SCX2_TITOB
ID SCX2_TITOB Reviewed; 87 AA.
AC P60212; H1ZZH1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Alpha-toxin To2;
DE AltName: Full=Alpha-toxin Tc48a;
DE AltName: Full=Alpha-toxin To48a;
DE AltName: Full=PT-alpha' NaTx11.1;
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 21-85, FUNCTION, AMIDATION AT LYS-85, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
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).
RN [3]
RP PROTEIN SEQUENCE OF 21-57, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=11821128; DOI=10.1016/s0041-0101(01)00252-5;
RA Batista C.V.F., Zamudio F.Z., Lucas S., Fox J.W., Frau A., Prestipino G.,
RA Possani L.D.;
RT "Scorpion toxins from Tityus cambridgei that affect Na(+)-channels.";
RL Toxicon 40:557-562(2002).
CC -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC channels (Nav) and inhibit the inactivation of the activated channels,
CC thereby blocking neuronal transmission. Affects the tetrodotoxin-
CC sensitive sodium current permeability of F-11 rat neuroblastoma cells.
CC Produces a dose dependent increase in amplitude and duration of the
CC current. {ECO:0000269|PubMed:15025998}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11821128,
CC ECO:0000269|PubMed:15025998}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11821128, ECO:0000305|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=7310; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15025998};
CC -!- MASS SPECTROMETRY: Mass=7318.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11821128};
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; HE585225; CCD31419.1; -; mRNA.
DR AlphaFoldDB; P60212; -.
DR SMR; P60212; -.
DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0044488; P:modulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
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 Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:11821128,
FT ECO:0000269|PubMed:15025998"
FT CHAIN 21..85
FT /note="Alpha-toxin To2"
FT /id="PRO_0000066809"
FT DOMAIN 22..84
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 85
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:15025998"
FT DISULFID 32..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 36..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 44..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 48..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 21
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33..34
FT /note="KM -> MN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 9832 MW; 8CFEF017BA0D39BD CRC64;
MIRFVLFISC FFLIGTVVEC NKDGYLMEGD GCKMGCLTRK ASYCVDQCKE VGGKDGYCYA
WLSCYCYNMP DSVEIWDSKN NKCGKGK
