SCX1_TITSE
ID SCX1_TITSE Reviewed; 84 AA.
AC P15226; A0A7S8RFZ4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Beta-mammal/insect toxin Ts1 {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:25199494, ECO:0000303|PubMed:31012002};
DE AltName: Full=Beta-like toxin Ts1;
DE AltName: Full=PT-Mice-Ins-beta NaTx6.1 {ECO:0000303|PubMed:22355312};
DE AltName: Full=Tityustoxin VII {ECO:0000303|PubMed:19689419};
DE Short=Toxin VII {ECO:0000303|PubMed:1339357, ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:6477555};
DE Short=Ts VII {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:21670206, ECO:0000303|PubMed:6477555};
DE Short=Ts7 {ECO:0000303|PubMed:19689419};
DE Short=TsTX-VII {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:6477555};
DE AltName: Full=Toxin II-11 {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:1993690};
DE AltName: Full=Toxin III-10 {ECO:0000303|PubMed:19689419};
DE AltName: Full=Toxin T2-IV {ECO:0000303|PubMed:1926167, ECO:0000303|PubMed:19689419};
DE AltName: Full=Toxin gamma {ECO:0000303|PubMed:19689419, ECO:0000303|PubMed:1993690, ECO:0000303|PubMed:4052021, ECO:0000303|PubMed:8243666, ECO:0000303|PubMed:9048656, ECO:0000303|Ref.7};
DE Short=T-gamma {ECO:0000303|PubMed:9611141};
DE Short=TiTx gamma {ECO:0000303|PubMed:9048656};
DE Short=Toxin-g {ECO:0000303|PubMed:10347806};
DE AltName: Full=TsTX-I {ECO:0000303|PubMed:19689419};
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] {ECO:0000312|EMBL:CAA46982.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=1339357; DOI=10.1016/0014-5793(92)80445-m;
RA Martin-Eauclaire M.-F., Ceard B., Ribeiro A.M., Diniz C.R., Rochat H.,
RA Bougis P.E.;
RT "Molecular cloning and nucleotide sequence analysis of a cDNA encoding the
RT main beta-neurotoxin from the venom of the South American scorpion Tityus
RT serrulatus.";
RL FEBS Lett. 302:220-222(1992).
RN [2] {ECO:0000312|EMBL:AAB29128.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8243666; DOI=10.1016/0014-5793(93)80428-w;
RA Becerril B., Corona M., Mejia M.C., Martin B.M., Lucas S., Bolivar F.,
RA Possani L.D.;
RT "The genomic region encoding toxin gamma from the scorpion Tityus
RT serrulatus contains an intron.";
RL FEBS Lett. 335:6-8(1993).
RN [3] {ECO:0000312|EMBL:QPD99041.1}
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).
RN [4]
RP PROTEIN SEQUENCE OF 21-81, AMIDATION AT CYS-81, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=6477555; DOI=10.1016/0006-291x(84)91211-7;
RA Bechis G., Sampieri F., Yuan P.-M., Brando T., Martin M.-F., Diniz C.R.,
RA Rochat H.;
RT "Amino acid sequence of toxin VII, a beta-toxin from the venom of the
RT scorpion Tityus serrulatus.";
RL Biochem. Biophys. Res. Commun. 122:1146-1153(1984).
RN [5]
RP PROTEIN SEQUENCE OF 21-81, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-LYS--MET-6.
RC TISSUE=Venom;
RX PubMed=4052021; DOI=10.1042/bj2290739;
RA Possani L.D., Martin B.M., Svendsen I., Rode G.S., Erickson B.W.;
RT "Scorpion toxins from Centruroides noxius and Tityus serrulatus. Primary
RT structures and sequence comparison by metric analysis.";
RL Biochem. J. 229:739-750(1985).
RN [6]
RP PROTEIN SEQUENCE OF 21-81, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1993690; DOI=10.1016/s0021-9258(18)49971-1;
RA Possani L.D., Martin B.M., Fletcher M.D., Fletcher P.L. Jr.;
RT "Discharge effect on pancreatic exocrine secretion produced by toxins
RT purified from Tityus serrulatus scorpion venom.";
RL J. Biol. Chem. 266:3178-3185(1991).
RN [7]
RP PROTEIN SEQUENCE OF 21-62, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Possani L.D., Martin B.M., Mochca-Morales J., Svendsen I.;
RT "Purification and chemical characterization of the major toxins from the
RT venom of the Brazilian scorpion Titus serrulatus Lutz and Mello.";
RL Carlsberg Res. Commun. 46:195-205(1981).
RN [8]
RP PROTEIN SEQUENCE OF 21-46, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1926167; DOI=10.1016/0041-0101(91)90058-y;
RA Sampaio S.V., Arantes E.C., Prado W.A., Riccioppo Neto F., Giglio J.R.;
RT "Further characterization of toxins T1IV (TsTX-III) and T2IV from Tityus
RT serrulatus scorpion venom.";
RL Toxicon 29:663-672(1991).
RN [9]
RP PROTEIN SEQUENCE OF 21-45, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=25199494; DOI=10.1016/j.toxicon.2014.08.064;
RA Pucca M.B., Amorim F.G., Cerni F.A., Bordon K.C.F., Cardoso I.A.,
RA Anjolette F.A., Arantes E.C.;
RT "Influence of post-starvation extraction time and prey-specific diet in
RT Tityus serrulatus scorpion venom composition and hyaluronidase activity.";
RL Toxicon 90:326-336(2014).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3651476; DOI=10.1016/0167-4838(87)90312-8;
RA Areas E.P.G., Giglio J.R., Arantes E.C., Kawanoa Y.;
RT "Raman and infrared spectra of toxin gamma from the venom of the scorpion
RT Tityus serrulatus.";
RL Biochim. Biophys. Acta 915:292-298(1987).
RN [11]
RP AMINO ACID COMPOSITION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=2781589; DOI=10.1016/0041-0101(89)90102-5;
RA Arantes E.C., Prado W.A., Sampaio S.V., Giglio J.R.;
RT "A simplified procedure for the fractionation of Tityus serrulatus venom:
RT isolation and partial characterization of TsTX-IV, a new neurotoxin.";
RL Toxicon 27:907-916(1989).
RN [12]
RP FUNCTION.
RX PubMed=9048656; DOI=10.1161/01.res.80.3.363;
RA Marcotte P., Chen L.Q., Kallen R.G., Chahine M.;
RT "Effects of Tityus serrulatus scorpion toxin gamma on voltage-gated Na+
RT channels.";
RL Circ. Res. 80:363-369(1997).
RN [13]
RP FUNCTION.
RX PubMed=9611141; DOI=10.1152/ajpcell.1998.274.6.c1745;
RA Conceicao I.M., Lebrun I., Cano-Abad M., Gandia L., Hernandez-Guijo J.M.,
RA Lopez M.G., Villarroya M., Jurkiewicz A., Garcia A.G.;
RT "Synergism between toxin-gamma from Brazilian scorpion Tityus serrulatus
RT and veratridine in chromaffin cells.";
RL Am. J. Physiol. 274:C1745-C1754(1998).
RN [14]
RP FUNCTION.
RX PubMed=10347806; DOI=10.1590/s0100-879x1999000400009;
RA Bucaretchi F., Vinagre A.M., Chavez-Olortegui C., Collares E.F.;
RT "Effect of toxin-g from Tityus serrulatus scorpion venom on gastric
RT emptying in rats.";
RL Braz. J. Med. Biol. Res. 32:431-434(1999).
RN [15]
RP SITES LYS-32; TRP-59 AND TRP-74.
RX PubMed=10091586; DOI=10.1046/j.1432-1327.1999.00152.x;
RA Hassani O., Mansuelle P., Cestele S., Bourdeaux M., Rochat H., Sampieri F.;
RT "Role of lysine and tryptophan residues in the biological activity of toxin
RT VII (Ts gamma) from the scorpion Tityus serrulatus.";
RL Eur. J. Biochem. 260:76-86(1999).
RN [16]
RP FUNCTION.
RX PubMed=17698594; DOI=10.1085/jgp.200609719;
RA Campos F.V., Chanda B., Beirao P.S., Bezanilla F.;
RT "Beta-scorpion toxin modifies gating transitions in all four voltage
RT sensors of the sodium channel.";
RL J. Gen. Physiol. 130:257-268(2007).
RN [17]
RP FUNCTION.
RX PubMed=17118417; DOI=10.1016/j.taap.2006.10.009;
RA Bosmans F., Martin-Eauclaire M.F., Tytgat J.;
RT "Differential effects of five 'classical' scorpion beta-toxins on rNav1.2a
RT and DmNav1 provide clues on species-selectivity.";
RL Toxicol. Appl. Pharmacol. 218:45-51(2007).
RN [18]
RP FUNCTION.
RX PubMed=19005548; DOI=10.1038/nature07473;
RA Bosmans F., Martin-Eauclaire M.F., Swartz K.J.;
RT "Deconstructing voltage sensor function and pharmacology in sodium
RT channels.";
RL Nature 456:202-208(2008).
RN [19]
RP FUNCTION ON NAV1.9/SCN11A.
RX PubMed=21670206; DOI=10.1085/jgp.201110614;
RA Bosmans F., Puopolo M., Martin-Eauclaire M.F., Bean B.P., Swartz K.J.;
RT "Functional properties and toxin pharmacology of a dorsal root ganglion
RT sodium channel viewed through its voltage sensors.";
RL J. Gen. Physiol. 138:59-72(2011).
RN [20]
RP FUNCTION.
RX PubMed=21549737; DOI=10.1016/j.toxicon.2011.04.017;
RA Zoccal K.F., Bitencourt C.S., Secatto A., Sorgi C.A., Bordon K.C.,
RA Sampaio S.V., Arantes E.C., Faccioli L.H.;
RT "Tityus serrulatus venom and toxins Ts1, Ts2 and Ts6 induce macrophage
RT activation and production of immune mediators.";
RL Toxicon 57:1101-1108(2011).
RN [21]
RP FUNCTION, AND SYNTHESIS OF 21-81 (BOTH AMIDATED AND NON-AMIDATED FORMS).
RX PubMed=24989851; DOI=10.1002/anie.201404438;
RA Dang B., Kubota T., Correa A.M., Bezanilla F., Kent S.B.;
RT "Total chemical synthesis of biologically active fluorescent dye-labeled
RT Ts1 toxin.";
RL Angew. Chem. Int. Ed. 53:8970-8974(2014).
RN [22]
RP MUTAGENESIS OF CYS-81, AND MASS SPECTROMETRY.
RX PubMed=24560880; DOI=10.1016/j.toxicon.2014.02.010;
RA Coelho V.A., Cremonez C.M., Anjolette F.A., Aguiar J.F., Varanda W.A.,
RA Arantes E.C.;
RT "Functional and structural study comparing the C-terminal amidated beta-
RT neurotoxin Ts1 with its isoform Ts1-G isolated from Tityus serrulatus
RT venom.";
RL Toxicon 83C:15-21(2014).
RN [23]
RP FUNCTION.
RX PubMed=25624450; DOI=10.1085/jgp.201411268;
RA Martin-Eauclaire M.F., Ferracci G., Bosmans F., Bougis P.E.;
RT "A surface plasmon resonance approach to monitor toxin interactions with an
RT isolated voltage-gated sodium channel paddle motif.";
RL J. Gen. Physiol. 145:155-162(2015).
RN [24]
RP FUNCTION.
RX PubMed=25862296; DOI=10.1016/j.neuropharm.2015.03.027;
RA Peigneur S., Cologna C.T., Cremonez C.M., Mille B.G., Pucca M.B.,
RA Cuypers E., Arantes E.C., Tytgat J.;
RT "A gamut of undiscovered electrophysiological effects produced by Tityus
RT serrulatus toxin 1 on NaV-type isoforms.";
RL Neuropharmacology 95:269-277(2015).
RN [25]
RP FUNCTION.
RX PubMed=28634472; DOI=10.3389/fmicb.2017.00984;
RA Santussi W.M., Bordon K.C.F., Rodrigues Alves A.P.N., Cologna C.T.,
RA Said S., Arantes E.C.;
RT "Antifungal activity against filamentous fungi of Ts1, a multifunctional
RT toxin from Tityus serrulatus scorpion venom.";
RL Front. Microbiol. 8:984-984(2017).
RN [26]
RP REVIEW.
RX PubMed=30059695; DOI=10.1016/j.toxicon.2018.07.024;
RA Martin-Eauclaire M.F., Bougis P.E., de Lima M.E.;
RT "Ts1 from the Brazilian scorpion Tityus serrulatus: a half-century of
RT studies on a multifunctional beta like-toxin.";
RL Toxicon 152:106-120(2018).
RN [27]
RP FUNCTION, AND RECOMBINANT EXPRESSION.
RX PubMed=31012002; DOI=10.1134/s1607672919010034;
RA Shenkarev Z.O., Shulepko M.A., Peigneur S., Myshkin M.Y., Berkut A.A.,
RA Vassilevski A.A., Tytgat J., Lyukmanova E.N., Kirpichnikov M.P.;
RT "Recombinant production and structure-function study of the Ts1 toxin from
RT the Brazilian scorpion Tityus serrulatus.";
RL Dokl. Biochem. Biophys. 484:9-12(2019).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 21-81, AND DISULFIDE BOND.
RX PubMed=10388565; DOI=10.1006/jmbi.1999.2868;
RA Polikarpov I., Junior M.S.M., Marangoni S., Toyama M.H., Teplyakov A.;
RT "Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides
RT insights into the specificity and toxicity of scorpion toxins.";
RL J. Mol. Biol. 290:175-184(1999).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 21-81, AND DISULFIDE BONDS.
RX PubMed=12595696; DOI=10.1107/s090744490202111x;
RA Pinheiro C.B., Marangoni S., Toyama M.H., Polikarpov I.;
RT "Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic
RT resolution: insights into interactions with Na+ channels.";
RL Acta Crystallogr. D 59:405-415(2003).
RN [30]
RP NOMENCLATURE.
RX PubMed=19689419; DOI=10.2174/092986609788923329;
RA Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.;
RT "Tityus serrulatus scorpion venom and toxins: an overview.";
RL Protein Pept. Lett. 16:920-932(2009).
RN [31]
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: Voltage-gated sodium channels (Nav) gating-modifier. Acts
CC both as alpha- and beta-toxin, since it affects not only activation but
CC also inactivation of Nav channels (PubMed:25862296) (Probable). Binds
CC to Nav domain DII and impairs the four Nav channel voltage sensors
CC movements (PubMed:17698594, PubMed:19005548). Depending on Nav channel
CC subtypes tested, can also bind Nav domains DIII (low affinity) and DIV
CC (very low affinity) (PubMed:17698594, PubMed:19005548,
CC PubMed:25624450). Acts on almost all the Nav channels tested (mammalian
CC Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A,
CC Nav1.9/SCN11A, and insect DmNav1) (PubMed:9048656, PubMed:17698594,
CC PubMed:21670206, PubMed:24989851, PubMed:25862296, PubMed:31012002). Is
CC highly active against both mammals and insects (PubMed:17118417,
CC PubMed:21549737). Irreversibly modulates DmNav channels
CC (PubMed:25862296). Other Ts1 activities have been studied, such as
CC immunomodulation, antimicrobial activity or exocrine secretion
CC (Probable). This toxin exhibits an antifungal activity against
CC filamentous fungi (PubMed:28634472). In vitro, it has an important
CC immunomodulatory effect on macrophages by stimulating the release of
CC pro-inflammatory cytokines (PubMed:21549737). It also shows an activity
CC in exocrine secretion in pancreas, stomach and adrenal gland
CC (PubMed:1993690, PubMed:9611141, PubMed:10347806).
CC {ECO:0000269|PubMed:10347806, ECO:0000269|PubMed:17118417,
CC ECO:0000269|PubMed:17698594, ECO:0000269|PubMed:19005548,
CC ECO:0000269|PubMed:1993690, ECO:0000269|PubMed:21549737,
CC ECO:0000269|PubMed:21670206, ECO:0000269|PubMed:24989851,
CC ECO:0000269|PubMed:25624450, ECO:0000269|PubMed:25862296,
CC ECO:0000269|PubMed:28634472, ECO:0000269|PubMed:31012002,
CC ECO:0000269|PubMed:9048656, ECO:0000269|PubMed:9611141, ECO:0000305,
CC ECO:0000305|PubMed:30059695}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-7.5. Is almost completely inactivated at pH 11.5.
CC {ECO:0000269|PubMed:3651476};
CC Temperature dependence:
CC Optimum temperature is 25-60 degrees Celsius. All temperatures tested
CC are optimal. {ECO:0000269|PubMed:3651476};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1926167,
CC ECO:0000269|PubMed:1993690, ECO:0000269|PubMed:25199494,
CC ECO:0000269|PubMed:4052021, ECO:0000269|PubMed:6477555,
CC ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25199494}.
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 -!- PTM: C-terminal amidation is important for high activity.
CC {ECO:0000269|PubMed:24560880, ECO:0000269|PubMed:24989851}.
CC -!- MASS SPECTROMETRY: Mass=6879.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:24560880};
CC -!- TOXIC DOSE: LD(50) is 4.7 ug by subcutaneous injection into mice (235
CC ug/kg). {ECO:0000305|PubMed:30059695}.
CC -!- TOXIC DOSE: LD(50) is 826 +/- 156 ug/kg by intravenous injection into
CC mice. {ECO:0000269|PubMed:2781589}.
CC -!- TOXIC DOSE: LD(50) is 11 +/- 9 ug/kg by intracistenal injection into
CC mice. {ECO:0000269|PubMed:2781589}.
CC -!- TOXIC DOSE: LD(50) is 0.6 ng by intracerebroventricular injection into
CC mice (30 ng/kg). {ECO:0000269|PubMed:2781589,
CC ECO:0000305|PubMed:30059695}.
CC -!- TOXIC DOSE: LD(50) is 1.7 ng by intracerebroventricular injection into
CC mice (85 ng/kg). {ECO:0000269|PubMed:10091586}.
CC -!- MISCELLANEOUS: Is the main neurotoxin of the venom of T.serrulatus.
CC -!- MISCELLANEOUS: Does not show activity on Nav1.1/SCN1A, Nav1.7/SCN9A,
CC Nav1.8/SCN10A and the bacterial NaChBac. {ECO:0000269|PubMed:21670206,
CC ECO:0000269|PubMed:25862296, ECO:0000305|PubMed:30059695}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. {ECO:0000305}.
CC -!- CAUTION: The 'mutant' Ts1-G was isolated from the venom before the last
CC step maturation (i.e. amidation) thanks to a right purification
CC technique (PubMed:24560880). It is indicated here as a mutant, since it
CC does not correspond to the mature toxin. {ECO:0000305|PubMed:24560880}.
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DR EMBL; X66256; CAA46982.1; -; mRNA.
DR EMBL; S66941; AAB29128.1; -; Genomic_DNA.
DR EMBL; MT450705; QPD99041.1; -; mRNA.
DR PIR; S21158; S21158.
DR PDB; 1B7D; X-ray; 1.73 A; A=21-81.
DR PDB; 1NPI; X-ray; 1.16 A; A=21-81.
DR PDBsum; 1B7D; -.
DR PDBsum; 1NPI; -.
DR AlphaFoldDB; P15226; -.
DR SMR; P15226; -.
DR ABCD; P15226; 1 sequenced antibody.
DR EvolutionaryTrace; P15226; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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 3D-structure; Amidation; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Fungicide; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1926167,
FT ECO:0000269|PubMed:1993690, ECO:0000269|PubMed:25199494,
FT ECO:0000269|PubMed:6477555, ECO:0000269|Ref.7"
FT CHAIN 21..81
FT /note="Beta-mammal/insect toxin Ts1"
FT /evidence="ECO:0000269|PubMed:1993690,
FT ECO:0000269|PubMed:6477555"
FT /id="PRO_0000035305"
FT DOMAIN 21..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT SITE 32
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:10091586"
FT SITE 59
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:10091586"
FT SITE 74
FT /note="Important for activity"
FT /evidence="ECO:0000269|PubMed:10091586"
FT MOD_RES 81
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:6477555"
FT DISULFID 31..81
FT /evidence="ECO:0000269|PubMed:10388565,
FT ECO:0000269|PubMed:12595696, ECO:0007744|PDB:1B7D,
FT ECO:0007744|PDB:1NPI"
FT DISULFID 35..57
FT /evidence="ECO:0000269|PubMed:10388565,
FT ECO:0000269|PubMed:12595696, ECO:0007744|PDB:1B7D,
FT ECO:0007744|PDB:1NPI"
FT DISULFID 43..62
FT /evidence="ECO:0000269|PubMed:10388565,
FT ECO:0000269|PubMed:12595696, ECO:0007744|PDB:1B7D,
FT ECO:0007744|PDB:1NPI"
FT DISULFID 47..64
FT /evidence="ECO:0000269|PubMed:10388565,
FT ECO:0000269|PubMed:12595696, ECO:0007744|PDB:1B7D,
FT ECO:0007744|PDB:1NPI"
FT MUTAGEN 21..26
FT /note="Missing: Loss of toxicity to mice."
FT /evidence="ECO:0000269|PubMed:4052021"
FT MUTAGEN 81
FT /note="C->CG: Decrease of affinity of this non amidated
FT toxin (Ts1-G) for sodium channel."
FT /evidence="ECO:0000269|PubMed:24560880"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1NPI"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1NPI"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1NPI"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1B7D"
SQ SEQUENCE 84 AA; 9382 MW; 430F3FCA74823E77 CRC64;
MKGMILFISC LLLIGIVVEC KEGYLMDHEG CKLSCFIRPS GYCGRECGIK KGSSGYCAWP
ACYCYGLPNW VKVWDRATNK CGKK
