ID   STXA_SYNVE              Reviewed;         703 AA.
AC   A0ZSK3;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Neoverrucotoxin subunit alpha;
DE            Short=NeoVTX subunit alpha;
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   ACETYLATION AT SER-2, NUMBER OF DISULFIDE BONDS, AND TOXIC DOSE.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17023116; DOI=10.1016/j.bbagen.2006.08.017;
RA   Ueda A., Suzuki M., Honma T., Nagai H., Nagashima Y., Shiomi K.;
RT   "Purification, properties and cDNA cloning of neoverrucotoxin (neoVTX), a
RT   hemolytic lethal factor from the stonefish Synanceia verrucosa venom.";
RL   Biochim. Biophys. Acta 1760:1713-1722(2006).
CC   -!- FUNCTION: Has hemolytic and lethal activities. Its hemolytic activity
CC       is inhibited by anionic lipids, especially potently by cardiolipin.
CC       {ECO:0000269|PubMed:17023116}.
CC   -!- SUBUNIT: Heterodimer of alpha and beta subunits.
CC       {ECO:0000269|PubMed:17023116}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17023116}.
CC       Note=Secreted into the venom gland lumen. The secretion is proved by
CC       the fact that the complete sequence showed below is found in the venom
CC       gland's lumen, although no signal peptide has been found. This protein
CC       may follow a novel secretion pathway. It has been reported that venom-
CC       secreting cells of stonefishes do not possess Golgi apparatus and rough
CC       endoplasmic reticulum.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Not glycosylated.
CC   -!- PTM: Four intrachain disulfide linkages are present in the heterodimer.
CC       No interchain disulfide bound links the two subunits.
CC   -!- TOXIC DOSE: LD(50) is 0.047 mg/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:17023116}.
CC   -!- SIMILARITY: Belongs to the SNTX/VTX toxin family. {ECO:0000305}.
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DR   EMBL; AB262392; BAF41221.1; -; mRNA.
DR   AlphaFoldDB; A0ZSK3; -.
DR   SMR; A0ZSK3; -.
DR   iPTMnet; A0ZSK3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR040581; Thioredoxin_11.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF18078; Thioredoxin_11; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
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   Acetylation; Cytolysis; Disulfide bond; Hemolysis; Secreted; Toxin.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..703
FT                   /note="Neoverrucotoxin subunit alpha"
FT                   /id="PRO_0000353123"
FT   DOMAIN          508..703
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000305|PubMed:17023116"
SQ   SEQUENCE   703 AA;  79670 MW;  7FC475E4F9A2EA9F CRC64;
     MSSDLVMPAL GRPFTLGMLY DTRREKLIPG FSLFGDETLQ QYQSSNTQRS SEFKIVASDS
     TESKSSAMDI EASLGVSFLG GLVEVGGSAK YLNNTKKYQN QSRVTLKYKA TTIYKQFTAP
     PGTVKVQETV ITQRGLATHV VTGILYGANA FFVFDSDKVE DTNLQDIQGK MEAVIKKIPT
     ISIEGSASVQ LTDEEKSLAS NLSCKFHGDF LLESLPTTFE DAVTTYQTLP TLLGEDGASA
     VPMKVWLVPL KKFFSKAKLL TQEITVSKVR RIHTTLEELY KLKRRANEAM DDKLVQQIPL
     IHDKISNFHQ IFQDYMLTVQ KKIAEKLPLV RAGTESEQSL QKIIDDRAKS PFSNENVSTW
     LEVIEREIAV LKSCAGMVEG TQAKFVSNQT ELDREVLAED VKHALCFVFT SVERNDPYLK
     VLSDYLESPD SKDGKEAVPS TEDKWCFSTR VVLKMKQRAQ TFCDHVNDFE KSRNVGFFVT
     ALENGKFQGA SIYHYKDGSL ATQDFTFPRM PFVQGYKKRS DLLWYACDLT FDRNTINIWV
     SLSDNDTFAA SEHGKRQNYP KHPERFLCYN QVLCNEGLTG KHYWEVEWNG YVDVGVAYIS
     ISRKEDNWVS AIGHNTCSWV FSSIPRAGYV ERYNQRQYYV TVPTPGFKQL GVFLNWPDGS
     LSFYAVSSDE VHHLHTFKTK FTEPVYPAFC LGYRFDHGTV RLL