ID   TXI3_ERAAG              Reviewed;          68 AA.
AC   O46168;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=U1-agatoxin-Ta1c;
DE            Short=U1-AGTX-Ta1c;
DE   AltName: Full=Insecticidal toxin 3 {ECO:0000303|PubMed:9589602};
DE            Short=TaITX-3 {ECO:0000303|PubMed:9589602};
DE   Flags: Precursor;
OS   Eratigena agrestis (Hobo spider) (Tegenaria agrestis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Agelenidae; Eratigena.
OX   NCBI_TaxID=1686644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-27, AMIDATION AT LYS-67,
RP   MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=9589602;
RX   DOI=10.1002/(sici)1520-6327(1998)38:1<19::aid-arch3>3.0.co;2-q;
RA   Johnson J.H., Bloomquist J.R., Krapcho K.J., Kral R.M. Jr., Trovato R.,
RA   Eppler K.G., Morgan T.K., Delmar E.G.;
RT   "Novel insecticidal peptides from Tegenaria agrestis spider venom may have
RT   a direct effect on the insect central nervous system.";
RL   Arch. Insect Biochem. Physiol. 38:19-31(1998).
CC   -!- FUNCTION: Toxin that paralyzes insects. May have a direct effect on the
CC       insect central nervous system. {ECO:0000269|PubMed:9589602}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9589602}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9589602}.
CC   -!- DOMAIN: Comprises exclusively 4 tightly packed alpha helices (no beta
CC       strand is present). {ECO:0000250|UniProtKB:O46166}.
CC   -!- MASS SPECTROMETRY: Mass=5643.09; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9589602};
CC   -!- MISCELLANEOUS: Arose via modification of ancestral neuropeptide
CC       hormones (ion transport peptide/crustacean hyperglycemic hormones
CC       (ITP/CHH)). {ECO:0000250|UniProtKB:O46166}.
CC   -!- SIMILARITY: Belongs to the helical arthropod-neuropeptide-derived
CC       (HAND) family. {ECO:0000305}.
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DR   EMBL; AJ224129; CAA11841.1; -; mRNA.
DR   AlphaFoldDB; O46168; -.
DR   SMR; O46168; -.
DR   ArachnoServer; AS000351; U1-agatoxin-Ta1c.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:9589602"
FT   CHAIN           18..67
FT                   /note="U1-agatoxin-Ta1c"
FT                   /id="PRO_0000035557"
FT   MOD_RES         67
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:9589602"
FT   DISULFID        23..53
FT                   /evidence="ECO:0000250|UniProtKB:O46166"
FT   DISULFID        39..49
FT                   /evidence="ECO:0000250|UniProtKB:O46166"
FT   DISULFID        42..62
FT                   /evidence="ECO:0000250|UniProtKB:O46166"
SQ   SEQUENCE   68 AA;  7705 MW;  8EC9F34D6664126D CRC64;
     MKLQLMICLV LLPCFFCEPD EICRARMTNK EFTYKSNVCN GCGDQVAACE AECFRNDVYT
     ACHEAQKG