TX1G_APHSP
ID TX1G_APHSP Reviewed; 39 AA.
AC P61510; P18928;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Omega-theraphotoxin-Asp1g {ECO:0000305};
DE Short=Omega-TRTX-Asp1g {ECO:0000305};
DE AltName: Full=Eurypelma spider toxin 2 {ECO:0000303|PubMed:2742756};
DE Short=ESTx2 {ECO:0000303|PubMed:2742756};
OS Aphonopelma sp. (American tarantula).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Aphonopelma; unclassified Aphonopelma.
OX NCBI_TaxID=29932;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2742756; DOI=10.1515/bchm3.1989.370.1.485;
RA Savel-Niemann A.;
RT "Tarantula (Eurypelma californicum) venom, a multicomponent system.";
RL Biol. Chem. Hoppe-Seyler 370:485-498(1989).
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:P0DL81,
CC ECO:0000250|UniProtKB:P61509}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2742756}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2742756}.
CC -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC to that of venom protein 1 from Brachypelma smithi (AC P0DL80).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 06 (TXP1)
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P61510; -.
DR SMR; P61510; -.
DR ArachnoServer; AS000249; omega-theraphotoxin-Asp1g.
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-Asp1g"
FT /evidence="ECO:0000269|PubMed:2742756"
FT /id="PRO_0000044981"
FT DISULFID 4..25
FT /evidence="ECO:0000250|UniProtKB:P0DL80"
FT DISULFID 8..31
FT /evidence="ECO:0000250|UniProtKB:P0DL80"
FT DISULFID 17..36
FT /evidence="ECO:0000250|UniProtKB:P0DL80"
SQ SEQUENCE 39 AA; 4405 MW; E572A54E64903422 CRC64;
IFECVFSCDI EKEGKPCKPK GEKKCSGGWK CKIKLCLKI