ID   VTXB_SYNVE              Reviewed;         696 AA.
AC   Q98993;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Verrucotoxin subunit beta;
DE            Short=VTX subunit beta;
OS   Synanceia verrucosa (Reef stonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Scorpaenoidei; Synanceiidae; Synanceiinae;
OC   Synanceia.
OX   NCBI_TaxID=51996;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=9003430; DOI=10.1016/s0167-4838(96)00187-2;
RA   Garnier P., Ducancel F., Ogawa T., Boulain J.-C., Goudey-Perriere F.,
RA   Perriere C., Menez A.;
RT   "Complete amino-acid sequence of the beta-subunit of VTX from venom of the
RT   stonefish (Synanceia verrucosa) as identified from cDNA cloning
RT   experiments.";
RL   Biochim. Biophys. Acta 1337:1-5(1997).
RN   [2]
RP   FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=7597718; DOI=10.1016/0041-0101(94)00151-w;
RA   Garnier P., Goudey-Perriere F., Breton P., Dewulf C., Petek F.,
RA   Perriere C.;
RT   "Enzymatic properties of the stonefish (Synanceia verrucosa Bloch and
RT   Schneider, 1801) venom and purification of a lethal, hypotensive and
RT   cytolytic factor.";
RL   Toxicon 33:143-155(1995).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9028008; DOI=10.1016/s0041-0101(96)00075-x;
RA   Garnier P., Sauviat M.P., Goudey-Perriere F., Perriere C.;
RT   "Cardiotoxicity of verrucotoxin, a protein isolated from the venom of
RT   Synanceia verrucosa.";
RL   Toxicon 35:47-55(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=17572694; DOI=10.1038/sj.bjp.0707340;
RA   Yazawa K., Wang J.-W., Hao L.-Y., Onoue Y., Kameyama M.;
RT   "Verrucotoxin, a stonefish venom, modulates calcium channel activity in
RT   guinea-pig ventricular myocytes.";
RL   Br. J. Pharmacol. 151:1198-1203(2007).
CC   -!- FUNCTION: This lethal (towards mice) toxin induces hemolytic, cytolytic
CC       and hypotensive activities. Inhibits calcium channels and may activate
CC       ATP-sensitive potassium channels in frog atrial heart muscle. In
CC       guinea-pig ventricular myocytes, it modulates calcium channel activity
CC       through the beta-adrenoceptor-cAMP-PKA pathway (ADRB).
CC       {ECO:0000269|PubMed:17572694, ECO:0000269|PubMed:7597718,
CC       ECO:0000269|PubMed:9028008}.
CC   -!- SUBUNIT: Tetramer composed of 2 alpha and 2 beta subunits.
CC       {ECO:0000269|PubMed:7597718}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=However, no signal peptide has
CC       been found. This protein may follow a novel secretion pathway.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the SNTX/VTX toxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA69254.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y07957; CAA69254.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q98993; -.
DR   SMR; Q98993; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR040581; Thioredoxin_11.
DR   Pfam; PF18078; Thioredoxin_11; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Cytolysis;
KW   G-protein coupled receptor impairing toxin; Glycoprotein; Hemolysis;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..696
FT                   /note="Verrucotoxin subunit beta"
FT                   /id="PRO_0000221557"
FT   DOMAIN          506..696
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
SQ   SEQUENCE   696 AA;  78849 MW;  83CEC6F5E8A37466 CRC64;
     MPSDILVVAA LGRPFTLGML YDARNDKLIP GFTLWEDEVI EESTVESSQP SSAFEIIASD
     SIDDKSSLME IEASLKASFL GGLVEVGGSA KYLNNQKKFK NQSRVTLQYK ATTNFKQLMT
     NLGTKHVEYS ELFENIQATH VVIGILYGAN AFFVFDSNKV DSTNVQEIQG QMEAVIKKIP
     SVEISGKASV QLTSEETDIT NSFSCEFHGD FFLTSNPTTF EDAVKTYQQL PQMMGKDNAV
     PMTVWLVPMV NFYSEAPQLM ADSSTPILRK VRNTLEAIVQ VQMRCNDALD DPTVNLFTEV
     QKKLSDFQII CDDHMSKLQA TIAKKLFAIR SGDEDESALV NLFEENLQSP FNTESLNMWM
     EFEEREINVL KSCMDILTKA KPKVIFNQGV LFKELYDSKV KHGLCYVFTN VTKNDDFLTV
     LNDFLDSPQS RPKKLRPSPK DYWYSYDDIP EMMREKAHLF RNLAKEMNNR CVHFFVTAIN
     NPKQEGAGIH YYRESIQIIH EFTKPHMPGV ETIKDRRELQ WYDCELTLDT ETAHQVLTLS
     EGNKRQCRGV RVTRRSLREF SHFQQVMCHQ GAEWTPLLGV RVAGHVSAGV TYKGISRKTS
     TPDSSLGKNQ KSWVFEYTKK SGYQQIHNGK NARVTVSSIG FKQLGVYLDW PAGTLSFYIG
     QQSLGDSSPH LPHQILRGCL SSLPDWGCTT ESQWSN