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 27-MAR-2024, entry version 97.
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:0031640; P:killing of cells of 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; IPR048997; Stonustoxin-like_helical.
DR InterPro; IPR040581; Thioredoxin_11.
DR PANTHER; PTHR31594; AIG1-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31594:SF16; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF21109; Stonustoxin_helical; 1.
DR Pfam; PF18078; Thioredoxin_11; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//
