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P13208 (SRTX_ATREN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sarafotoxin

Cleaved into the following 5 chains:

  1. Sarafotoxin-A, Ser-isoform
    Short name=SRTX-A
    Short name=Sarafotoxin-A
    Alternative name(s):
    S6A
  2. Sarafotoxin-C
    Short name=SRTX-C
    Alternative name(s):
    S6C
  3. Sarafotoxin-B
    Short name=SRTX-B
    Alternative name(s):
    S6B
  4. Sarafotoxin-E
    Short name=SRTX-E
    Alternative name(s):
    S6E
  5. Sarafotoxin-A, Thr-isoform
OrganismAtractaspis engaddensis (Israeli burrowing asp) (Israeli mole viper)
Taxonomic identifier8600 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Atractaspididae › Atractaspis ›

Protein attributes

Sequence length543 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.

Sarafotoxin-B: vasoconstrictor activity. Causes cardiac arrest probably as a result of coronary vasospasm By similarity. Displays high agonistic activities towards endothelin-2 receptor (EDNRB) (displays affinity in the picomolar range) and endothelin-1 receptor (EDNRA) (lower affinities) (Ref.6).

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

Sarafotoxin-A and sarafotoxin-B: LD50 is 0.015 mg/kg by intravenous injection into mice (Ref.3). Ref.2

Sarafotoxin-C: LD50 is 0.3 mg/kg by intravenous injection into mice. Ref.2

Sequence similarities

Belongs to the endothelin/sarafotoxin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionCardiotoxin
G-protein coupled receptor impairing toxin
Toxin
Vasoactive
Vasoconstrictor
   PTMDisulfide 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 – 6946
PRO_0000008123
Peptide70 – 9021Sarafotoxin-A, Ser-isoform
PRO_0000008124
Propeptide92 – 10918
PRO_0000008125
Peptide110 – 13021Sarafotoxin-C
PRO_0000008126
Propeptide132 – 14918
PRO_0000008127
Peptide150 – 17021Sarafotoxin-B
PRO_0000008128
Propeptide172 – 18918
PRO_0000008129
Peptide190 – 21021Sarafotoxin-C
PRO_0000008130
Propeptide212 – 22918
PRO_0000008131
Peptide230 – 25021Sarafotoxin-C
PRO_0000008132
Propeptide252 – 26918
PRO_0000008133
Peptide270 – 29021Sarafotoxin-E
PRO_0000008134
Propeptide292 – 30918
PRO_0000008135
Peptide310 – 33021Sarafotoxin-A, Ser-isoform
PRO_0000008136
Propeptide332 – 34918
PRO_0000008137
Peptide350 – 37021Sarafotoxin-C
PRO_0000008138
Propeptide372 – 38918
PRO_0000008139
Peptide390 – 41021Sarafotoxin-C
PRO_0000008140
Propeptide412 – 42918
PRO_0000008141
Peptide430 – 45021Sarafotoxin-B
PRO_0000008142
Propeptide452 – 46918
PRO_0000008143
Peptide470 – 49021Sarafotoxin-A, Ser-isoform
PRO_0000008144
Propeptide492 – 50918
PRO_0000008145
Peptide510 – 53021Sarafotoxin-A, Thr-isoform
PRO_0000008146
Propeptide532 – 54312
PRO_0000008147

Regions

Repeat51 – 90401
Repeat91 – 130402
Repeat131 – 170403
Repeat171 – 210404
Repeat211 – 250405
Repeat251 – 290406
Repeat291 – 330407
Repeat331 – 370408
Repeat371 – 410409
Repeat411 – 4504010
Repeat451 – 4904011
Repeat491 – 5304012
Region51 – 53048012 X 40 AA tandem repeats

Sites

Site901Endothelin-receptor binding site By similarity
Site1301Endothelin-receptor binding site By similarity
Site1701Endothelin-receptor binding site By similarity
Site2101Endothelin-receptor binding site By similarity
Site2501Endothelin-receptor binding site By similarity
Site2901Endothelin-receptor binding site By similarity
Site3301Endothelin-receptor binding site By similarity
Site3701Endothelin-receptor binding site By similarity
Site4101Endothelin-receptor binding site By similarity
Site4501Endothelin-receptor binding site By similarity
Site4901Endothelin-receptor binding site By similarity
Site5301Endothelin-receptor binding site By similarity

Amino acid modifications

Disulfide bond70 ↔ 84 By similarity
Disulfide bond72 ↔ 80 By similarity
Disulfide bond110 ↔ 124 By similarity
Disulfide bond112 ↔ 120 By similarity
Disulfide bond150 ↔ 164 Ref.5
Disulfide bond152 ↔ 160 Ref.5
Disulfide bond190 ↔ 204 By similarity
Disulfide bond192 ↔ 200 By similarity
Disulfide bond230 ↔ 244 By similarity
Disulfide bond232 ↔ 240 By similarity
Disulfide bond270 ↔ 284 By similarity
Disulfide bond272 ↔ 280 By similarity
Disulfide bond310 ↔ 324 By similarity
Disulfide bond312 ↔ 320 By similarity
Disulfide bond350 ↔ 364 By similarity
Disulfide bond352 ↔ 360 By similarity
Disulfide bond390 ↔ 404 By similarity
Disulfide bond392 ↔ 400 By similarity
Disulfide bond430 ↔ 444 Ref.5
Disulfide bond432 ↔ 440 Ref.5
Disulfide bond470 ↔ 484 By similarity
Disulfide bond472 ↔ 480 By similarity
Disulfide bond510 ↔ 524 By similarity
Disulfide bond512 ↔ 520 By similarity

Experimental info

Mutagenesis1701W → WVNRN or WDEP: Drastic decrease in affinity for ET-B receptors (3 and 5-orders or magnitude for VNRN and DEP, respectively). Ref.6
Mutagenesis4501W → WVNRN or DEP: Drastic decrease in affinity for ET-B receptors (3 and 5-orders or magnitude for VNRN and DEP, respectively). Ref.6

Secondary structure

1 ..... 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13208 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: DF84A9631392FE4A

FASTA54362,326
        10         20         30         40         50         60 
MALLPRLAAG GLLLLLALAA LEGKPAPSAL SQLLEKRSED QAAAGRIIDG GDTKQAARDP 

        70         80         90        100        110        120 
SPQRNVEPLC SCKDMSDKEC LNFCHQDVIW RDTKQAARDP SPQRNVEPLC TCNDMTDEEC 

       130        140        150        160        170        180 
LNFCHQDVIW RDTKQAARDP SPQRNVEPLC SCKDMTDKEC LYFCHQDVIW RDTKQAARDP 

       190        200        210        220        230        240 
SPQRNVEPLC TCNDMTDEEC LNFCHQDVIW RDTKQAARDP SPQRNVEPLC TCNDMTDEEC 

       250        260        270        280        290        300 
LNFCHQDVIW RDTKQAARDP SPQRNVEPLC TCKDMTDKEC LYFCHQGIIW RDTKQAARDP 

       310        320        330        340        350        360 
SPQRNVEPLC SCKDMSDKEC LNFCHQDVIW RDTKQAARDP SPQRNVEPLC TCNDMTDEEC 

       370        380        390        400        410        420 
LNFCHQDVIW RDTKQAARDP SPQRNVEPLC TCNDMTDEEC LNFCHQDVIW RDTKQAARDP 

       430        440        450        460        470        480 
SPQRNVEPLC SCKDMTDKEC LYFCHQDVIW RDTKQAARDP SPQRNVEPLC SCKDMSDKEC 

       490        500        510        520        530        540 
LNFCHQDVIW RDTKQAARDP SPQRNVEPLC SCKDMTDKEC LNFCHQDVIW KNADTSANPE 


FLG

« Hide

References

[1]"Cloning and sequence analysis of cDNAs encoding precursors of sarafotoxins. Evidence for an unusual 'rosary-type' organization."
Ducancel F., Matre V., Dupont C., Lajeunesse E., Wollberg Z., Bdolah A., Kochva E., Boulain J.-C., Menez A.
J. Biol. Chem. 268:3052-3055(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Sarafotoxins S6: several isotoxins from Atractaspis engaddensis (burrowing asp) venom that affect the heart."
Takasaki C., Tamiya N., Bdolah A., Wollberg Z., Kochva E.
Toxicon 26:543-548(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (SARAFOTOXINS A; B AND C), LETHAL DOSE.
Tissue: Venom.
[3]"Sarafotoxin, a novel vasoconstrictor peptide: phosphoinositide hydrolysis in rat heart and brain."
Kloog Y., Ambar I., Sokolovsky M., Kochva E., Wollberg Z., Bdolah A.
Science 242:268-270(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (SARAFOTOXINS A; B AND C).
Tissue: Venom.
[4]"Cloning and sequence analysis of a snake, Atractaspis engaddensis gene encoding sarafotoxin S6c."
Takasaki C., Itoh Y., Onda H., Fujino M.
Biochem. Biophys. Res. Commun. 189:1527-1533(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-130.
Tissue: Liver.
[5]"Studies on the disulfide bridges of sarafotoxins. Chemical synthesis of sarafotoxin S6B and its homologue with different disulfide bridges."
Aimoto S., Hojoh H., Takasaki C.
Biochem. Int. 21:1051-1057(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, SYNTHESIS OF SARAFOTOXIN B.
[6]"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: FONCTION, TOXIN TARGET, MUTAGENESIS OF TRP-170 AND TRP-450.
[7]"Conformation of sarafotoxin-6b in aqueous solution determined by NMR spectroscopy and distance geometry."
Mills R.G., Atkins A.R., Harvey T., Junius F.K., Smith R., King G.F.
FEBS Lett. 282:247-252(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SARAFOTOXIN B.
[8]"1H NMR study of the solution structure of sarafotoxin-S6b."
Aumelas A., Chiche L., Mahe E., Le-Nguyen D., Sizun P., Berthault P., Perly B.
Neurochem. Int. 18:471-475(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SARAFOTOXIN B.
[9]"1H NMR studies of sarafotoxin SRTb, a nonselective endothelin receptor agonist, and IRL 1620, an ETB receptor-specific agonist."
Atkins A.R., Martin R.C., Smith R.
Biochemistry 34:2026-2033(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SARAFOTOXIN B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L07528 mRNA. Translation: AAA48515.1.
D13322 Genomic DNA. Translation: BAA02579.2.
PIRA46601.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SRBNMR-A430-450[»]
ProteinModelPortalP13208.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG017852.

Family and domain databases

InterProIPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamPF00322. Endothelin. 12 hits.
[Graphical view]
SMARTSM00272. END. 12 hits.
[Graphical view]
PROSITEPS00270. ENDOTHELIN. 12 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13208.

Entry information

Entry nameSRTX_ATREN
AccessionPrimary (citable) accession number: P13208
Secondary accession number(s): P13209, P13210
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1994
Last modified: May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents