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STXB_SYNVE
ID   STXB_SYNVE              Reviewed;         700 AA.
AC   A0ZSK4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Neoverrucotoxin subunit beta;
DE            Short=NeoVTX 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], PROTEIN SEQUENCE OF 2-10, FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, 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; AB262393; BAF41222.1; -; mRNA.
DR   AlphaFoldDB; A0ZSK4; -.
DR   SMR; A0ZSK4; -.
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   Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis; Secreted;
KW   Toxin.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:17023116"
FT   CHAIN           2..700
FT                   /note="Neoverrucotoxin subunit beta"
FT                   /id="PRO_0000353124"
FT   DOMAIN          506..700
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
SQ   SEQUENCE   700 AA;  79500 MW;  00F85473420FEE41 CRC64;
     MPSDILVVAA LGRPFTLGML YDARNDKLIP GFTLWEDEVI EESTVESSQP SSAFEIIASD
     SIDDKSSLMD 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 FNIESLNMWM
     EFEEREINVL KSCMDILTKA KPKVIFNQGV LFKELYDSKV KHGLCYVFTN VTKNDDFLTV
     LNDFLDSPQS RPKKLRPSPK DYWYSYDDIP EMMREKAHLF RNLAKEMNNR CVHFFVTAIN
     NPKQEGAGIH YYRESIQIIH EFTKPHMPGV ETIKDRRELQ WYDCELTLDT ETAHQVLTLS
     EGNKKAVSGS TKSPADHFEK FSHFQQVMCT KGLSGRHYWE LEWSGHVSAG VTYKGISRKT
     STPDSSLGKN QKSWVFEYTK KSGYQQIHNG KNARVTVSSI GFKQLGVYLD WPAGTLSFYM
     VNKAWVTHLH TFHTKFYEAV YPAFLIGDAQ QKVNGQIKLL
 
 
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