| IED ID | IndEnz0002015808 |
| Enzyme Type ID | protease015808 |
| Protein Name |
Venom nerve growth factor v-NGF vNGF |
| Gene Name | |
| Organism | Bungarus multicinctus (Many-banded krait) |
| 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 Elapidae Bungarinae Bungarus Bungarus multicinctus (Many-banded krait) |
| Enzyme Sequence | MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPAKSDFSDTNCAQTHEGLKTSRNTDQHHPTPKKSEDQELGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVKFLDTEDTLNRNIWANNENHPVHNQGEHSVCDSISVWVTNKTKATDIKGNTVTVMVDVNLNNEVYKQYFFETKCRNPNPVPSGCRGIDSRHWNSYCTTTDTFVKALTMEGNRASWRFIRIDTACVCVISRKTENF |
| Enzyme Length | 243 |
| Uniprot Accession Number | P34128 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity). {ECO:0000250|UniProtKB:P61898, ECO:0000250|UniProtKB:P61899}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Disulfide bond (3); Glycosylation (1); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,514 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |