ID   ICK30_TRILK             Reviewed;         116 AA.
AC   W4VS15;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=U16-barytoxin-Tl1c;
DE            Short=U16-BATX-Tl1c;
DE   AltName: Full=Toxin ICK-30 {ECO:0000303|PubMed:24351713};
DE   Flags: Precursor;
OS   Trittame loki (Brush-footed trapdoor spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Barychelidae; Trittame.
OX   NCBI_TaxID=1295018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24351713; DOI=10.3390/toxins5122488;
RA   Undheim E.A., Sunagar K., Herzig V., Kely L., Low D.H., Jackson T.N.,
RA   Jones A., Kurniawan N., King G.F., Ali S.A., Antunes A., Ruder T.,
RA   Fry B.G.;
RT   "A proteomics and transcriptomics investigation of the venom from the
RT   barychelid spider Trittame loki (brush-foot trapdoor).";
RL   Toxins 5:2488-2503(2013).
CC   -!- FUNCTION: Ion channel inhibitor. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 06 (ICK-Trit)
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GAQE01000033; JAB84521.1; -; Transcribed_RNA.
DR   AlphaFoldDB; W4VS15; -.
DR   ArachnoServer; AS001717; U16-barytoxin-Tl1c.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012627; Toxin_22.
DR   Pfam; PF08092; Toxin_22; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..74
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000435153"
FT   CHAIN           75..116
FT                   /note="U16-barytoxin-Tl1c"
FT                   /id="PRO_0000429237"
FT   DISULFID        75..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..110
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   116 AA;  12988 MW;  D83BBC7134375810 CRC64;
     MKTIIVFLSL LVLATKFGDA NEGVNQEQMK EVIQNEFRED FLNEMAAMSL LQQLEAIEST
     LLEKEADRNS RQKRCNGKNV PCGSNHSPCC SGLSCEETFG YGWLYKSPYC VIPSNG