ID   LVA28_TITSE             Reviewed;          90 AA.
AC   A0A218QX08;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Putative sodium channel toxin Ts28 {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Putative NaTx {ECO:0000303|PubMed:33181162};
DE   AltName: Full=Putative lipolysis-activating peptide {ECO:0000250|UniProtKB:P84810};
DE   AltName: Full=Tityustoxin-28 {ECO:0000305};
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:JAW06977.1, ECO:0000312|EMBL:JAW07017.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA   de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA   Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA   Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT   "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT   obscurus and T. serrulatus scorpions.";
RL   PLoS ONE 13:e0193739-e0193739(2018).
RN   [2] {ECO:0000312|EMBL:QPD99056.1}
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: The edited BmKBTx-like may modulate voltage-gated sodium
CC       channels (Nav). {ECO:0000250|UniProtKB:P84810}.
CC   -!- FUNCTION: The non-edited form is able to form a heterodimer (By
CC       similarity). In orthologs, a heterodimer with LVP beta-chain induces
CC       lipolysis in rat adipocytes, which is mediated through the beta-2
CC       adrenergic receptor pathway (ADRB2) (By similarity). Since no LVP beta-
CC       chains have been identified in the venom of this scorpion, it is
CC       possible that this protein is not involved in a lipolysis process
CC       (Probable). {ECO:0000250|UniProtKB:P84810,
CC       ECO:0000305|PubMed:33181162}.
CC   -!- SUBUNIT: Monomer (edited version) and heterodimer (non-edited version)
CC       of this alpha chain and a beta chain (AC P0CI43).
CC       {ECO:0000250|UniProtKB:P84810}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29561852,
CC       ECO:0000305|PubMed:33181162}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29561852, 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   -!- RNA EDITING: Modified_positions=81 {ECO:0000250|UniProtKB:Q6WJF5};
CC       Note=The stop codon (UGA) at position 81 is created by RNA editing.
CC       {ECO:0000250|UniProtKB:Q6WJF5};
CC   -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GEUW01000068; JAW06977.1; -; mRNA.
DR   EMBL; GEUW01000028; JAW07017.1; -; mRNA.
DR   EMBL; MT450720; QPD99056.1; -; mRNA.
DR   SMR; A0A218QX08; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin; Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..90
FT                   /note="Putative sodium channel toxin Ts28"
FT                   /id="PRO_5011910044"
FT   DOMAIN          26..86
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        40..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        46..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        50..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   90 AA;  10569 MW;  B9B2BEBB2D0E04E5 CRC64;
     MKISLVTWLI TALCLMEIEE IDGDTPGNYP VDFQGIYYEC IVYNRCERDC KIHGASYGYC
     YAGVCFCEYL PDENKNFWDV MKKQCDYMNN