LVA41_TITSE
ID LVA41_TITSE Reviewed; 93 AA.
AC A0A7S8MVN3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Putative sodium channel toxin Ts41 {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-41 {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:QPD99032.1}
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33181162}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {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 (4 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; MT081350; QPD99032.1; -; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion 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 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..93
FT /note="Putative sodium channel toxin Ts41"
FT /id="PRO_5031412909"
FT DOMAIN 26..88
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 22..87
FT /evidence="ECO:0000305"
FT DISULFID 39..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 52..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 93 AA; 11052 MW; 0FE0D4EB14DC8D0B CRC64;
MKIGVLFTII SMLCLLEVRK ICSKKEGGYP RYFSFGYKCQ NWGTNEYCRT VCQLHKGEYG
YCYAGDCYCE GLTEENRLFW NVYRKYCKNP LFD
