ID   TX21A_MYRGU             Reviewed;          80 AA.
AC   P0DSL4;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=U-myrmeciitoxin(02)-Mg1a {ECO:0000305};
DE            Short=MIITX(02)-Mg1a {ECO:0000303|PubMed:30214940};
DE            Short=U-MIITX(02)-Mg1a {ECO:0000305};
DE   Flags: Precursor;
OS   Myrmecia gulosa (Red bulldog ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmeciinae; Myrmeciini; Myrmecia.
OX   NCBI_TaxID=36170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
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: Unknown. Does not cause cytolysis since the toxin does not
CC       cause a change in calcium concentration in DRG cells.
CC       {ECO:0000269|PubMed:30214940}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30214940}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:30214940}.
CC   -!- MASS SPECTROMETRY: Mass=5787.37; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:30214940};
CC   -!- SIMILARITY: Belongs to the EGF domain peptide family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC       (NCBI);
CC       URL="https://www.ncbi.nlm.nih.gov/nuccore/GGFG01000015";
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DR   PDB; 7R6P; NMR; -; A=31-80.
DR   PDBsum; 7R6P; -.
DR   AlphaFoldDB; P0DSL4; -.
DR   SMR; P0DSL4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; EGF-like domain; Secreted; Signal; Toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..30
FT                   /evidence="ECO:0000305|PubMed:30214940"
FT                   /id="PRO_0000447108"
FT   CHAIN           31..80
FT                   /note="U-myrmeciitoxin(02)-Mg1a"
FT                   /evidence="ECO:0000269|PubMed:30214940"
FT                   /id="PRO_0000447109"
FT   DOMAIN          35..75
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        39..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        47..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        65..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   80 AA;  9099 MW;  5ED1BD17D998E0C0 CRC64;
     MKNNYISTCI VYLMAALLLI SVISIKECTA DISDYGDPCS DDLKDYCIHG DCFFLKELNQ
     PACRCYTGYY GSRCEHIDHN