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Protein

Sarafotoxin-i1

Gene
N/A
Organism
Atractaspis irregularis (Variable burrowing asp) (Elaps irregularis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Vasoconstrictor activity. These toxins cause cardiac arrest probably as a result of coronary vasospasm (By similarity).By similarity
Sarafotoxin-i3: vasoconstrictor activity. Causes cardiac arrest probably as a result of coronary vasospasm (By similarity). Displays low agonistic activities towards endothelin-2 receptor (EDNRB) (displays affinity in the micromolar range).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei105 – 1051Endothelin-receptor binding siteBy similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cardiotoxin, G-protein coupled receptor impairing toxin, Toxin, Vasoactive, Vasoconstrictor

Names & Taxonomyi

Protein namesi
Recommended name:
Sarafotoxin-i1
Short name:
SRTX-i1
Alternative name(s):
Sarafotoxin-i3
Short name:
SRTX-i3
OrganismiAtractaspis irregularis (Variable burrowing asp) (Elaps irregularis)
Taxonomic identifieri512568 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaLamprophiidaeAtractaspidinaeAtractaspis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1094Missing : Drastic 4-orders or magnitude increase in affinity for ET-B receptors. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 84611 PublicationPRO_0000421164Add
BLAST
Peptidei85 – 10925Sarafotoxin-i1PRO_0000421165Add
BLAST
Propeptidei112 – 1187PRO_0000421166

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi85 ↔ 99By similarity
Disulfide bondi87 ↔ 95By similarity

Post-translational modificationi

Different length molecules ranging from 15 (85-99) to 30 amino acids (85-114) have been found in the venom.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDENMR-A85-109[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the endothelin/sarafotoxin family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamiPF00322. Endothelin. 1 hit.
[Graphical view]
PROSITEiPS00270. ENDOTHELIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0DJK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLPRLAAG GLLLLLALAA LDGKPAPPKL LQKLMDGGQR RSEDQAAAGR
60 70 80 90 100
IIDYEDGDEP VAVSVGDTKQ AARALSPLRK PQPLCSCTDM SDLECMNFCH
110
KDVIWINRNR KPSPIQSS
Length:118
Mass (Da):12,722
Last modified:February 6, 2013 - v1
Checksum:iD16BD000685310C1
GO

RNA editingi

Edited at position 106.Curated
RNA editing may explain why no precursor for this sequence have been cloned.Curated

Mass spectrometryi

Molecular mass is 2972.2 Da from positions 85 - 109. Determined by ESI. Monoisotopic mass, sarafotoxin-i1.1 Publication
Molecular mass is 2958.2 Da from positions 85 - 109. Determined by ESI. Monoisotopic mass, sarafotoxin-i3.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061I → V in RNA edited version, Sarafotoxin-i3.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDENMR-A85-109[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamiPF00322. Endothelin. 1 hit.
[Graphical view]
PROSITEiPS00270. ENDOTHELIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of toxins within crude venoms by combined use of Fourier transform mass spectrometry and cloning."
    Quinton L., Le Caer J.P., Phan G., Ligny-Lemaire C., Bourdais-Jomaron J., Ducancel F., Chamot-Rooke J.
    Anal. Chem. 77:6630-6639(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 85-109, MASS SPECTROMETRY, PROBABLE RNA EDITING.
    Tissue: Venom and Venom gland.
  2. "Pharmacological and structural characterization of long-sarafotoxins, a new family of endothelin-like peptides: role of the C-terminus extension."
    Mourier G., Hajj M., Cordier F., Zorba A., Gao X., Coskun T., Herbet A., Marcon E., Beau F., Delepierre M., Ducancel F., Servent D.
    Biochimie 94:461-470(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 85-109, FUNCTION (SARAFOTOXIN-I3), STRUCTURE BY NMR OF 85-109, DISULFIDE BONDS, MUTAGENESIS OF 106-ILE--ASN-109.

Entry informationi

Entry nameiSRTX1_ATRIR
AccessioniPrimary (citable) accession number: P0DJK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: February 6, 2013
Last modified: February 4, 2015
This is version 12 of the entry and version 1 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

External Data

Dasty 3

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 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.