Reviewed,
UniProtKB/Swiss-Prot P26324 (VSP1_AGKRH)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ancrod EC=3.4.21.74 Alternative name(s): Venombin-A Protein C activator ACC-C |
| Organism | Agkistrodon rhodostoma (Malayan pit viper) (Calloselasma rhodostoma) |
| Taxonomic identifier | 8717 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Calloselasma |
Protein attributes
| Sequence length | 234 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Thrombin-like snake venom serine protease. Cleaves fibrinopeptides AM, AO, and AY; the aberrant fibrinogen is then incapable of being cross-linked, forming easily dispersible clots. |
| 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 | |
| Tissue specificity | Expressed by the venom gland. |
| Pharmaceutical use | Used for the treatment of acute ischemic stroke. Until 2002 was available under the name Arvin (Knoll). Is actually available under the name Viprinex (Abbott). |
| Sequence similarities | Belongs to the peptidase S1 family. Snake venom subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Hydrolase Protease Serine protease Toxin |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Direct protein sequencing Pharmaceutical |
| Gene Ontology (GO) | |
| Biological process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 234 | 234 | Ancrod | PRO_0000088730 | |||||||
Regions | |||||||||||
| Domain | 1 – 227 | 227 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 43 | 1 | Charge relay system By similarity | ||||||||
| Active site | 88 | 1 | Charge relay system By similarity | ||||||||
| Active site | 182 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 23 | 1 | N-linked (GlcNAc...) Ref.1 | ||||||||
| Glycosylation | 79 | 1 | N-linked (GlcNAc...) Ref.1 | ||||||||
| Glycosylation | 99 | 1 | N-linked (GlcNAc...) Ref.1 | ||||||||
| Glycosylation | 148 | 1 | N-linked (GlcNAc...) Ref.1 | ||||||||
| Glycosylation | 229 | 1 | N-linked (GlcNAc...) Ref.1 | ||||||||
| Disulfide bond | 7 ↔ 141 | By similarity | |||||||||
| Disulfide bond | 28 ↔ 44 | By similarity | |||||||||
| Disulfide bond | 78 ↔ 232 | By similarity | |||||||||
| Disulfide bond | 120 ↔ 188 | By similarity | |||||||||
| Disulfide bond | 152 ↔ 167 | By similarity | |||||||||
| Disulfide bond | 178 ↔ 203 | By similarity | |||||||||
Sequences
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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. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S20407. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BQY based on UniProtKB Q91516. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.178. |
PTM databases | |
| GlycoSuiteDB | P26324. |
Phylogenomic databases | |
| HOVERGEN | P26324. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.74. 18614. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VSP1_AGKRH | ||||||||
| Accession | Primary (citable) accession number: P26324 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


