| Identification |
|---|
| HMDB Protein ID
| HMDBP13498 |
| Secondary Accession Numbers
| None |
| Name
| Zinc metalloproteinase/disintegrin |
| Synonyms
|
Not Available
|
| Gene Name
| Not Available |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| fibrinolytic and fibrinogenolytic metalloproteinase that hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen. Its fibrinolytic activity is direct, without any plasminogen activation. Also hydrolyzes casein and B-chain of oxidized insulin. Inhibits ADP-induced and collagen-induced platelet aggregation. Shows low hemorrhagic activity. Cleaves the plasma proteinase inhibitors alpha(2)-macroglobulin (A2M) and pregnancy zone protein (PZP), and is inhibited by them. The metalloprotease has no strict P1-P1' specificity requirement. Hydrolysis at sites with a Pro residue at P1 is observed with bradykinin, substance P, PZP and alpha chain fibrinogen (FGA) (PubMed:11910177).poor inhibitor of platelet aggregation. The disintegrin inhibits the adhesion of the alpha-4/beta-1 (ITGA4/ITGB1) integrin to VCAM-1. Inhibition on alpha-2b/beta-3 (ITGA2B/ITGB3) is low (By similarity). |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Cellular Component |
| extracellular region |
| Molecular Function |
| metal ion binding |
| toxin activity |
| metalloendopeptidase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| 53479.745 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q98995 |
| UniProtKB/Swiss-Prot Entry Name
| VM2L2_MACLB |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Siigur J, Aaspollu A, Tonismagi K, Trummal K, Samel M, Vija H, Subbi J, Siigur E: Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis. Haemostasis. 2001 May-Dec;31(3-6):123-32. doi: 10.1159/000048055. [PubMed:11910177 ]
- Siigur E, Aaspollu A, Tu AT, Siigur J: cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom. Biochem Biophys Res Commun. 1996 Jul 5;224(1):229-36. doi: 10.1006/bbrc.1996.1012. [PubMed:8694817 ]
- Siigur E, Siigur J: Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom. Biochim Biophys Acta. 1991 Jul 8;1074(2):223-9. doi: 10.1016/0304-4165(91)90156-b. [PubMed:2065076 ]
- Siigur J, Samel M, Tonismagi K, Subbi J, Siigur E, Tu AT: Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom. Thromb Res. 1998 Apr 1;90(1):39-49. doi: 10.1016/s0049-3848(98)00009-7. [PubMed:9678676 ]
- Saidi N, Samel M, Siigur J, Jensen PE: Lebetase, an alpha(beta)-fibrin(ogen)olytic metalloproteinase of Vipera lebetina snake venom, is inhibited by human alpha-macroglobulins. Biochim Biophys Acta. 1999 Sep 14;1434(1):94-102. doi: 10.1016/s0167-4838(99)00164-8. [PubMed:10556563 ]
|
