SCXI_TITBA
ID SCXI_TITBA Reviewed; 63 AA.
AC P60275;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Insect toxin TbIT-1;
DE AltName: Full=P-Ins-beta* NaTx4.3;
DE AltName: Full=TbIT-I;
OS Tityus bahiensis (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=50343;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=11223090; DOI=10.1016/s0041-0101(00)00240-3;
RA Pimenta A.M.C., Martin-Eauclaire M.-F., Rochat H., Figueiredo S.G.,
RA Kalapothakis E., Afonso L.C.C., De Lima M.E.;
RT "Purification, amino-acid sequence and partial characterization of two
RT toxins with anti-insect activity from the venom of the South American
RT scorpion Tityus bahiensis (Buthidae).";
RL Toxicon 39:1009-1019(2001).
RN [2]
RP NOMENCLATURE.
RX PubMed=22355312; DOI=10.1371/journal.pone.0030478;
RA Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D.,
RA Schwartz E.F.;
RT "Identification and phylogenetic analysis of Tityus pachyurus and Tityus
RT obscurus novel putative Na+-channel scorpion toxins.";
RL PLoS ONE 7:E30478-E30478(2012).
CC -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing (By similarity). This toxin is only
CC active against insects. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=6813.34; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11223090};
CC -!- TOXIC DOSE: LD(50) is 80.0 ng/house fly. {ECO:0000269|PubMed:11223090}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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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 GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..63
FT /note="Insect toxin TbIT-1"
FT /id="PRO_0000066796"
FT DOMAIN 2..63
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 24..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 28..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 63 AA; 6821 MW; 3F6D6527A369AFE2 CRC64;
GKEGYPVDSR GCKVTCFFTG AGYCDKECKL KKASSGYCAW PACYCYGLPD SVPVYDNASN
KCB
