ID   ASC3B_DOLGE             Reviewed;          69 AA.
AC   A0A3G5BIB1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=U-Asilidin(12)-Dg3b {ECO:0000303|PubMed:30400621};
DE   Flags: Precursor;
OS   Dolopus genitalis (Giant Australian assassin fly) (Asilus genitalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Asilidae; Asilinae; Dolopus.
OX   NCBI_TaxID=2488630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=30400621; DOI=10.3390/toxins10110456;
RA   Walker A.A., Dobson J., Jin J., Robinson S.D., Herzig V., Vetter I.,
RA   King G.F., Fry B.G.;
RT   "Buzz kill: function and proteomic composition of venom from the giant
RT   assassin fly Dolopus genitalis (Diptera: Asilidae).";
RL   Toxins 10:E456-E456(2018).
RN   [2] {ECO:0007744|PDB:6PX8}
RP   STRUCTURE BY NMR OF 34-69, FUNCTION, DISULFIDE BONDS, RECOMBINANT
RP   EXPRESSION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=31870846; DOI=10.1016/j.ibmb.2019.103310;
RA   Jin J., Agwa A.J., Szanto T.G., Csoti A., Panyi G., Schroeder C.I.,
RA   Walker A.A., King G.F.;
RT   "Weaponisation 'on the fly': convergent recruitment of knottin and defensin
RT   peptide scaffolds into the venom of predatory assassin flies.";
RL   Insect Biochem. Mol. Biol. 118:103310-103310(2020).
CC   -!- FUNCTION: The recombinant peptide moderately increases
CC       Kv11.1/KCNH2/ERG1 currents and shifts the voltage-dependence of the
CC       channel activation to hyperpolarised potentials (PubMed:31870846). In
CC       vivo, induces neurotoxic effects when injected into insects (tested on
CC       L.cuprina and A.domesticus) (PubMed:31870846).
CC       {ECO:0000269|PubMed:31870846}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30400621,
CC       ECO:0000269|PubMed:31870846}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:30400621, ECO:0000305|PubMed:31870846}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305|PubMed:30400621}.
CC   -!- MASS SPECTROMETRY: Mass=4073.85; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:30400621};
CC   -!- MASS SPECTROMETRY: Mass=4073.59; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:31870846};
CC   -!- MISCELLANEOUS: Is abundant in venom, since it accounts for 45.2% of
CC       precursor counts. {ECO:0000269|PubMed:30400621}.
CC   -!- MISCELLANEOUS: The recombinant peptide contains an extra Gly residue at
CC       N-terminal position. {ECO:0000269|PubMed:31870846}.
CC   -!- MISCELLANEOUS: The recombinant peptide has no effect on Kv1.3/KCNA3,
CC       Kv2.1/KCNB1, Kv10.1/KCNH1/EAG1, KCa1.1/KCNMA1, or the drosophila Shaker
CC       IR channel. {ECO:0000269|PubMed:31870846}.
CC   -!- SIMILARITY: Belongs to the asilidin-12 family. {ECO:0000305}.
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DR   EMBL; MK075121; AYV99524.1; -; mRNA.
DR   PDB; 6PX8; NMR; -; A=34-69.
DR   PDBsum; 6PX8; -.
DR   AlphaFoldDB; A0A3G5BIB1; -.
DR   BMRB; A0A3G5BIB1; -.
DR   SMR; A0A3G5BIB1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:UniProt.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..33
FT                   /evidence="ECO:0000305|PubMed:30400621"
FT                   /id="PRO_0000452537"
FT   CHAIN           34..69
FT                   /note="U-Asilidin(12)-Dg3b"
FT                   /evidence="ECO:0000269|PubMed:30400621"
FT                   /id="PRO_5018247767"
FT   DISULFID        36..59
FT                   /evidence="ECO:0000269|PubMed:31870846,
FT                   ECO:0007744|PDB:6PX8"
FT   DISULFID        45..65
FT                   /evidence="ECO:0000269|PubMed:31870846,
FT                   ECO:0007744|PDB:6PX8"
FT   DISULFID        49..67
FT                   /evidence="ECO:0000269|PubMed:31870846,
FT                   ECO:0007744|PDB:6PX8"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:6PX8"
FT   HELIX           43..52
FT                   /evidence="ECO:0007829|PDB:6PX8"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:6PX8"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:6PX8"
SQ   SEQUENCE   69 AA;  7939 MW;  94B4FFA19BFA9AA0 CRC64;
     MRFLNIFLFF AVMIAFVSAS PVLEEEEIDI EPRITCDLIG NERLCVVHCL AKGFRGGWCD
     SRKVCNCRR