Detail Information for IndEnz0002010865
IED ID IndEnz0002010865
Enzyme Type ID protease010865
Protein Name Zinc metalloproteinase-disintegrin-like VAP1
EC 3.4.24.-
Snake venom metalloproteinase
SVMP
Vascular apoptosis-inducing protein 1
Vap-1
Gene Name
Organism Crotalus atrox (Western diamondback rattlesnake)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Crotalus Crotalus atrox (Western diamondback rattlesnake)
Enzyme Sequence MIQVLLVTISLAVFPYQGSSVILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPPVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTQNWESYEPIKKASQSNLTPEQQRYLNAKKYVKLFLVADYIMYLKYGRNLTAVRTRMYDIVNVITPIYHRMNIHVALVGLEIWSNTDKIIVQSSADVTLDLFAKWRATDLLSRKSHDNAQLLTGINFNGPTAGLGYLGGICNTMYSAGIVQDHSKIHHLVAIAMAHEMGHNLGMDHDKDTCTCGTRPCVMAGALSCEASFLFSDCSQKDHREFLIKNMPQCILKKPLKTDVVSPAVCGNYFVEVGEECDCGSPRTCRDPCCDATTCKLRQGAQCAEGLCCDQCRFKGAGTECRAAKDECDMADVCTGRSAECTDRFQRNGQPCKNNNGYCYNGKCPIMADQCIALFGPGATVSQDACFQFNREGNHYGYCRKEQNTKIACEPQDVKCGRLYCFPNSPENKNPCNIYYSPNDEDKGMVLPGTKCADRKACSNGQCVDVTTPY
Enzyme Length 610
Uniprot Accession Number Q9DGB9
Absorption
Active Site ACT_SITE 336; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"
Activity Regulation ACTIVITY REGULATION: Inhibited by EDTA and EGTA, but not by PMSF. {ECO:0000269|PubMed:11071872}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities. It induces apoptosis in vascular endothelial cells (VEC), without degrading extracellular matrix (it cannot cleave collagen) or inhibiting adhesion of VEC. VAP1-induced apoptosis is inhibited by antibodies for integrin alpha-3, alpha-6, beta-1 and CD9. Apoptosis is accompanied by severe cell fragmentation, which is controlled by caspases. {ECO:0000269|PubMed:11071872, ECO:0000269|PubMed:11821125, ECO:0000269|PubMed:15922392, ECO:0000269|PubMed:18657564, ECO:0000269|PubMed:9196035}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (16); Chain (1); Disulfide bond (18); Domain (2); Glycosylation (1); Helix (10); Metal binding (14); Modified residue (1); Motif (1); Propeptide (1); Signal peptide (1); Turn (9)
Keywords 3D-structure;Apoptosis;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue MOD_RES 190; /note=Pyrrolidone carboxylic acid (Glu); /evidence=ECO:0000250|UniProtKB:P0DM89
Post Translational Modification PTM: The N-terminus is blocked. {ECO:0000269|PubMed:19371136}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D X-ray crystallography (3)
Cross Reference PDB 2ERO; 2ERP; 2ERQ;
Mapped Pubmed ID -
Motif MOTIF 467..469; /note=D/ECD-tripeptide
Gene Encoded By
Mass 67,960
Kinetics
Metal Binding METAL 335; /note=Zinc; catalytic; METAL 339; /note=Zinc; catalytic; METAL 345; /note=Zinc; catalytic; METAL 405; /note=Calcium 1; via carbonyl oxygen; METAL 408; /note=Calcium 1; METAL 410; /note=Calcium 1; via carbonyl oxygen; METAL 412; /note=Calcium 1; METAL 415; /note=Calcium 1; METAL 418; /note=Calcium 1; METAL 469; /note=Calcium 2; METAL 470; /note=Calcium 2; via carbonyl oxygen; METAL 472; /note=Calcium 2; METAL 483; /note=Calcium 2; METAL 484; /note=Calcium 2; via carbonyl oxygen
Rhea ID
Cross Reference Brenda