TXBS1_BRASM
ID TXBS1_BRASM Reviewed; 99 AA.
AC B3FIV1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Omega-theraphotoxin-Bs2a;
DE Short=Omega-TRTX-Bs2a;
DE AltName: Full=Brachypelma smithi toxin 1;
DE Short=Bs1;
DE Flags: Precursor;
OS Brachypelma smithi (Mexican red knee tarantula) (Eurypelma smithi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Brachypelma.
OX NCBI_TaxID=54074;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 58-96, FUNCTION,
RP SUBCELLULAR LOCATION, AMIDATION AT SER-98, MASS SPECTROMETRY, AND TOXIC
RP DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18687374; DOI=10.1016/j.peptides.2008.07.003;
RA Corzo G., Diego-Garcia E., Clement H., Peigneur S., Odell G., Tytgat J.,
RA Possani L.D., Alagon A.;
RT "An insecticidal peptide from the theraposid Brachypelma smithi spider
RT venom reveals common molecular features among spider species from different
RT genera.";
RL Peptides 29:1901-1908(2008).
CC -!- FUNCTION: Has minor, but significant effects on the Para/tipE insect
CC sodium channel. {ECO:0000269|PubMed:18687374}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18687374}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18687374}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=4916.57; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18687374};
CC -!- TOXIC DOSE: LD(50) is 27 +- 11 ug/g in crickets.
CC {ECO:0000269|PubMed:18687374}.
CC -!- MISCELLANEOUS: Has no effect of mammalian sodium channels Nav1.2/SCN2A,
CC Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A and potassium channels
CC Kv1.3/KCNA3 and Shaker IR. {ECO:0000269|PubMed:18687374}.
CC -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 08 (Ltx-4)
CC subfamily. {ECO:0000305}.
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DR EMBL; EU196048; ABY59791.1; -; mRNA.
DR AlphaFoldDB; B3FIV1; -.
DR ArachnoServer; AS000648; omega-theraphotoxin-Bs2a.
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 InterPro; IPR012627; Toxin_22.
DR Pfam; PF08092; Toxin_22; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..57
FT /evidence="ECO:0000269|PubMed:18687374"
FT /id="PRO_0000359434"
FT CHAIN 58..98
FT /note="Omega-theraphotoxin-Bs2a"
FT /evidence="ECO:0000269|PubMed:18687374"
FT /id="PRO_0000359435"
FT MOD_RES 98
FT /note="Serine amide"
FT /evidence="ECO:0000305|PubMed:18687374"
FT DISULFID 58..73
FT /evidence="ECO:0000250"
FT DISULFID 65..78
FT /evidence="ECO:0000250"
FT DISULFID 72..93
FT /evidence="ECO:0000250"
SQ SEQUENCE 99 AA; 11336 MW; D4323457785DAD08 CRC64;
MNTIQVIIFA VVLVLTVTVG QADEDSAETS LLRKLEEAEA AMFGQYLEES KNSREKRCIG
ESVPCDKDDP RCCREYECLK PTGYGWWYAS YYCYRKKSG
