SCX5_TITBA
ID SCX5_TITBA Reviewed; 86 AA.
AC P0C5K8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Toxin TbTx5;
DE AltName: Full=T-alpha* NaTx3.4;
DE Flags: Precursor;
OS Tityus bahiensis (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=50343;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11072047; DOI=10.1016/s0041-0101(00)00194-x;
RA Kalapothakis E., Jardim S., Magalhaes A.C., Mendes T.M., De Marco L.,
RA Afonso L.C.C., Chavez-Olortegui C.;
RT "Screening of expression libraries using ELISA: identification of
RT immunogenic proteins from Tityus bahiensis and Tityus serrulatus venom.";
RL Toxicon 39:679-685(2001).
RN [2]
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: 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. {ECO:0000250|UniProtKB:P01496}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:11072047}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11072047}.
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 -!- 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 AlphaFoldDB; P0C5K8; -.
DR SMR; P0C5K8; -.
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 3: Inferred from homology;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..83
FT /note="Toxin TbTx5"
FT /evidence="ECO:0000305|PubMed:11072047"
FT /id="PRO_0000309006"
FT DOMAIN 21..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 83
FT /note="Proline amide"
FT /evidence="ECO:0000250|UniProtKB:P01484"
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..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 86 AA; 9598 MW; FCDAF902D7F612F0 CRC64;
MNDFVFLVVA CLLTAGTEGK KDGYPVEGDN CAFVCFGYDN AYCDKLCKDK KADSGYCYWV
HILCYCYGLP DKEPTKTNGR CKPGKK
