SCX38_TITCO
ID SCX38_TITCO Reviewed; 84 AA.
AC Q5G8A8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Toxin-like TcoNTxP1;
DE AltName: Full=Insect-like toxic peptide Tco 38.32-2;
DE AltName: Full=PT-alpha* NaTx4.5;
DE Flags: Precursor;
OS Tityus costatus (Brazilian scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=309814;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT CYS-81, PROTEIN SEQUENCE OF 20-49,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15683865; DOI=10.1016/j.toxicon.2004.10.014;
RA Diego-Garcia E., Batista C.V.F., Garcia-Gomez B.I., Lucas S., Candido D.M.,
RA Gomez-Lagunas F., Possani L.D.;
RT "The Brazilian scorpion Tityus costatus Karsch: genes, peptides and
RT function.";
RL Toxicon 45:273-283(2005).
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: This protein is not toxic. It induces an immune response
CC similar to that induced by whole venom. Thus, polyclonal antibodies
CC raised against this protein can neutralize the effects of the venom (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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=6566.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15683865};
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 EMBL; AY740693; AAW72463.1; -; mRNA.
DR AlphaFoldDB; Q5G8A8; -.
DR SMR; Q5G8A8; -.
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:InterPro.
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 Amidation; Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..81
FT /note="Toxin-like TcoNTxP1"
FT /id="PRO_0000231503"
FT PROPEP 82..84
FT /id="PRO_0000231504"
FT DOMAIN 21..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 81
FT /note="Cysteine amide"
FT /evidence="ECO:0000305|PubMed:15683865"
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..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 84 AA; 9036 MW; 54D9DB4C9F74F0AF CRC64;
MKRMILFTSC LLLIDIVVGG KEGYPADSKG CKVTCFLTAA GYCNTECKLQ KASSGYCAWP
ACYCYGLPDS ASVWDSATNK CGKK
