ID   TXP2_BRAAI              Reviewed;          39 AA.
AC   P85504;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Omega-theraphotoxin-Ba1b {ECO:0000305};
DE            Short=Omega-TRTX-Ba1b {ECO:0000305};
DE   AltName: Full=Ba2 {ECO:0000303|PubMed:19374957};
OS   Brachypelma albiceps (Mexican golden redrump tarantula) (Brachypelma
OS   ruhnaui).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Brachypelma.
OX   NCBI_TaxID=503929;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   STRUCTURE BY NMR, DISULFIDE BONDS, AND TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=19374957; DOI=10.1016/j.bbapap.2009.04.004;
RA   Corzo G., Bernard C., Clement H., Villegas E., Bosmans F., Tytgat J.,
RA   Possani L.D., Darbon H., Alagon A.;
RT   "Insecticidal peptides from the theraposid spider Brachypelma albiceps: an
RT   NMR-based model of Ba2.";
RL   Biochim. Biophys. Acta 1794:1190-1196(2009).
CC   -!- FUNCTION: Inhibits voltage-gated calcium channels (Cav) in rat
CC       cerebellar granule cells (By similarity). Has insecticidal activity to
CC       crickets (Acheta domesticus) (PubMed:19374957). Is not toxic to mice
CC       (PubMed:19374957). {ECO:0000250|UniProtKB:P0DL81,
CC       ECO:0000269|PubMed:19374957}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19374957}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19374957}.
CC   -!- MASS SPECTROMETRY: Mass=4440.67; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19374957};
CC   -!- TOXIC DOSE: LD(50) is 9.2 +-0.9 mg/kg in juvenile house crickets
CC       (Acheta domesticus). {ECO:0000269|PubMed:19374957}.
CC   -!- MISCELLANEOUS: Does not inhibit insect and mice voltage-gated sodium
CC       channels (para/tipE, Nav1.2/SCN2A, Nav1.5/SCN5A).
CC       {ECO:0000269|PubMed:19374957}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 06 (TXP1)
CC       subfamily. {ECO:0000305}.
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DR   PDB; 2KGH; NMR; -; A=1-39.
DR   PDBsum; 2KGH; -.
DR   AlphaFoldDB; P85504; -.
DR   BMRB; P85504; -.
DR   SMR; P85504; -.
DR   ArachnoServer; AS000401; omega-theraphotoxin-Ba1b.
DR   EvolutionaryTrace; P85504; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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   3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..39
FT                   /note="Omega-theraphotoxin-Ba1b"
FT                   /evidence="ECO:0000269|PubMed:19374957"
FT                   /id="PRO_0000332948"
FT   DISULFID        4..17
FT                   /evidence="ECO:0000269|PubMed:19374957,
FT                   ECO:0007744|PDB:2KGH"
FT   DISULFID        8..31
FT                   /evidence="ECO:0000269|PubMed:19374957,
FT                   ECO:0007744|PDB:2KGH"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000269|PubMed:19374957,
FT                   ECO:0007744|PDB:2KGH"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:2KGH"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:2KGH"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:2KGH"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:2KGH"
SQ   SEQUENCE   39 AA;  4446 MW;  E56D984E6A760122 CRC64;
     IFECVFSCDI KKEGKPCKPK GEKKCTGGWR CKIKLCLKI