Reviewed,
UniProtKB/Swiss-Prot P82807 (FA10V_NOTSC)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Venom coagulation factor Xa-like protease EC=3.4.21.6 Cleaved into the following 2 chains: 1- Recommended name: Venom coagulation factor Xa-like protease light chain 2- Recommended name: Venom coagulation factor Xa-like protease heavy chain |
| Organism | Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake) |
| Taxonomic identifier | 70142 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Notechis |
Protein attributes
| Sequence length | 98 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Act as a toxin in venom by activating thrombin. It is a procoagulant protein functionally similar to blood coagulation factor Xa. |
| Catalytic activity | Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. |
| Subunit structure | The two chains are formed from a single-chain precursor and are held together by 1 or more disulfide bonds. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 Gla (gamma-carboxy-glutamate) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Ligand | Calcium |
| Molecular function | Hydrolase Toxin |
| PTM | Disulfide bond Gamma-carboxyglutamic acid |
| 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 proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred 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 – 40 | 40 | Venom coagulation factor Xa-like protease light chain | PRO_0000027819 | |||||||
| Chain | 41 – ›98 | ›58 | Venom coagulation factor Xa-like protease heavy chain | PRO_0000027821 | |||||||
Regions | |||||||||||
| Domain | 1 – 40 | 40 | Gla | ||||||||
| Region | 41 – 98 | 58 | Catalytic By similarity | ||||||||
Sites | |||||||||||
| Active site | 91 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 6 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 7 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 14 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 16 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 19 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 20 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 25 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 26 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 29 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 32 | 1 | 4-carboxyglutamate | ||||||||
| Modified residue | 35 | 1 | 4-carboxyglutamate | ||||||||
| Disulfide bond | 17 ↔ 22 | By similarity | |||||||||
| Disulfide bond | 47 ↔ 52 | By similarity | |||||||||
| Disulfide bond | 67 ↔ ? | By similarity | |||||||||
Experimental info | |||||||||||
| Non-adjacent residues | 40 – 41 | 2 | |||||||||
| Non-adjacent residues | 78 – 79 | 2 | |||||||||
| Non-terminal residue | 98 | 1 | |||||||||
Sequences
References
| [1] | "Identification and purification of vitamin K-dependent proteins and peptides with monoclonal antibodies specific for gamma-carboxyglutamyl (Gla) residues." Brown M.A., Stenberg L.M., Persson U., Stenflo J. J. Biol. Chem. 275:19795-19802(2000) [PubMed: 10779512] [Abstract] Cited for: PROTEIN SEQUENCE, CHARACTERIZATION. Tissue: Venom. |
Cross-references
3D structure databases | |
|---|---|
| HSSP | HSSP built from PDB template 1CFH based on UniProtKB P00740. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.425. |
Phylogenomic databases | |
| HOVERGEN | P82807. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.6. 292759. |
Family and domain databases | |
| InterPro | IPR017857. Coagulation_fac_subset_Gla. IPR002383. Coagulation_factor_Gla. IPR000294. GLA_domain. IPR001254. Peptidase_S1_S6. [Graphical view] |
| Gene3D | G3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit. |
| Pfam | PF00594. Gla. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00001. GLABLOOD. |
| SMART | SM00069. GLA. 1 hit. [Graphical view] |
| PROSITE | PS00011. GLA_1. False negative. PS50998. GLA_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FA10V_NOTSC | ||||||||
| Accession | Primary (citable) accession number: P82807 | ||||||||
| 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


