ID   ASI1A_MACAT             Reviewed;          51 AA.
AC   P0DQI8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=U-Asilidin(1)-Mar1a {ECO:0000303|PubMed:29303983};
DE   Flags: Precursor;
OS   Machimus arthriticus (Breck robberfly) (Asilus arthriticus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Asiloidea;
OC   Asilidae; Asilinae; Machimus.
OX   NCBI_TaxID=1936065;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=29303983; DOI=10.3390/toxins10010029;
RA   Drukewitz S.H., Fuhrmann N., Undheim E.A.B., Blanke A., Giribaldi J.,
RA   Mary R., Laconde G., Dutertre S., von Reumont B.M.;
RT   "A Dipteran's novel sucker punch: evolution of arthropod atypical venom
RT   with a neurotoxic component in robber fliezs (Asilidae, Diptera).";
RL   Toxins 10:0-0(2018).
CC   -!- FUNCTION: Induces neurotoxic effect on honeybees, including slow
CC       movements, disorientation and paralysis (PubMed:29303983). Since it
CC       provokes similar symptoms than omega-atracotoxin, it is probable that
CC       it acts in the same way by inhibiting voltage-gated calcium channels.
CC       {ECO:0000269|PubMed:29303983, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29303983}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. Is the most highly
CC       expressed peptide and is around 3000 times higher expressed in the
CC       thoracic glands compared to its body tissues.
CC       {ECO:0000305|PubMed:29303983}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000305|PubMed:29303983}.
CC   -!- SIMILARITY: Belongs to the asilidin-1 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC       (NCBI);
CC       URL="https://www.ncbi.nlm.nih.gov/nuccore/GFZQ00000000";
CC   -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC       (NCBI);
CC       URL="https://www.ncbi.nlm.nih.gov/nuccore/GFFZ00000000";
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DR   AlphaFoldDB; P0DQI8; -.
DR   SMR; P0DQI8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..51
FT                   /note="U-Asilidin(1)-Mar1a"
FT                   /id="PRO_0000448210"
FT   DISULFID        26..40
FT                   /evidence="ECO:0000305|PubMed:29303983"
FT   DISULFID        33..44
FT                   /evidence="ECO:0000305|PubMed:29303983"
FT   DISULFID        39..49
FT                   /evidence="ECO:0000305|PubMed:29303983"
SQ   SEQUENCE   51 AA;  5519 MW;  9CA737C00781757E CRC64;
     MANYIEVFSV LAIIFATVLA ALAQDCSPEG AQCVRDSECC YNECIDSLCQ P