TX17A_ODOMO
ID TX17A_ODOMO Reviewed; 68 AA.
AC A0A348G6I9;
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)-Om4b {ECO:0000250|UniProtKB:A0A348G5W2};
DE Short=U-PONTX(01)-Om4b {ECO:0000250|UniProtKB:A0A348G5W2};
DE AltName: Full=Pilosulin-like peptide 7 {ECO:0000312|EMBL:BBF98062.1};
DE Short=PLP7 {ECO:0000250|UniProtKB:A0A348G6I7};
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].
RC TISSUE=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 MASS SPECTROMETRY, 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, S.aureus
CC (MIC=3.1 uM), and S.cerevisiae (MIC=3.1 uM). It also shows histamine-
CC releasing activity (66.4% at 10 uM) and a weak hemolytic activity
CC (10.5% at 50 uM). {ECO:0000250|UniProtKB:A0A348G5W0}.
CC -!- SUBUNIT: Homo- or heterodimer with PLP4 (AC A0A348G5W0); disulfide-
CC linked. {ECO:0000269|PubMed:30658410}.
CC -!- SUBCELLULAR LOCATION: Secreted {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=3241.79; Method=Electrospray; Note=in reducing
CC conditions, Monoisotopic mass.; Evidence={ECO:0000269|PubMed:30658410};
CC -!- MASS SPECTROMETRY: Mass=6367.6; Method=Electrospray; Note=Homodimer,
CC Monoisotopic mass.; Evidence={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}.
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; LC416796; BBF98062.1; -; mRNA.
DR AlphaFoldDB; A0A348G6I9; -.
DR SMR; A0A348G6I9; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..39
FT /evidence="ECO:0000305"
FT /id="PRO_0000447075"
FT PEPTIDE 40..68
FT /note="U-poneritoxin(01)-Om4b"
FT /evidence="ECO:0000269|PubMed:30658410"
FT /id="PRO_5016855820"
FT DISULFID 60
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:30658410"
SQ SEQUENCE 68 AA; 7308 MW; 74BD77C278CE6BD3 CRC64;
MKPSGLTLAF LVVFMMAIMY NSVQAEALAD ADAEAFAEAG VKELFGKAWG LVKKHLPKAC
GLMGYVKQ
