Q2PQJ3 (VSP1_BOTJR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 31.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thrombin-like enzyme BjussuSP-1 Short name=SVTLE BjussuSP-1 EC=3.4.21.- Alternative name(s): Fibrinogen-clotting enzyme Snake venom serine protease 1 Short name=SVSP Thrombin-like enzyme BjussuSP-I Short name=SVTLE BjussuSP-I |
| Organism | Bothrops jararacussu (Jararacussu) |
| Taxonomic identifier | 8726 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops![]() |
Protein attributes
| Sequence length | 232 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Thrombin-like enzyme that shows clotting activity upon human plasma. Shows specific fibrinogenolytic activity for Aalpha chain (FGA). Hydrolyzes fibrin, BAPNA and TAME, as well as chromogenic artificial substrates of the blood coagulation cascasde: S-27654 for factor X (F10), S-2302 for kallikrein (KLK), factor XIa (F11), and XIIa (F12), and S-2266 for kallikrein and factor XIa (F11). Subcutaneous injection into mice induces a mild edema. Intravenous and intramuscular injection reduce plasma fibrinogen concentration and increase the levels of fibrin(ogen) degradation products. Intramuscular injection also promotes an increase in the expression of proMMP-9, but is unable to activate it. Ref.1 Ref.2 Ref.3 |
| Enzyme regulation | Inhibited by PMSF, leupeptin, heparin, and 1.10-phenantroline. Ref.1 Ref.2 |
| Subunit structure | Monomer. Ref.2 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | N-glycosylated. Contains sialic acid residues. Deglycosylation reduces in 50% the formation of fibrin clot. Ref.1 Ref.2 |
| Miscellaneous | Does not show hemorrhagic and myotoxic activities (Ref.2), as well as activity on platelet aggregation and plasmin (represented by the chromogenic substrate S-2251) (Ref.1). |
| Sequence similarities | Belongs to the peptidase S1 family. Snake venom subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Inflammatory response |
| Cellular component | Secreted |
| Ligand | Sialic acid |
| Molecular function | Blood coagulation cascade activating toxin Fibrinolytic toxin Hemostasis impairing toxin Hydrolase Protease Serine protease Toxin |
| PTM | Disulfide bond Glycoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 232 | 232 | Thrombin-like enzyme BjussuSP-1 | PRO_0000296362 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Domain | 1 – 223 | 223 | Peptidase S1 | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Active site | 40 | 1 | Charge relay system By similarity | ||||||||||||||||||||||||||||||||||||||||
| Active site | 85 | 1 | Charge relay system By similarity | ||||||||||||||||||||||||||||||||||||||||
| Active site | 178 | 1 | Charge relay system By similarity | ||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 77 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 129 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 7 ↔ 138 | By similarity | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 25 ↔ 41 | By similarity | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 73 ↔ 230 | By similarity | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 117 ↔ 184 | By similarity | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 149 ↔ 163 | By similarity | |||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 174 ↔ 199 | By similarity | |||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Turn | 9 – 11 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 15 – 29 | 15 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 39 – 41 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 47 – 51 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 63 – 65 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 67 – 72 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 87 – 93 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 116 – 123 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 129 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 137 – 143 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 147 – 150 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 161 – 165 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 181 – 184 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 187 – 194 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 206 – 210 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 211 – 214 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 215 – 223 | 9 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Molecular characterization of BjussuSP-I, a new thrombin-like enzyme with procoagulant and kallikrein-like activity isolated from Bothrops jararacussu snake venom." Sant'Ana C.D., Bernardes C.P., Izidoro L.F., Mazzi M.V., Soares S.G., Fuly A.L., Zingali R.B., Magro A.J., Braz A.S., Fontes M.R., Stabeli R.G., Sampaio S.V., Soares A.M. Biochimie 90:500-507(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, GLYCOSYLATION. Tissue: Venom gland. |
| [2] | "BjussuSP-I: a new thrombin-like enzyme isolated from Bothrops jararacussu snake venom." Sant' Ana C.D., Ticli F.K., Oliveira L.L., Giglio J.R., Rechia C.G., Fuly A.L., Selistre de Araujo H.S., Franco J.J., Stabeli R.G., Soares A.M., Sampaio S.V. Comp. Biochem. Physiol. 151:443-454(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBUNIT, ENZYME REGULATION, GLYCOSYLATION. Tissue: Venom. |
| [3] | "Local and systemic pathophysiological alterations induced by a serine proteinase from the venom of the snake Bothrops jararacussu." Perez A.V., Saravia P., Rucavado A., Sant'Ana C.D., Soares A.M., Gutierrez J.M. Toxicon 49:1063-1069(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Tissue: Venom. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | DQ307451 mRNA. Translation: ABC24687.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q2PQJ3. | ||||||||||||
| SMR | Q2PQJ3. Positions 1-232. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | S01.023. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | HBG013304. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view] | ||||||||||||
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00722. CHYMOTRYPSIN. | ||||||||||||
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. | ||||||||||||
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | VSP1_BOTJR | ||||||||
| Accession | Primary (citable) accession number: Q2PQJ3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal Toxin Annotation Program | ||||||||
| Annotation program | Chordata 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 |

Clusters with
