TX2A_MYRPI
ID TX2A_MYRPI Reviewed; 75 AA.
AC Q26464;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=M-myrmeciitoxin-Mp2a {ECO:0000303|PubMed:26805882};
DE Short=M-MIITX-Mp2a {ECO:0000303|PubMed:26805882};
DE AltName: Full=Allergen Myr p II {ECO:0000303|PubMed:8605256};
DE AltName: Full=DELTA-myrtoxin-Mp1a A chain {ECO:0000303|PubMed:28513074, ECO:0000303|PubMed:32629771};
DE Short=Mp1a A chain {ECO:0000303|PubMed:28513074, ECO:0000303|PubMed:32629771};
DE AltName: Full=Pilosin-3 subunit a {ECO:0000305};
DE Short=Pilosulin-3a {ECO:0000303|PubMed:26805882, ECO:0000305};
DE AltName: Full=Pilosulin-2 {ECO:0000303|PubMed:15019477};
DE AltName: Allergen=Myr p 2 {ECO:0000303|PubMed:8605256};
DE Flags: Precursor;
OS Myrmecia pilosula (Jack jumper ant) (Australian jumper ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmeciinae; Myrmeciini; Myrmecia.
OX NCBI_TaxID=13618;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-54, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=8605256; DOI=10.1016/0167-4781(95)00197-2;
RA Street M.D., Donovan G.R., Baldo B.A.;
RT "Molecular cloning and characterization of the major allergen Myr p II from
RT the venom of the jumper ant Myrmecia pilosula: Myr p I and Myr p II share a
RT common protein leader sequence.";
RL Biochim. Biophys. Acta 1305:87-97(1996).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=8866004; DOI=10.1080/15216549600201022;
RA Donovan G.R., Street M.D., Tetaz T., Smith A.I., Alewood D., Alewood P.F.,
RA Sutherland S.K., Baldo B.A.;
RT "Expression of jumper ant (Myrmecia pilosula) venom allergens: post-
RT translational processing of allergen gene products.";
RL Biochem. Mol. Biol. Int. 39:877-885(1996).
RN [3]
RP AMIDATION AT LEU-74, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=15019477; DOI=10.1016/j.toxicon.2003.11.021;
RA Davies N.W., Wiese M.D., Brown S.G.A.;
RT "Characterisation of major peptides in 'jack jumper' ant venom by mass
RT spectrometry.";
RL Toxicon 43:173-183(2004).
RN [4]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=26805882; DOI=10.3390/toxins8010030;
RA Touchard A., Aili S.R., Fox E.G., Escoubas P., Orivel J., Nicholson G.M.,
RA Dejean A.;
RT "The biochemical toxin arsenal from ant venoms.";
RL Toxins 8:1-28(2016).
RN [5]
RP FUNCTION, SYNTHESIS OF 49-74 IN COMPLEX WITH B CHAIN, BIOASSAY, AND TOXIC
RP DOSE.
RX PubMed=32629771; DOI=10.3390/biomedicines8070185;
RA Nixon S.A., Dekan Z., Robinson S.D., Guo S., Vetter I., Kotze A.C.,
RA Alewood P.F., King G.F., Herzig V.;
RT "It takes two: dimerization is essential for the broad-spectrum predatory
RT and defensive activities of the venom peptide Mp1a from the jack jumper ant
RT Myrmecia pilosula.";
RL Biomedicines 8:0-0(2020).
RN [6]
RP STRUCTURE BY NMR OF 49-74 IN COMPLEX WITH B CHAIN, FUNCTION, SYNTHESIS OF
RP 49-74 IN COMPLEX WITH B CHAIN, AND BIOASSAY.
RX PubMed=28513074; DOI=10.1002/anie.201703360;
RA Dekan Z., Headey S.J., Scanlon M., Baldo B.A., Lee T.H., Aguilar M.I.,
RA Deuis J.R., Vetter I., Elliott A.G., Amado M., Cooper M.A., Alewood D.,
RA Alewood P.F.;
RT "Delta-myrtoxin-Mp1a is a helical heterodimer from the venom of the jack
RT jumper ant that has antimicrobial, membrane-disrupting, and nociceptive
RT activities.";
RL Angew. Chem. Int. Ed. 56:8495-8499(2017).
CC -!- FUNCTION: Heterodimer protein that may serve both defensive (pain-
CC inducing) and predatory (insecticidal) roles (PubMed:28513074). Has
CC membrane-disrupting activity and shows induction of non-specific
CC calcium influx into cells, (PubMed:28513074). Shows broad-spectrum
CC activity against a diverse range of bacteria, and cell lines, as well
CC as hemolytic activity (EC(50)=2.18 uM) (PubMed:28513074). In vivo,
CC shows moderate insecticidal activity against D.melanogaster and potent
CC anthelmintic activity against the veterinary nematode H.contortus
CC (PubMed:32629771). In addition, intraplantar injection into mice
CC induces nocifensive behavior and mechanical allodynia
CC (PubMed:28513074). {ECO:0000269|PubMed:28513074,
CC ECO:0000269|PubMed:32629771}.
CC -!- SUBUNIT: Heterodimer with M-MIITX-Mp2b (pilosin-3b) (AC P0C023);
CC disulfide-linked (PubMed:8866004, PubMed:15019477). Only heterodimers
CC (and not monomers) have been identified in the venom (PubMed:15019477).
CC {ECO:0000269|PubMed:15019477, ECO:0000269|PubMed:8866004}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8605256}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8605256}.
CC -!- ALLERGEN: The heterodimer causes an allergic reaction in human. Binds
CC to IgE. It is speculated that the antigenic site is on the A chain.
CC {ECO:0000269|PubMed:15019477}.
CC -!- TOXIC DOSE: LD(50) of the heterodimer is 260.1 +- 16.6 pmol/g towards
CC D.melanogaster. {ECO:0000269|PubMed:32629771}.
CC -!- MISCELLANEOUS: Dekan et al., 2017 and Nixon et al., 2020 report
CC synthesis and functional analysis of heterodimers with different
CC disulfide patterns as well as different A and B chain monomeric forms.
CC {ECO:0000305|PubMed:28513074, ECO:0000305|PubMed:32629771}.
CC -!- SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily.
CC Ant pilosulin family. {ECO:0000305}.
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DR EMBL; S81785; AAB36316.1; -; mRNA.
DR PIR; S65711; S65711.
DR AlphaFoldDB; Q26464; -.
DR Allergome; 3381; Myr p 2.0101.
DR Allergome; 3575; Myr p 2.0102.
DR Allergome; 481; Myr p 2.
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 Allergen; Amidation; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Hemolysis; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..48
FT /evidence="ECO:0000305|PubMed:8605256"
FT /id="PRO_0000035164"
FT PEPTIDE 49..74
FT /note="M-myrmeciitoxin-Mp2a"
FT /evidence="ECO:0000305|PubMed:8605256"
FT /id="PRO_0000035165"
FT MOD_RES 74
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:15019477"
FT DISULFID 64
FT /note="Interchain (with C-17 in M-MIITX-Mp2b)"
FT /evidence="ECO:0000269|PubMed:15019477"
FT DISULFID 71
FT /note="Interchain (with C-10 in M-MIITX-Mp2b)"
FT /evidence="ECO:0000269|PubMed:15019477"
SQ SEQUENCE 75 AA; 8145 MW; 4FFE49969405F7AC CRC64;
MKLSCLLLTL AIIFVLTIVH APNVEAKALA DPESDAVGFA DAVGEADPID WKKVDWKKVS
KKTCKVMLKA CKFLG
