ID   SCX2_TITMA              Reviewed;          69 AA.
AC   C0HLM0;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Toxin Tma2 {ECO:0000303|PubMed:31402191};
OS   Tityus macrochirus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=2599738 {ECO:0000303|PubMed:31402191};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000303|PubMed:31402191};
RX   PubMed=31402191; DOI=10.1016/j.toxicon.2019.07.013;
RA   Rincon-Cortes C.A., Olamendi-Portugal T., Carcamo-Noriega E.N.,
RA   Santillan E.G., Zuniga F.Z., Reyes-Montano E.A., Vega Castro N.A.,
RA   Possani L.D.;
RT   "Structural and functional characterization of toxic peptides purified from
RT   the venom of the Colombian scorpion Tityus macrochirus.";
RL   Toxicon 169:5-11(2019).
CC   -!- FUNCTION: Inhibits voltage-gated sodium channels (Nav). This toxin
CC       shows insect lethality against crickets. {ECO:0000269|PubMed:31402191}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31402191}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31402191}.
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. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLM0; -.
DR   SMR; C0HLM0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR   GO; GO:0044493; P:envenomation resulting in negative regulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
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   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..69
FT                   /note="Toxin Tma2"
FT                   /id="PRO_0000448249"
FT   DOMAIN          2..66
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        14..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        18..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   69 AA;  7830 MW;  C41CC516ADF7319D CRC64;
     KKDDYPVDTA ERNCKFECNI VDDKGYCDNL CKGRKAEKGY CYSLKASCYC YGLPDDSPTK
     TSKRCNPNV