SCX14_TITOB
ID SCX14_TITOB Reviewed; 89 AA.
AC H1ZZI3; P84684;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Toxin To14;
DE AltName: Full=T-alpha* NaTx3.10;
DE AltName: Full=Toxin Tc41 {ECO:0000303|PubMed:15025998};
DE AltName: Full=Toxin To41 {ECO:0000303|PubMed:15025998};
DE Flags: Precursor;
OS Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=1221240;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RC TISSUE=Venom gland;
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).
RN [2]
RP PROTEIN SEQUENCE OF 21-30, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15025998; DOI=10.1016/j.jchromb.2003.09.002;
RA Batista C.V.F., del Pozo L., Zamudio F.Z., Contreras S., Becerril B.,
RA Wanke E., Possani L.D.;
RT "Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and
RT the role of prolines on mass spectrometry analysis of toxins.";
RL J. Chromatogr. B 803:55-66(2004).
CC -!- FUNCTION: Inhibits voltage-gated sodium channels (Nav). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15025998}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15025998}.
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 -!- MASS SPECTROMETRY: Mass=7109.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15025998};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. {ECO:0000305}.
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DR EMBL; HE585237; CCD31431.1; -; mRNA.
DR AlphaFoldDB; H1ZZI3; -.
DR SMR; H1ZZI3; -.
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: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 Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..88
FT /note="Toxin To14"
FT /evidence="ECO:0000250|UniProtKB:P0DQU6,
FT ECO:0000269|PubMed:15025998"
FT /id="PRO_5000851440"
FT DOMAIN 21..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 33..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 37..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 50..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 89 AA; 10106 MW; 93F0593CE8B92A51 CRC64;
MNCLMLIFVV FLLAFGVECK KDDYPVDTAK RNCMLDCNVW DDEGYCDKFC KGRKADSGYC
YKLKAACYCY GLPDDSPTKT SGRCNPNVR
