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Q6RY98 (SRTXL_ATRMM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 36. 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:
Long-sarafotoxin

Short name=L-SRTX

Cleaved into the following 6 chains:

  1. Sarafotoxin-m
    Short name=SRTX-m
  2. Sarafotoxin-m1
    Short name=SRTX-m1
  3. Sarafotoxin-m2
    Short name=SRTX-m2
  4. Sarafotoxin-m3
    Short name=SRTX-m3
  5. Sarafotoxin-m4
    Short name=SRTX-m4
  6. Sarafotoxin-m5
    Short name=SRTX-m5
OrganismAtractaspis microlepidota microlepidota
Taxonomic identifier172021 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaAtractaspididaeAtractaspis

Protein attributes

Sequence length351 AA.
Sequence statusFragment.
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. The major effects of sarafotoxin-m are a progressive decrease in heart rate (bradycardia) that turns into an arrhythmic phase that is followed by an A-V block. Ref.1

Sarafotoxin-m: 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). Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Toxic dose

Sarafotoxin-m: LD50 is 27-37 µg/kg by intravenous injection into mice. Ref.1

Sequence similarities

Belongs to the endothelin/sarafotoxin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   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

Peptide‹1 – 5›5Sarafotoxin-m5
PRO_0000315373
Propeptide6 – 2924
PRO_0000315374
Peptide30 – 5324Sarafotoxin-m Ref.1
PRO_5000092481
Propeptide54 – 7724
PRO_0000315375
Peptide78 – 10124Sarafotoxin-m1
PRO_5000092482
Propeptide102 – 12524
PRO_0000315376
Peptide126 – 14924Sarafotoxin-m3
PRO_5000092483
Propeptide150 – 17324
PRO_0000315377
Peptide174 – 19724Sarafotoxin-m2
PRO_5000092484
Propeptide198 – 22124
PRO_0000315378
Peptide222 – 24524Sarafotoxin-m2
PRO_5000092485
Propeptide246 – 26924
PRO_0000315379
Peptide270 – 29324Sarafotoxin-m
PRO_5000092486
Propeptide294 – 31724
PRO_0000315380
Peptide318 – 34124Sarafotoxin-m4
PRO_5000092487
Propeptide342 – 35110
PRO_0000315381

Regions

Repeat6 – 53481
Repeat54 – 101482
Repeat102 – 149483
Repeat150 – 197484
Repeat198 – 245485
Repeat246 – 293486
Repeat294 – 341487
Region6 – 3413367 X 48 AA tandem repeats

Sites

Site21Endothelin-receptor binding site By similarity
Site501Endothelin-receptor binding site By similarity
Site981Endothelin-receptor binding site By similarity
Site1461Endothelin-receptor binding site By similarity
Site1941Endothelin-receptor binding site By similarity
Site2421Endothelin-receptor binding site By similarity
Site2901Endothelin-receptor binding site By similarity
Site3381Endothelin-receptor binding site By similarity

Amino acid modifications

Disulfide bond30 ↔ 44 Ref.2
Disulfide bond32 ↔ 40 Ref.2
Disulfide bond78 ↔ 92 By similarity
Disulfide bond80 ↔ 88 By similarity
Disulfide bond126 ↔ 140 By similarity
Disulfide bond128 ↔ 136 By similarity
Disulfide bond174 ↔ 188 By similarity
Disulfide bond176 ↔ 184 By similarity
Disulfide bond222 ↔ 236 By similarity
Disulfide bond224 ↔ 232 By similarity
Disulfide bond270 ↔ 284 By similarity
Disulfide bond272 ↔ 280 By similarity
Disulfide bond318 ↔ 332 By similarity
Disulfide bond320 ↔ 328 By similarity

Experimental info

Mutagenesis51 – 533Missing: Drastic 4-orders or magnitude increase in affinity for ET-B receptors. Ref.2
Non-terminal residue11

Secondary structure

..... 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6RY98 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F901846C8D6E01CC

FASTA35140,341
        10         20         30         40         50         60 
IWDEPVVVSA RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW DEPVVVSVRD 

        70         80         90        100        110        120 
TEEAARVPSP QKRPQPRCSC NDMNDKECMY FCHQDVIWDE PVVVSVRDTE EAARVPSPQK 

       130        140        150        160        170        180 
RSQPRCSCND MNDKECVYFC HLDIIWDEPV VVSVRDTEEA TRVPSPQKRS QPLCSCNDIN 

       190        200        210        220        230        240 
DKECMYFCHQ DIIWDEPVVV SVRDTEEAAR VPSPQKRSQP LCSCNDINDK ECMYFCHQDI 

       250        260        270        280        290        300 
IWDEPVVVSV RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW DEPVVVSVQD 

       310        320        330        340        350 
TEEAARVPSP QKRSQPLCSC NNMSDKECLN FCNLDIIWEN VDTSADPEFL G 

« Hide

References

[1]"Long-sarafotoxins: characterization of a new family of endothelin-like peptides."
Hayashi M.A.F., Ligny-Lemaire C., Wollberg Z., Wery M., Galat A., Ogawa T., Muller B.H., Lamthanh H., Doljansky Y., Bdolah A., Stoecklin R., Ducancel F.
Peptides 25:1243-1251(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-53; 78-101; 126-149; 174-197; 222-245; 270-293 AND 318-341, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE, SYNTHESIS OF SARAFOTOXIN-M, IDENTIFICATION BY MASS SPECTROMETRY.
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: STRUCTURE BY NMR OF SARAFOTOXIN-M, DISULFIDE BONDS, MUTAGENESIS OF 51-ASP--PRO-53.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY485934 mRNA. Translation: AAR84382.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LDFNMR-A270-293[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG017852.

Family and domain databases

InterProIPR020475. Bibrotoxin/Sarafotoxin-D.
IPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamPF00322. Endothelin. 7 hits.
[Graphical view]
PRINTSPR00365. ENDOTHELIN.
SMARTSM00272. END. 7 hits.
[Graphical view]
PROSITEPS00270. ENDOTHELIN. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ6RY98.

Entry information

Entry nameSRTXL_ATRMM
AccessionPrimary (citable) accession number: Q6RY98
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references