ID   ASC3A_DOLGE             Reviewed;          69 AA.
AC   A0A3G5BIB4;
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)-Dg3a {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).
CC   -!- FUNCTION: Moderately increases Kv11.1/KCNH2/ERG1 currents and shifts
CC       the voltage-dependence of the channel activation to hyperpolarised
CC       potentials (By similarity). In vivo, induces neurotoxic effects when
CC       injected into insects (tested on L.cuprina and A.domesticus) (By
CC       similarity). {ECO:0000250|UniProtKB:A0A3G5BIB1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30400621}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:30400621}.
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=4057.85; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:30400621};
CC   -!- MISCELLANEOUS: Is abundant in venom, since it accounts for 45.2% of
CC       precursor counts. {ECO:0000269|PubMed:30400621}.
CC   -!- SIMILARITY: Belongs to the asilidin-12 family. {ECO:0000305}.
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DR   EMBL; MK075120; AYV99523.1; -; mRNA.
DR   AlphaFoldDB; A0A3G5BIB4; -.
DR   SMR; A0A3G5BIB4; -.
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   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_0000452536"
FT   CHAIN           34..69
FT                   /note="U-Asilidin(12)-Dg3a"
FT                   /evidence="ECO:0000269|PubMed:30400621"
FT                   /id="PRO_5018045393"
FT   DISULFID        36..59
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G5BIB1"
FT   DISULFID        45..65
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G5BIB1"
FT   DISULFID        49..67
FT                   /evidence="ECO:0000250|UniProtKB:A0A3G5BIB1"
SQ   SEQUENCE   69 AA;  7932 MW;  A58A07CDE09524C6 CRC64;
     MRFLNIFLFF AAIIAFATAS QVFEEDEIDM EPRITCDLIG NERLCVLHCL AKGFRGGWCD
     GRKVCNCRR