ID   TXP1A_BRASM             Reviewed;          39 AA.
AC   P0DL80; P49265;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Omega-theraphotoxin-Bs1a {ECO:0000305};
DE            Short=Omega-TRTX-Bs1a {ECO:0000305};
DE   AltName: Full=BsTX1a;
DE   AltName: Full=Venom protein 1 {ECO:0000303|PubMed:7801344};
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   PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=7801344; DOI=10.1016/0041-0101(94)90392-1;
RA   Kaiser I.I., Griffin P.R., Aird S.D., Hudiburg S., Shabanowitz J.,
RA   Francis B., John T.R., Hunt D.F., Odell G.V.;
RT   "Primary structures of two proteins from the venom of the Mexican red knee
RT   tarantula (Brachypelma smithii).";
RL   Toxicon 32:1083-1093(1994).
RN   [2]
RP   ALTERNATIVE DISULFIDE BONDS TOPOLOGY.
RX   PubMed=11790834; DOI=10.1110/ps.30502;
RA   Shu Q., Lu S.Y., Gu X.-C., Liang S.-P.;
RT   "The structure of spider toxin huwentoxin-II with unique disulfide linkage:
RT   evidence for structural evolution.";
RL   Protein Sci. 11:245-252(2002).
CC   -!- FUNCTION: Inhibits voltage-gated calcium channels (Cav) in rat
CC       cerebellar granule cells (By similarity). Has insecticidal activity (By
CC       similarity). {ECO:0000250|UniProtKB:P0DL63,
CC       ECO:0000250|UniProtKB:P85497}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7801344}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:7801344}.
CC   -!- MASS SPECTROMETRY: Mass=4400.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7801344};
CC   -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC       to that of Eurypelma spider toxin 2 from Aphonopelma californicum (AC
CC       P61510). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 06 (TXP1)
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is reported in PubMed:11790834 that disulfide bonds may be
CC       in positions 4-17, 8-31 and 25-36. {ECO:0000305|PubMed:11790834}.
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DR   AlphaFoldDB; P0DL80; -.
DR   SMR; P0DL80; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012625; Toxin_20.
DR   Pfam; PF08089; Toxin_20; 1.
DR   PROSITE; PS60022; HWTX_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..39
FT                   /note="Omega-theraphotoxin-Bs1a"
FT                   /evidence="ECO:0000269|PubMed:7801344"
FT                   /id="PRO_0000044982"
FT   DISULFID        4..25
FT                   /evidence="ECO:0000269|PubMed:7801344"
FT   DISULFID        8..31
FT                   /evidence="ECO:0000269|PubMed:7801344"
FT   DISULFID        17..36
FT                   /evidence="ECO:0000269|PubMed:7801344"
SQ   SEQUENCE   39 AA;  4405 MW;  E572A54E64903422 CRC64;
     IFECVFSCDI EKEGKPCKPK GEKKCSGGWK CKIKLCLKI