TXP1_BRAAI
ID TXP1_BRAAI Reviewed; 39 AA.
AC P85497;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Omega-theraphotoxin-Ba1a {ECO:0000305};
DE Short=Omega-TRTX-Ba1a {ECO:0000305};
DE AltName: Full=Ba1 {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, AND
RP 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=4406.43; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19374957};
CC -!- TOXIC DOSE: LD(50) is 10.8 +- 1.4 mg/kg in juvenile house crickets
CC (Acheta domesticus). {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 AlphaFoldDB; P85497; -.
DR BMRB; P85497; -.
DR SMR; P85497; -.
DR ArachnoServer; AS000397; omega-theraphotoxin-Ba1a.
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 Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT PEPTIDE 1..39
FT /note="Omega-theraphotoxin-Ba1a"
FT /evidence="ECO:0000269|PubMed:19374957"
FT /id="PRO_0000332947"
FT DISULFID 4..25
FT /evidence="ECO:0000250|UniProtKB:P85504"
FT DISULFID 8..31
FT /evidence="ECO:0000250|UniProtKB:P85504"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P85504"
SQ SEQUENCE 39 AA; 4412 MW; 676D984E6A780FC2 CRC64;
ILECVFSCDI KKEGKPCKPK GEKKCTGGWR CKIKLCLKI