Reviewed,
UniProtKB/Swiss-Prot Q9PS28 (VSP34_CERCE)
Last modified
June 16, 2009.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Proteinase RP34 EC=3.4.21.74 |
| Organism | Cerastes cerastes (Horned desert viper) |
| Taxonomic identifier | 8697 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Cerastes |
Protein attributes
| Sequence length | 33 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Thrombin-like snake venom serine protease. Displays proteolytic activity toward the natural substrate casein as well as clotting activity on fibrinogen. Shows both arginine-ester hydrolase and amidase activities on synthetic substrates. 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. |
| Subunit structure | Homodimer. Ref.1 |
| Subcellular location | |
| 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 | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Molecular function | Hydrolase Protease Serine protease Toxin |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "A fibrinogen-clotting serine proteinase from Cerastes cerastes (horned viper) venom with arginine-esterase and amidase activities. Purification, characterization and kinetic parameter determination." Laraba-Djebari F., Martin-Eauclaire M.-F., Marchot P. Toxicon 30:1399-1410(1992) [PubMed: 1485336] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A44181. |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q9PS28. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.74. 18553. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. Partial match. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | VSP34_CERCE | ||||||||
| Accession | Primary (citable) accession number: Q9PS28 | ||||||||
| Entry history |
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| 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


