Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0DJK0 (SRTX1_ATRIR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sarafotoxin-i1

Short name=SRTX-i1
Alternative name(s):
Sarafotoxin-i3
Short name=SRTX-i3
OrganismAtractaspis irregularis (Variable burrowing asp) (Elaps irregularis)
Taxonomic identifier512568 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaAtractaspididaeAtractaspis

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vasoconstrictor activity. These toxins cause cardiac arrest probably as a result of coronary vasospasm By similarity. Ref.2

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). Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

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

Sequence similarities

Belongs to the endothelin/sarafotoxin family.

Mass spectrometry

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

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

RNA editing

Edited at position 106.
RNA editing may explain why no precursor for this sequence have been cloned Probable. Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityRNA editing
   DomainSignal
   Molecular functionCardiotoxin
G-protein coupled receptor impairing toxin
Toxin
Vasoactive
Vasoconstrictor
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processregulation of vasoconstriction

Inferred from electronic annotation. Source: InterPro

vasoconstriction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 8461
PRO_0000421164
Peptide85 – 10925Sarafotoxin-i1 Ref.1
PRO_0000421165
Propeptide112 – 1187
PRO_0000421166

Sites

Site1051Endothelin-receptor binding site By similarity

Amino acid modifications

Disulfide bond85 ↔ 99 By similarity
Disulfide bond87 ↔ 95 By similarity

Natural variations

Natural variant1061I → V in RNA edited version, Sarafotoxin-i3.

Experimental info

Mutagenesis106 – 1094Missing: Drastic 4-orders or magnitude increase in affinity for ET-B receptors. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0DJK0 [UniParc].

Last modified February 6, 2013. Version 1.
Checksum: D16BD000685310C1

FASTA11812,722
        10         20         30         40         50         60 
MALLPRLAAG GLLLLLALAA LDGKPAPPKL LQKLMDGGQR RSEDQAAAGR IIDYEDGDEP 

        70         80         90        100        110 
VAVSVGDTKQ AARALSPLRK PQPLCSCTDM SDLECMNFCH KDVIWINRNR KPSPIQSS 

« Hide

References

[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.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDENMR-A85-109[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamPF00322. Endothelin. 1 hit.
[Graphical view]
PROSITEPS00270. ENDOTHELIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSRTX1_ATRIR
AccessionPrimary (citable) accession number: P0DJK0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2013
Last sequence update: February 6, 2013
Last modified: December 11, 2013
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references