TXA25_ANDAU
ID TXA25_ANDAU Reviewed; 82 AA.
AC Q4LCS8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Beta-insect toxin AaBTxL1;
DE AltName: Full=Neurotoxin AaBTX-L1;
DE AltName: Full=Peptide AaF1CA25;
DE Flags: Precursor;
OS Androctonus australis (Sahara scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6858;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAH03780.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-35, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:15963953}, and
RC Venom gland {ECO:0000269|PubMed:15963953};
RX PubMed=15963953; DOI=10.1016/j.bbrc.2005.05.148;
RA Martin-Eauclaire M.-F., Ceard B., Bosmans F., Rosso J.-P., Tytgat J.,
RA Bougis P.E.;
RT "New 'birtoxin analogs' from Androctonus australis venom.";
RL Biochem. Biophys. Res. Commun. 333:524-530(2005).
CC -!- FUNCTION: Shifts the voltage of activation of para/tipE voltage-
CC dependent sodium channels (Nav) toward more negative potentials.
CC {ECO:0000269|PubMed:15963953}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15963953}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15963953}.
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 -!- MISCELLANEOUS: Is totally devoid of toxicity when
CC intracerebroventricularly injected into mice and does not compete with
CC radiolabeled voltage-gated potassium and sodium channel toxins in
CC binding experiments on rat brain synaptosomes.
CC {ECO:0000305|PubMed:15963953}.
CC -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR EMBL; AJ781834; CAH03780.1; -; mRNA.
DR AlphaFoldDB; Q4LCS8; -.
DR SMR; Q4LCS8; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 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..22
FT /evidence="ECO:0000269|PubMed:15963953"
FT CHAIN 23..82
FT /note="Beta-insect toxin AaBTxL1"
FT /id="PRO_0000228821"
FT DOMAIN 25..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 40..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 50..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 54..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 34
FT /note="S -> SS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 82 AA; 9425 MW; DF9FC3346676DCF7 CRC64;
MMKLVLFSVI VILFSLIGSI HGADVPGNYP LDRSGKKYPC TITWKKNPSC IQICKKHGVK
YGYCFDFQCW CEIFGRLKTF KI
