A1FB8CFDBC7 CRC64;
     MKPSSLTLAF LVVFMMAIMY NSVQAEALAD ADAEAFAEAG VKELFGKAWG LVKKHLPKAC
     GLLGYVKQ