SCNA4_TITDI
ID SCNA4_TITDI Reviewed; 83 AA.
AC P0C1X7; C9X4J4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Ardiscretin;
DE AltName: Full=PT-Arthr-beta* NaTx2.1;
DE AltName: Full=Toxin TdNa4;
DE Flags: Precursor;
OS Tityus discrepans (Venezuelan scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX NCBI_TaxID=57059;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-81, AMIDATION AT CYS-81,
RP FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15033324; DOI=10.1016/j.toxicon.2003.12.004;
RA D'Suze G., Sevcik C., Corona M., Zamudio F.Z., Batista C.V.F.,
RA Coronas F.I., Possani L.D.;
RT "Ardiscretin a novel arthropod-selective toxin from Tityus discrepans
RT scorpion venom.";
RL Toxicon 43:263-272(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19470401; DOI=10.1016/j.biochi.2009.05.005;
RA D'Suze G., Schwartz E.F., Garcia-Gomez B.I., Sevcik C., Possani L.D.;
RT "Molecular cloning and nucleotide sequence analysis of genes from a cDNA
RT library of the scorpion Tityus discrepans.";
RL Biochimie 91:1010-1019(2009).
RN [3]
RP PROTEIN SEQUENCE OF 21-30, AND MASS SPECTROMETRY.
RX PubMed=16705749; DOI=10.1002/pmic.200500525;
RA Batista C.V.F., D'Suze G., Gomez-Lagunas F., Zamudio F.Z., Encarnacion S.,
RA Sevcik C., Possani L.D.;
RT "Proteomic analysis of Tityus discrepans scorpion venom and amino acid
RT sequence of novel toxins.";
RL Proteomics 6:3718-3727(2006).
RN [4]
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: Inhibits the sodium (Nav) currents in an apparent
CC irreversible manner. Produces small depolarization and induces
CC repetitive firing in squid axons. Is specific for arthropods (crickets,
CC triatomides, crabs and squids), but is non-toxic to mice
CC (PubMed:15033324). Shows antibacterial activity against both Gram-
CC positive and Gram-negative bacteria (By similarity).
CC {ECO:0000250|UniProtKB:P0CF39, ECO:0000269|PubMed:15033324}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15033324}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15033324}.
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=7103.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15033324, ECO:0000269|PubMed:16705749};
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR EMBL; FN392272; CAY61916.1; -; mRNA.
DR EMBL; FN392280; CAY61933.1; -; mRNA.
DR AlphaFoldDB; P0C1X7; -.
DR SMR; P0C1X7; -.
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 Amidation; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15033324,
FT ECO:0000269|PubMed:16705749"
FT CHAIN 21..81
FT /note="Ardiscretin"
FT /evidence="ECO:0000269|PubMed:15033324"
FT /id="PRO_0000250205"
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:0000269|PubMed:15033324"
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 83 AA; 9506 MW; B83E24156F6F1331 CRC64;
MKGMIMLISC LMLIDVVVES KNGYIIEPKG CKYSCFWGSS TWCNRECKFK KGSSGYCAWP
ACWCYGLPDN VKIFDYYNNK CGK
