TX12A_ODOMO
ID TX12A_ODOMO Reviewed; 81 AA.
AC A0A348G5V8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=U-poneritoxin(01)-Om2a {ECO:0000250|UniProtKB:A0A348G5W2};
DE Short=U-PONTX(01)-Om2a {ECO:0000250|UniProtKB:A0A348G5W2};
DE AltName: Full=Pilosulin-like peptide 2 {ECO:0000312|EMBL:BBF97831.1};
DE Short=PLP2 {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], PROTEIN SEQUENCE OF 48-66, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
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, IDENTIFICATION BY MASS SPECTROMETRY, SYNTHESIS OF PEPTIDE WITH
RP UNKNOWN TERMINAL RESIDUES, AND SUBCELLULAR LOCATION.
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: Cationic amphipathic alpha-helical peptide with antimicrobial
CC activities against E.coli (MIC=6.2 uM), S.aureus (MIC=6.2 uM), and
CC S.cerevisiae (MIC=50 uM). Also shows histamine-releasing activity
CC (30.1% at 10 uM) and a weak hemolytic activity (10.4% at 50 uM).
CC {ECO:0000269|PubMed:30658410}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29027956}.
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:29027956, ECO:0000305|PubMed:30658410}.
CC -!- MASS SPECTROMETRY: Mass=3361.756; Method=Electrospray;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:29027956};
CC -!- SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily.
CC {ECO:0000305}.
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DR EMBL; FX985495; BBF97831.1; -; mRNA.
DR AlphaFoldDB; A0A348G5V8; -.
DR SMR; A0A348G5V8; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..47
FT /evidence="ECO:0000305|PubMed:29027956"
FT /id="PRO_0000447069"
FT PEPTIDE 48..80
FT /note="U-poneritoxin(01)-Om2a"
FT /evidence="ECO:0000269|PubMed:30658410,
FT ECO:0000305|PubMed:29027956"
FT /id="PRO_5016905946"
SQ SEQUENCE 81 AA; 8379 MW; A671F81BD02BB427 CRC64;
MKPSGITFAF LVVFMMAIMY NSVQAAAIAD ADADAEAKAF ADAFAEAGWG SIFKTVGKMI
AKAAVKAAPE AISAMASQNE K