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P26324 (VSPF1_CALRH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
Thrombin-like enzyme ancrod

Short name=SVTLE
EC=3.4.21.74
Alternative name(s):
Venombin A
OrganismCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifier8717 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thrombin-like snake venom serine protease that acts as an anticoagulant. It cleaves fibrinogen to split off the A-fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The resulting fibrin polymers are imperfectly formed and much smaller in size (1 to 2 um long) than the fibrin polymers produced by the action of thrombin. These ancrod-induced microthrombi are friable, unstable, urea-soluble and have significantly degraded alpha chains. They do not cross-link to form thrombi. They are markedly susceptible to digestion by plasmin and are rapidly removed from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the removal of fibrinogen from the blood is rapid, occurring within hours following its administration. It does not activate plasminogen and does not degrade preformed, fully cross-linked thrombin fibrin. It also reduces the level of plasminogen activator inhibitor (PAI) and may stimulate the release of tissue plasminogen activator (PLAT) from the endothelium. The profibrinolytic effect of these 2 actions appears to be limited to local microthrombus degradation.

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.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Pharmaceutical use

Used for the treatment of acute ischemic stroke. Until 2002 was available under the brand name Arvin or Arwin (Knoll). Is actually available under the brand name Viprinex (Abbott).

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Pharmaceutical
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 – 234234Thrombin-like enzyme ancrod
PRO_0000088730

Regions

Domain1 – 227227Peptidase S1

Sites

Active site431Charge relay system By similarity
Active site881Charge relay system By similarity
Active site1821Charge relay system By similarity

Amino acid modifications

Glycosylation231N-linked (GlcNAc...) Ref.1
Glycosylation791N-linked (GlcNAc...) Ref.1
Glycosylation991N-linked (GlcNAc...) Ref.1
Glycosylation1481N-linked (GlcNAc...) Ref.1
Glycosylation2291N-linked (GlcNAc...) Ref.1
Disulfide bond7 ↔ 141 By similarity
Disulfide bond28 ↔ 44 By similarity
Disulfide bond78 ↔ 232 By similarity
Disulfide bond120 ↔ 188 By similarity
Disulfide bond152 ↔ 167 By similarity
Disulfide bond178 ↔ 203 By similarity

Sequences

Sequence LengthMass (Da)Tools
P26324 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 3C55F0276B65E5CF

FASTA23426,570
        10         20         30         40         50         60 
VIGGDECNIN EHRFLVAVYE GTNWTFICGG VLIHPEWVIT AEHCARRRMN LVFGMHRKSE 

        70         80         90        100        110        120 
KFDDEQERYP KKRYFIRCNK TRTSWDEDIM LIRLNKPVNN SEHIAPLSLP SNPPIVGSDC 

       130        140        150        160        170        180 
RVMGWGSINR RIDVLSDEPR CANINLHNFT MCHGLFRKMP KKGRVLCAGD LRGRRDSCNS 

       190        200        210        220        230 
DSGGPLICNE ELHGIVARGP NPCAQPNKPA LYTSIYDYRD WVNNVIAGNA TCSP 

« Hide

References

[1]"Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma."
Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. III
FEBS Lett. 297:297-301(1992) [PubMed: 1544412] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
+Additional computationally mapped references.

Web resources

Wikipedia

Ancrod entry

RxMed

Viprinex entry

Cross-references

Sequence databases

PIRS20407.

3D structure databases

ProteinModelPortalP26324.
SMRP26324. Positions 1-233.
ModBaseSearch...

Protein family/group databases

MEROPSS01.178.

PTM databases

GlycoSuiteDBP26324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
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. False negative.
PS00135. TRYPSIN_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSPF1_CALRH
AccessionPrimary (citable) accession number: P26324
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: January 25, 2012
This is version 69 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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families