ID   CT1B_CORTR              Reviewed;          82 AA.
AC   P0DL78;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=U1-theraphotoxin-Ct1b {ECO:0000303|PubMed:27793656};
DE            Short=U1-TRTX-Ct1b {ECO:0000303|PubMed:27793656};
DE   Flags: Precursor;
OS   Coremiocnemis tropix (Australian tarantula spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Coremiocnemis.
OX   NCBI_TaxID=1904443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=27793656; DOI=10.1016/j.toxicon.2016.10.013;
RA   Ikonomopoulou M.P., Smith J.J., Herzig V., Pineda S.S., Dziemborowicz S.,
RA   Er S.Y., Durek T., Gilchrist J., Alewood P.F., Nicholson G.M., Bosmans F.,
RA   King G.F.;
RT   "Isolation of two insecticidal toxins from venom of the Australian
RT   theraphosid spider Coremiocnemis tropix.";
RL   Toxicon 123:62-70(2016).
CC   -!- FUNCTION: This toxin causes paralysis and death to sheep blowflies. It
CC       does not target insect sodium channels. {ECO:0000250|UniProtKB:P0DL77,
CC       ECO:0000250|UniProtKB:P0DL81}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27793656}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:27793656}.
CC   -!- PTM: Contains 3 disulfide bonds. Two different connectivities are
CC       observed in similar proteins (C1-C3, C2-C5, C4-C6 or C1-C4, C2-C5, C3-
CC       C6). {ECO:0000305|PubMed:27793656}.
CC   -!- MASS SPECTROMETRY: Mass=4239.675; Method=MALDI; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:27793656};
CC   -!- MISCELLANEOUS: No effect of the synthetic peptide are observed on
CC       voltage-gated sodium channels from the American cockroach Periplanata
CC       americana or the German cockroach Blattella germanica.
CC       {ECO:0000250|UniProtKB:P0DL77}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 03 (juruin)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DL78; -.
DR   SMR; P0DL78; -.
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.
DR   InterPro; IPR012625; Toxin_20.
DR   Pfam; PF08089; Toxin_20; 1.
DR   PROSITE; PS60022; HWTX_2; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..44
FT                   /evidence="ECO:0000269|PubMed:27793656"
FT                   /id="PRO_0000442237"
FT   CHAIN           45..82
FT                   /note="U1-theraphotoxin-Ct1b"
FT                   /evidence="ECO:0000269|PubMed:27793656"
FT                   /id="PRO_0000442238"
SQ   SEQUENCE   82 AA;  9137 MW;  140E1A2CB9C8764F CRC64;
     MRTFTLIAIL TCALLVIYHA AEAEELEAKD VIESKALATL DEERFECSLS CDIKKNGKPC
     KGSGEKKCSG GWRCKMNFCL KF