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Reviewed, UniProtKB/Swiss-Prot P33588 (VSP1_AGKBI)

Last modified June 16, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ancrod
    EC=3.4.21.74
Alternative name(s):
    Venombin-A
    Protein C activator
    ACC-C
OrganismAgkistrodon bilineatus (Cantil) (Tropical moccasin)
Taxonomic identifier8718 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Thrombin-like snake venom serine protease. Activates protein C.

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.

Subcellular location

Secreted Potential.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
Toxin
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Ancrod
PRO_0000088724

Regions

Domain1 – ›20›20Peptidase S1

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P33588-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6E99F8B4CC53EFE1

FASTA202,191
        10         20 
VVGGDECNIN EHRSLALMYA 

« Hide

References

[1]"Isolation and characterization of a protein C activator from tropical moccasin venom."
Nakagaki T., Kazim A.L., Kisiel W.
Thromb. Res. 58:593-602(1990) [PubMed: 2385829] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.

Cross-references

Sequence databases

PIRA60489.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSS01.178.

Phylogenomic databases

HOVERGENP33588.

Enzyme and pathway databases

BRENDA3.4.21.74. 279476.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. Partial match.
PS00134. TRYPSIN_HIS. Partial match.
PS00135. TRYPSIN_SER. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVSP1_AGKBI
AccessionPrimary (citable) accession number: P33588
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents