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Protein

Stonustoxin subunit beta

Gene
N/A
Organism
Synanceia horrida (Estuarine stonefish) (Scorpaena horrida)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Myotoxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Stonustoxin subunit beta
Short name:
SNTX subunit beta
OrganismiSynanceia horrida (Estuarine stonefish) (Scorpaena horrida)
Taxonomic identifieri13279 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesScorpaenoideiSynanceiidaeSynanceiinaeSynanceia

Subcellular locationi

  • Secreted

  • Note: Secreted into the venom gland lumen. The secretion is proved by the fact that the complete sequence showed below is found in the venom gland's lumen, although no signal peptide has been found. This protein may follow a novel secretion pathway. It has been reported that venom-secreting cells of stonefishes do not possess Golgi apparatus and rough endoplasmic reticulum.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of stonustoxin is 0.017 mg/kg by intravenous injection.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002215562 – 700Stonustoxin subunit betaAdd BLAST699

Post-translational modificationi

Five intrachain disulfide linkages are present in the heterodimer. No interchain disulfide bound links the two subunits.
Not glycosylated.

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.

Structurei

Secondary structure

1700
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Beta strandi47 – 58Combined sources12
Helixi62 – 68Combined sources7
Helixi73 – 80Combined sources8
Helixi90 – 94Combined sources5
Beta strandi104 – 116Combined sources13
Beta strandi140 – 157Combined sources18
Helixi165 – 178Combined sources14
Helixi195 – 200Combined sources6
Beta strandi203 – 211Combined sources9
Helixi220 – 229Combined sources10
Turni230 – 232Combined sources3
Beta strandi240 – 248Combined sources9
Helixi265 – 289Combined sources25
Helixi292 – 296Combined sources5
Helixi298 – 327Combined sources30
Helixi337 – 348Combined sources12
Helixi353 – 378Combined sources26
Helixi388 – 395Combined sources8
Beta strandi401 – 408Combined sources8
Helixi416 – 426Combined sources11
Helixi439 – 441Combined sources3
Helixi443 – 445Combined sources3
Helixi448 – 466Combined sources19
Beta strandi469 – 478Combined sources10
Beta strandi486 – 493Combined sources8
Beta strandi496 – 501Combined sources6
Helixi510 – 512Combined sources3
Helixi516 – 520Combined sources5
Turni530 – 532Combined sources3
Beta strandi538 – 540Combined sources3
Turni541 – 544Combined sources4
Beta strandi545 – 547Combined sources3
Beta strandi562 – 564Combined sources3
Beta strandi566 – 570Combined sources5
Beta strandi575 – 583Combined sources9
Beta strandi588 – 592Combined sources5
Helixi603 – 605Combined sources3
Beta strandi609 – 617Combined sources9
Beta strandi625 – 628Combined sources4
Beta strandi631 – 634Combined sources4
Beta strandi638 – 641Combined sources4
Beta strandi643 – 650Combined sources8
Turni651 – 654Combined sources4
Beta strandi655 – 662Combined sources8
Beta strandi665 – 673Combined sources9
Beta strandi680 – 685Combined sources6
Beta strandi696 – 699Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WVMX-ray3.10B1-700[»]
ProteinModelPortaliQ91453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini506 – 700B30.2/SPRYPROSITE-ProRule annotationAdd BLAST195

Sequence similaritiesi

Belongs to the SNTX/VTX toxin family.Curated
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG079636.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSDILVVAA LGRPFTLGML YDARNDKLIP GFTLWEDEVI EESTLESSQP
60 70 80 90 100
SSAFEIIASD STDDKSSLMD IEASLKASFL GGLVEVGGSA KYLNNQKKFK
110 120 130 140 150
NQSRVTLQYK ATTSFKQLMT NLGTKHVEYS ELFENIQATH VVIGILYGAN
160 170 180 190 200
AFFVFDSNKV DSTNVQEIQG QMEAVIKKIP SVEISGKASV QLTGEETDIT
210 220 230 240 250
NSFSCEFHGD FFLTTNPTTF EDAVKTYQQL PQMMGKDNAV PMTVWLVPMV
260 270 280 290 300
NFYSEAPQLM ADSSTPILRK VRNTLEAIVQ VQMRCNDALD DPTVNLFTEV
310 320 330 340 350
QKKLSDFQKI CDDHMSKLQA TIAKKLFAIR SGDEDESALL NLFEENLQSP
360 370 380 390 400
FNIESLNMWM EFEEREINVL RSCMDILTKA KPKVIFNQGV LFKGLYDSKV
410 420 430 440 450
KHALCYVFTN VTKNDVFLNV LNEFLDSPQS RPKKLRPSPK DYWYSYDDIP
460 470 480 490 500
ETMREKAYLF RNLAKEMNNR CVHFFVTAIH NPKQEGAGIH YYRESIQIID
510 520 530 540 550
EFTKPYMPGV ESIKDRRELQ WYDCELTLDP ETAHQVLTLS EGNKKAVSGN
560 570 580 590 600
TKSPTDHLEK FSHFQQVMCT KGLSGRHYWE LEWSGYVGAG VTYKGIGRKT
610 620 630 640 650
STSDSSLGKN EKSWLFEYST KSGYQQIHNS KKTRVTVSST GFKLLGVYLD
660 670 680 690 700
WPAGTLSFYM VNKAWVTHLH TFHTKFNEAV YPAFLIGDAQ QKVNGQIKLL
Length:700
Mass (Da):79,425
Last modified:January 23, 2007 - v3
Checksum:i53445821AA3A46C1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti506Y → P (PubMed:7725338).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32516 mRNA. Translation: AAC60021.1.
PIRiI51333. A61527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U32516 mRNA. Translation: AAC60021.1.
PIRiI51333. A61527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WVMX-ray3.10B1-700[»]
ProteinModelPortaliQ91453.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG079636.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTXB_SYNHO
AccessioniPrimary (citable) accession number: Q91453
Secondary accession number(s): Q98986
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.