IED ID | IndEnz0002010889 |
Enzyme Type ID | protease010889 |
Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase-4 SVMP EC 3.4.24.- ; Disintegrin bitisgabonin Bitisgabonin-1 Bitisgabonin-2 Fragment |
Gene Name | |
Organism | Bitis gabonica (Gaboon adder) (Gaboon viper) |
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 Viperinae (vipers) Bitis Bitis gabonica (Gaboon adder) (Gaboon viper) |
Enzyme Sequence | KYENVEKGDEAPKKCGVTHTNLESDEPIEKASQLFGTSEQQRFDPRHIELVIVADHGMVMKHNGDLTAVRTWLHQIGNNLNVMFADLNIRITMAGLEMWSEKDLIDIQSAASETLRLFGEWRERYLLNRRMHDNAQLLTTVNLDGDTVGLAYVGGMCDPKNSVGIVQDHSRIAREVAATMAHELGHNLGMAHDGNQCNCGANGCVMSEEIIERTSYQFSDCSKEEYRTFLDNHNPQRILNEPLRTDTVSTPVYGNVLQNSPHPCCDPVTCKPKAWEHCISGPCCRDCKFLRPGTVCRVARGDWNDDFCTGRSSECESNPWNFWNH |
Enzyme Length | 325 |
Uniprot Accession Number | Q6T271 |
Absorption | |
Active Site | ACT_SITE 183; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: [Snake venom metalloproteinase-4]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin bitisgabonin]: In dimer with gabonin-1 (bitisgabonin-1), is a potent inhibitor of the adhesion of the RGD-dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to immobilized fibronectin. {ECO:0000269|PubMed:17203976}.; FUNCTION: [Disintegrin bitisgabonin]: In dimer with gabonin-2 (bitisgabonin-2), preferentially inhibits the adhesion of the alpha-4/beta-1 (ITGA4/ITGB1) and alpha-9/beta-1 (ITGA9/ITGB1) integrins to VCAM-1 and acts also as a strong antagonist of alpha-5/beta-1 (ITGA5/ITGB1). {ECO:0000269|PubMed:17203976}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (2); Disulfide bond (8); Domain (2); Metal binding (3); Modified residue (2); Motif (1); Non-terminal residue (1); Propeptide (2) |
Keywords | Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17203976}. |
Modified Residue | MOD_RES 40; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250; MOD_RES 258; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:17203976 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 300..302; /note=Cell attachment site |
Gene Encoded By | |
Mass | 36,670 |
Kinetics | |
Metal Binding | METAL 182; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 186; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 192; /note=Zinc; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |