ID   SCX1_TITTR              Reviewed;          84 AA.
AC   P0DMM8; A0A060BIT6;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Beta-mammal Tt1g;
DE   AltName: Full=T.trivittatus toxin 1 gamma-like;
DE   Flags: Precursor;
OS   Tityus trivittatus (Argentinean scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=369776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45, FUNCTION, AMIDATION
RP   AT CYS-81 TOXIC DOSE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24862827; DOI=10.1016/j.peptides.2014.05.002;
RA   Coronas F.I., Diego-Garcia E., Restano-Cassulini R., de Roodt A.R.,
RA   Possani L.D.;
RT   "Biochemical and physiological characterization of a new Na-channel
RT   specific peptide from the venom of the Argentinean scorpion Tityus
RT   trivittatus.";
RL   Peptides 68:11-16(2015).
CC   -!- FUNCTION: Beta toxins modify sodium channel function in two ways: an
CC       excitatory effect (shifting the activation process to more negative
CC       potential) and/or a depressant effect (reducing the peak current). At
CC       concentration of 500 nM this toxin produces channel opening at more
CC       negative potentials in hNav1.2/SCN2A and hNav1.3/SCN3A, which shows the
CC       biggest effect. On the other hand the peak current is decreased in
CC       hNav1.4/SCN4A and hNav1.5/SCN5A channels, without apparent modification
CC       of the activation gate. This toxin is active against mammals.
CC       {ECO:0000269|PubMed:24862827}.
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=6938.12; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:24862827};
CC   -!- TOXIC DOSE: LD(50) is 28.5 ug/kg by intracranial injection into mice.
CC   -!- MISCELLANEOUS: Does not produce significant modification of
CC       hNav1.1/SCN1A and hNav1.6/SCN8A currents.
CC       {ECO:0000305|PubMed:24862827}.
CC   -!- MISCELLANEOUS: This toxin is thought to be responsible for the
CC       intoxication symptoms caused by the sting of this species to humans.
CC       {ECO:0000305|PubMed:24862827}.
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   EMBL; KJ660065; AIA81145.1; -; mRNA.
DR   AlphaFoldDB; P0DMM8; -.
DR   SMR; P0DMM8; -.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:24862827"
FT   CHAIN           21..81
FT                   /note="Beta-mammal Tt1g"
FT                   /id="PRO_0000430182"
FT   DOMAIN          21..82
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   MOD_RES         81
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:24862827"
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..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        47..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   84 AA;  9438 MW;  430A2F9B621D30D7 CRC64;
     MKGMILFISC ILLIGIVVEC KEGYLMDHEG CKLSCFIRPS GYCGRECAIK KGSSGYCAWP
     ACYCYGLPNW VKVWERATNR CGKK