ID   TXI1_ERAAG              Reviewed;          68 AA.
AC   O46166;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=U1-agatoxin-Ta1a {ECO:0000303|PubMed:26073605};
DE            Short=U1-AGTX-Ta1a {ECO:0000303|PubMed:26073605};
DE   AltName: Full=Insecticidal toxin 1 {ECO:0000303|PubMed:9589602};
DE            Short=TaITX-1 {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 18-58, MASS SPECTROMETRY,
RP   TOXIC DOSE, 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).
RN   [2]
RP   STRUCTURE BY NMR OF 18-67, AMIDATION AT LYS-67, DOMAIN, DISULFIDE BONDS,
RP   AND TOXIC DOSE.
RX   PubMed=26073605; DOI=10.1016/j.str.2015.05.003;
RA   Undheim E.A., Grimm L.L., Low C.F., Morgenstern D., Herzig V.,
RA   Zobel-Thropp P., Pineda S.S., Habib R., Dziemborowicz S., Fry B.G.,
RA   Nicholson G.M., Binford G.J., Mobli M., King G.F.;
RT   "Weaponization of a hormone: convergent recruitment of hyperglycemic
RT   hormone into the venom of arthropod predators.";
RL   Structure 23:1283-1292(2015).
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: Is exclusively composed of 4 tightly packed alpha helices (no
CC       beta strand is present). {ECO:0000269|PubMed:26073605}.
CC   -!- MASS SPECTROMETRY: Mass=5678.55; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9589602};
CC   -!- TOXIC DOSE: LD(50) is 198 +- 33 pmol/g when injected into the ventro-
CC       lateral thoracic region of adult blowflies (L.cuprina) (at 24 hours
CC       post-injection) (PubMed:26073605). {ECO:0000269|PubMed:26073605}.
CC   -!- TOXIC DOSE: PD(50) is 0.89 nmol/g when injected into tobacco budworm
CC       (PubMed:9589602). {ECO:0000269|PubMed:9589602}.
CC   -!- TOXIC DOSE: PD(50) is 0.78 nmol/g when injected into cabbage looper
CC       (PubMed:9589602). {ECO:0000269|PubMed:9589602}.
CC   -!- TOXIC DOSE: PD(50) is 0.9 nmol/g when injected into beet army worm
CC       (PubMed:9589602). {ECO:0000269|PubMed:9589602}.
CC   -!- TOXIC DOSE: PD(50) is 2.0 nmol/g when injected into Southern corn
CC       rootworm (PubMed:9589602). {ECO:0000269|PubMed:9589602}.
CC   -!- MISCELLANEOUS: Arose via modification of ancestral neuropeptide
CC       hormones (ion transport peptide/crustacean hyperglycemic hormones
CC       (ITP/CHH)). {ECO:0000305|PubMed:26073605}.
CC   -!- SIMILARITY: Belongs to the helical arthropod-neuropeptide-derived
CC       (HAND) family. {ECO:0000305|PubMed:26073605}.
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DR   EMBL; AJ224127; CAA11839.1; -; mRNA.
DR   PDB; 2KSL; NMR; -; A=18-67.
DR   PDB; 6URP; NMR; -; A=18-67.
DR   PDBsum; 2KSL; -.
DR   PDBsum; 6URP; -.
DR   AlphaFoldDB; O46166; -.
DR   BMRB; O46166; -.
DR   SMR; O46166; -.
DR   ArachnoServer; AS000349; U1-agatoxin-Ta1a.
DR   EvolutionaryTrace; O46166; -.
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   3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:9589602"
FT   CHAIN           18..67
FT                   /note="U1-agatoxin-Ta1a"
FT                   /id="PRO_0000035555"
FT   MOD_RES         67
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:26073605"
FT   DISULFID        23..53
FT                   /evidence="ECO:0000269|PubMed:26073605"
FT   DISULFID        39..49
FT                   /evidence="ECO:0000269|PubMed:26073605"
FT   DISULFID        42..62
FT                   /evidence="ECO:0000269|PubMed:26073605"
FT   HELIX           21..26
FT                   /evidence="ECO:0007829|PDB:2KSL"
FT   HELIX           29..42
FT                   /evidence="ECO:0007829|PDB:2KSL"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:2KSL"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:6URP"
FT   HELIX           57..64
FT                   /evidence="ECO:0007829|PDB:2KSL"
SQ   SEQUENCE   68 AA;  7741 MW;  19578D59D92FF268 CRC64;
     MKLQLMICLV LLPCFFCEPD EICRARMTHK EFNYKSNVCN GCGDQVAACE AECFRNDVYT
     ACHEAQKG