IED ID | IndEnz0002001090 |
Enzyme Type ID | protease001090 |
Protein Name |
Salivary plasminogen activator alpha 2 EC 3.4.21.68 BAT-PA DSPA alpha-2 T-plasminogen activator |
Gene Name | |
Organism | Desmodus rotundus (Vampire bat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Chiroptera Microchiroptera Phyllostomidae (leaf-nosed bats) Desmodontinae Desmodus Desmodus rotundus (Vampire bat) |
Enzyme Sequence | MVNTMKTKLLCVLLLCGAVFSLPRQETYRQLARGSRAYGVACRDEKTQMIYQQQESWLRPEVRSKRVEHCRCDRGLAQCHTVPVKSCSELRCFNGGTCWQAASFSDFVCQCPKGYTGKQCEVDTHATCYKDQGVTYRGTWSTSESGAQCINWNSNLLTRRTYNGRRSDAITLGLGNHNYCRNPDNNSKPWCYVIKASKFILEFCSVPVCSKATCGLRKYKEPQLHSTGGLFTDITSHPWQAAIFAQNRRSSGERFLCGGILISSCWVLTAAHCFQERYPPQHLRVVLGRTYRVKPGKEEQTFEVEKCIVHEEFDDDTYNNDIALLQLKSGSPQCAQESDSVRAICLPEANLQLPDWTECELSGYGKHKSSSPFYSEQLKEGHVRLYPSSRCTSKFLFNKTVTNNMLCAGDTRSGEIYPNVHDACQGDSGGPLVCMNDNHMTLLGIISWGVGCGEKDIPGVYTKVTNYLGWIRDNMRP |
Enzyme Length | 477 |
Uniprot Accession Number | P15638 |
Absorption | |
Active Site | ACT_SITE 272; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 321; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 428; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Activity toward plasminogen is stimulated in the presence of fibrin I. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.68; |
DNA Binding | |
EC Number | 3.4.21.68 |
Enzyme Function | FUNCTION: Probably essential to support the feeding habits of this exclusively haematophagous animal. Probable potent thrombolytic agent. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (14); Domain (4); Glycosylation (2); Sequence conflict (3); Signal peptide (1) |
Keywords | Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Kringle;Plasminogen activation;Protease;Secreted;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 53,719 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |