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P81661 (VSPA_BOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Thrombin-like enzyme bothrombin

Short name=SVTLE
EC=3.4.21.74
Alternative name(s):
Reptilase
Venombin A
OrganismBothrops jararaca (Jararaca)
Taxonomic identifier8724 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thrombin-like snake venom serine protease. Aggregates platelets in the presence of exogenous fibrinogen, possibly through interaction with glycoprotein 1b. Activates blood coagulation factor VIII. Has specific fibrinogen clotting activity. Ref.1

Catalytic activity

Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.

Enzyme regulation

Inhibited by diisopropyl fluorophosphate, but not by hirudin. Ref.1

Subunit structure

Monomer. Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.4-8.0 for the clotting activity. Ref.1

Ontologies

Keywords
   Biological processBlood coagulation
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Thrombin-like enzyme bothrombin
PRO_0000088731

Regions

Domain1 – 223223Peptidase S1

Sites

Active site411Charge relay system By similarity
Active site861Charge relay system By similarity
Active site1781Charge relay system By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Probable
Glycosylation1461N-linked (GlcNAc...) Probable
Glycosylation2251N-linked (GlcNAc...) Probable
Disulfide bond7 ↔ 139 By similarity
Disulfide bond26 ↔ 42 By similarity
Disulfide bond74 ↔ 230 By similarity
Disulfide bond118 ↔ 184 By similarity
Disulfide bond150 ↔ 163 By similarity
Disulfide bond174 ↔ 199 By similarity

Secondary structure

............................................. 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81661 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: BFCD46A729D3E8AA

FASTA23225,584
        10         20         30         40         50         60 
VIGGDECDIN EHPFLAFMYY SPQYFCGMTL INQEWVLTAA HCDKTYMRIY LGIHTRSVAN 

        70         80         90        100        110        120 
DDEVIRYPKE KFICPNKKKN VITDKDIMLI RLNRPVKNST HIAPISLPSN PPSVGSVCRI 

       130        140        150        160        170        180 
MGWGAITTSE DTYPDVPHCA NINLFNNTVC REAYNGLPAK TLCAGVLQGG IDTCGGDSGG 

       190        200        210        220        230 
PLICNGQFQG ILSWGSDPCA EPRKPAFYTK VFDYLPWIQS IIAGNKTATC PP 

« Hide

References

[1]"Purification and characterization of bothrombin, a fibrinogen-clotting serine protease from the venom of Bothrops jararaca."
Nishida S., Fujimura Y., Miura S., Ozaki Y., Usami Y., Suzuki M., Titani K., Yoshida E., Sugimoto M., Yoshioka A., Fukui H.
Biochemistry 33:1843-1849(1994) [PubMed: 8110787] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Venom.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA54361.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXMmodel-A1-232[»]
ProteinModelPortalP81661.
SMRP81661. Positions 1-232.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSPA_BOTJA
AccessionPrimary (citable) accession number: P81661
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 64 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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families