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P0DL27 · VSP41_BOTPI

Function

function

Snake venom serine protease that interferes with the hemostatic system of the prey. It almost completely degrades both Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen. It presents a higher ability to degrade fibrin clots than BpirSP27. It hydrolyzes chromogenic substrates S-2238 (used for testing thrombin activity), S-2222 (factor Xa), S-2266 (glandular kallikrein and factor XIa), and S-2302 (plasma kallikrein, factor XIa and XIIa). It shows a decrease in the clotting time of human plasma in the presence of increasing doses of the enzyme. Its minimum coagulant dose (MCD) is 20 ug. It promotes platelet aggregation with a maximum of aggregation of 20%, regardless of the concentration increase or the presence of calcium. It also shows 40% inhibition of the hemolytic activity promoted by the complement pathways and possess only a minor role in the induction of edema and pain in rat.

Miscellaneous

Acidic enzyme (pI is 3.7).
Negative results: does not degrade the gamma chain of fibrinogen (FGG). It has no activity on S-2251 (used for testing plasmin activity) (PubMed:22819993).

Activity regulation

Inhibited by serine protease inhibitors PMSF, benzamidine, leupeptin and aprotinin, as well as by copper ions (Cu2+). Not inhibited by metalloprotease inhibitors EDTA, EGTA and 1,10-phenanthroline, as well as by barium (Ba2+) and calcium ion (Ca2+).

pH Dependence

Optimum pH is 6.0-10.5.

Temperature Dependence

Optimum temperature is 4-60 degrees Celsius.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site40Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionserine-type endopeptidase activity
Molecular Functiontoxin activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thrombin-like enzyme BpirSP41
  • EC number
  • Short names
    SVTLE
  • Alternative names
    • Fibrinogen-clotting enzyme
    • Snake venom serine protease (SVSP)

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Bothrops

Accessions

  • Primary accession
    P0DL27

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_00004222771-50Thrombin-like enzyme BpirSP41
Disulfide bond7↔?
Disulfide bond25↔41

Post-translational modification

N-glycosylated.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-50Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    50
  • Mass (Da)
    5,836
  • Last updated
    2013-05-01 v1
  • MD5 Checksum
    120FCAA3BDBB4DACA144DAFC205702EF
VVGGDECDINEHPFLAFLYSHGYFCGLTLINQEWVLTAAHCDRRFMRIYL

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue50

Mass Spectrometry

Molecular mass is 40,639 Da. Determined by MALDI.

Keywords

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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