TXM4E_DINQU
ID TXM4E_DINQU Reviewed; 69 AA.
AC P0DSK2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=M-poneratoxin-Dq4e {ECO:0000303|PubMed:28976889};
DE Short=M-PONTX-Dq4e {ECO:0000303|PubMed:28976889};
DE AltName: Full=Peptide sDq-3348 {ECO:0000303|PubMed:28976889};
DE AltName: Full=U-poneritoxin(01)-Dq7a {ECO:0000305};
DE Short=PONTX(01)-Dq7 (contig 1) {ECO:0000303|PubMed:30214940};
DE Short=U-PONTX(01)-Dq7a {ECO:0000305};
DE AltName: Full=contig 9 {ECO:0000303|PubMed:24498135};
DE Flags: Precursor;
OS Dinoponera quadriceps (South American ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Dinoponera.
OX NCBI_TaxID=609295;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=24498135; DOI=10.1371/journal.pone.0087556;
RA Torres A.F., Huang C., Chong C.M., Leung S.W., Prieto-da-Silva A.R.,
RA Havt A., Quinet Y.P., Martins A.M., Lee S.M., Radis-Baptista G.;
RT "Transcriptome analysis in venom gland of the predatory giant ant
RT Dinoponera quadriceps: insights into the polypeptide toxin arsenal of
RT hymenopterans.";
RL PLoS ONE 9:E87556-E87556(2014).
RN [2]
RP FUNCTION, AND SYNTHESIS OF 40-69.
RX PubMed=28976889; DOI=10.1515/hsz-2017-0198;
RA Lima D.B., Mello C.P., Bandeira I.C.J., Pessoa Bezerra de Menezes R.R.P.,
RA Sampaio T.L., Falcao C.B., Morlighem J.R.L., Radis-Baptista G.,
RA Martins A.M.C.;
RT "The dinoponeratoxin peptides from the giant ant Dinoponera quadriceps
RT display in vitro antitrypanosomal activity.";
RL Biol. Chem. 399:187-196(2018).
RN [3]
RP NOMENCLATURE.
RX PubMed=30214940; DOI=10.1126/sciadv.aau4640;
RA Robinson S.D., Mueller A., Clayton D., Starobova H., Hamilton B.R.,
RA Payne R.J., Vetter I., King G.F., Undheim E.A.B.;
RT "A comprehensive portrait of the venom of the giant red bull ant, Myrmecia
RT gulosa, reveals a hyperdiverse hymenopteran toxin gene family.";
RL Sci. Adv. 4:EAAU4640-EAAU4640(2018).
CC -!- FUNCTION: May have antimicrobial properties, like most ant linear
CC peptides (Probable). In addition, when tested in vitro on the parasite
CC Trypanosoma cruzi (responsible of the Chagas disease), is able to
CC moderately reduce the number of the three forms (epimastigote,
CC trypomastigote and amastigote) by inducing cell death through necrosis
CC (PubMed:28976889). {ECO:0000269|PubMed:28976889, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24498135}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24498135}.
CC -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC (NCBI);
CC URL="https://www.ncbi.nlm.nih.gov/nuccore/GANS01000002";
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DR AlphaFoldDB; P0DSK2; -.
DR SMR; P0DSK2; -.
DR Proteomes; UP000515204; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 3: Inferred from homology;
KW Antimicrobial; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..39
FT /evidence="ECO:0000305|PubMed:24498135"
FT /id="PRO_0000447087"
FT PEPTIDE 40..69
FT /note="M-poneratoxin-Dq4e"
FT /evidence="ECO:0000305|PubMed:24498135"
FT /id="PRO_0000447088"
SQ SEQUENCE 69 AA; 7398 MW; 9AC463F87B4D0A2C CRC64;
MKLSAFTLAF ALILMMAIMY NMAEAAALAD ADADAEAIAG LKDWWNKHKD KIVKVVKEMG
KAGINAAGK