SCX17_TITSE
ID SCX17_TITSE Reviewed; 86 AA.
AC A0A7S8MU55;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Putative sodium channel toxin Ts17 {ECO:0000303|PubMed:33181162};
DE AltName: Full=Putative alpha-NaTx {ECO:0000303|PubMed:33181162};
DE AltName: Full=Putative alpha-toxin {ECO:0000303|Ref.1};
DE AltName: Full=Tityustoxin-17 {ECO:0000305|PubMed:33181162};
DE Flags: Precursor;
OS Tityus serrulatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=6887;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX DOI=10.4236/ojgen.2012.24027;
RA Alvarenga E.R., Mendes T.M., Magalhaes B.F., Siqueira F.F., Dantas A.E.,
RA Barroca T.M., Horta C.C., Kalapothakis E.;
RT "Transcriptome analysis of the Tityus serrulatus scorpion venom gland.";
RL O. J. Gen. 2:210-220(2012).
RN [2] {ECO:0000312|EMBL:QPD99021.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Telson;
RX PubMed=33181162; DOI=10.1016/j.toxicon.2020.11.001;
RA Kalapothakis Y., Miranda K., Pereira A.H., Witt A.S.A., Marani C.,
RA Martins A.P., Leal H.G., Campos-Junior E., Pimenta A.M.C., Borges A.,
RA Chavez-Olortegui C., Kalapothakis E.;
RT "Novel components of Tityus serrulatus venom: a transcriptomic approach.";
RL Toxicon 189:91-104(2021).
CC -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC channels (Nav) and inhibit the inactivation of the activated channels,
CC thereby blocking neuronal transmission. {ECO:0000250|UniProtKB:P01496}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33181162}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:33181162}.
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 -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000305}.
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DR EMBL; MT081339; QPD99021.1; -; mRNA.
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:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR CDD; cd00107; Knot1; 1.
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 3: Inferred from homology;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..83
FT /note="Putative sodium channel toxin Ts17"
FT /evidence="ECO:0000305"
FT /id="PRO_5031227619"
FT DOMAIN 21..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 83
FT /note="Proline amide"
FT /evidence="ECO:0000305"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 43..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 86 AA; 9605 MW; 1D2883ABC75B3D2D CRC64;
MNYFIFLVVA CLLTAGTEGK KDGYPVEGDN CAFACFGYDN AYCDKLCKDK KADSGYCYWV
HILCYCYGLP DKEPTKTSGR CKPGKK
