AS1C_DOLGE
ID AS1C_DOLGE Reviewed; 80 AA.
AC A0A3G5BIC2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=U-Asilidin(1)-Dg12 {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:6PX7}
RP STRUCTURE BY NMR OF 47-80, 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: Neurotoxin that may modulate ions channels (other than those
CC tested) (PubMed:31870846). In vivo, induces neurotoxic effects when
CC injected into insects (tested on L.cuprina and A.domesticus)
CC (PubMed:31870846). {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: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:31870846}.
CC -!- MASS SPECTROMETRY: Mass=3906.6; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:30400621};
CC -!- MASS SPECTROMETRY: Mass=3906.80; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:31870846};
CC -!- MISCELLANEOUS: The recombinant peptide has no effect on Kv1.3/KCNA3,
CC Kv10.1/KCNH1/EAG1, Kv11.1/KCNH2/ERG1, KCa1.1/KCNMA1, and on the
CC drosophila Shaker IR channel. {ECO:0000269|PubMed:31870846}.
CC -!- SIMILARITY: Belongs to the asilidin-1 family. {ECO:0000305}.
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DR EMBL; MK075130; AYV99533.1; -; mRNA.
DR PDB; 6PX7; NMR; -; A=47-80.
DR PDBsum; 6PX7; -.
DR AlphaFoldDB; A0A3G5BIC2; -.
DR BMRB; A0A3G5BIC2; -.
DR SMR; A0A3G5BIC2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Ion channel impairing toxin; Knottin;
KW Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..46
FT /evidence="ECO:0000305|PubMed:30400621"
FT /id="PRO_0000452538"
FT CHAIN 47..80
FT /note="U-Asilidin(1)-Dg12"
FT /evidence="ECO:0000269|PubMed:30400621"
FT /id="PRO_5018286706"
FT DISULFID 53..67
FT /evidence="ECO:0000269|PubMed:31870846,
FT ECO:0007744|PDB:6PX7"
FT DISULFID 60..71
FT /evidence="ECO:0000269|PubMed:31870846,
FT ECO:0007744|PDB:6PX7"
FT DISULFID 66..78
FT /evidence="ECO:0000269|PubMed:31870846,
FT ECO:0007744|PDB:6PX7"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6PX7"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6PX7"
SQ SEQUENCE 80 AA; 8756 MW; 2348295A9E1DA9FD CRC64;
MARLLVVSVG VFLAVIMLSS ETMSLPAGEN LPALTLFEAQ NQLIGLSQEQ RQCKKIGEHC
YVADECCSKR CLFYAAKCVS