SCX4_TITSE
ID SCX4_TITSE Reviewed; 84 AA.
AC O77463; A0A7S8MVH0; P45669;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Toxin Ts4 {ECO:0000303|PubMed:19689419};
DE AltName: Full=Non-toxic protein TsNTxP {ECO:0000303|PubMed:9080578};
DE Short=NTxP {ECO:0000303|PubMed:9080578};
DE AltName: Full=P-Allerg-alpha* NaTx4.1;
DE AltName: Full=PT-Immun-alpha* NaTx4.2;
DE AltName: Full=Tityustoxin VI;
DE Short=Ts VI;
DE Short=TsTX-VI;
DE Short=TsTXVI;
DE Short=TsVI;
DE AltName: Full=Tityustoxin-6;
DE Short=Ts-6;
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:AAC25688.1, ECO:0000312|EMBL:AAC25689.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10080354; DOI=10.1016/s0041-0101(98)00187-1;
RA Guatimosim S.C., Prado V.F., Diniz C.R., Chavez-Olortegui C.,
RA Kalapothakis E.;
RT "Molecular cloning and genomic analysis of TsNTxp: an immunogenic protein
RT from Tityus serrulatus scorpion venom.";
RL Toxicon 37:507-517(1999).
RN [2] {ECO:0000312|EMBL:QPD99044.1}
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 [3]
RP PROTEIN SEQUENCE OF 20-81, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=2085384; DOI=10.1007/bf01025013;
RA Marangoni S., Ghiso J., Sampaio S.V., Arantes E.C., Giglio J.R.,
RA Oliveira B., Frangione B.;
RT "The complete amino acid sequence of toxin TsTX-VI isolated from the venom
RT of the scorpion Tityus serrulatus.";
RL J. Protein Chem. 9:595-601(1990).
RN [4]
RP PROTEIN SEQUENCE OF 20-34, 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 [5]
RP FUNCTION.
RX PubMed=8843341; DOI=10.1080/15216549600201811;
RA Sampaio S.V., Coutinho-Netto J., Arantes E.C., Marangoni S., Oliveira B.,
RA Giglio J.R.;
RT "Isolation of toxin TsTX-VI from Tityus serrulatus scorpion venom. Effects
RT on the release of neurotransmitters from synaptosomes.";
RL Biochem. Mol. Biol. Int. 39:729-740(1996).
RN [6]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9080578; DOI=10.1016/s0041-0101(96)00133-x;
RA Chavez-Olortegui C., Kalapothakis E., Ferreira A.M.B.M., Ferreira A.P.,
RA Diniz C.R.;
RT "Neutralizing capacity of antibodies elicited by a non-toxic protein
RT purified from the venom of the scorpion Tityus serrulatus.";
RL Toxicon 35:213-221(1997).
RN [7]
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 [8]
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: Not toxic. Induces an immune response similar to that induced
CC by whole venom. Induces a dose dependent release of the
CC neurotransmitters glutamic acid and gamma aminobutyric acid from rat
CC brain synaptosomes. Thus, polyclonal antibodies raised against this
CC protein can neutralize the effects of the venom.
CC {ECO:0000269|PubMed:8843341, ECO:0000269|PubMed:9080578}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2085384,
CC ECO:0000269|PubMed:25199494}.
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 -!- TOXIC DOSE: LD(50) is 15 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:2085384}.
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; AF039600; AAC25689.1; -; Genomic_DNA.
DR EMBL; AF039599; AAC25688.1; -; mRNA.
DR EMBL; MT450708; QPD99044.1; -; mRNA.
DR PIR; A61484; A61484.
DR AlphaFoldDB; O77463; -.
DR SMR; O77463; -.
DR TCDB; 8.B.1.1.3; the long (4c-c) scorpion toxin (l-st) superfamily.
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 1: Evidence at protein level;
KW Allergen; Amidation; Direct protein sequencing; Disulfide bond; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000305|PubMed:2085384,
FT ECO:0000305|PubMed:25199494"
FT CHAIN 20..81
FT /note="Toxin Ts4"
FT /evidence="ECO:0000269|PubMed:2085384"
FT /id="PRO_0000035303"
FT PROPEP 82..84
FT /evidence="ECO:0000305|PubMed:2085384"
FT /id="PRO_0000035304"
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:0000250|UniProtKB:P56612"
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"
FT CONFLICT 69
FT /note="D -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9176 MW; DDEDE77B5B18C8EA CRC64;
MKRMILFISC LLLIDIVVGG REGYPADSKG CKITCFLTAA GYCNTECTLK KGSSGYCAWP
ACYCYGLPDS VKIWTSETNK CGKK
