Detail Information for IndEnz0002015814
IED ID IndEnz0002015814
Enzyme Type ID protease015814
Protein Name Venom nerve growth factor
v-NGF
vNGF

Cleaved into: Truncated venom nerve growth factor
Gene Name
Organism Macrovipera lebetina (Levantine viper) (Vipera lebetina)
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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina)
Enzyme Sequence MSMLCYTLIIAFLIGIWAAPKSEDNVSLGSPATPDLSDTSCAKTHEALKTSRNTDQHYPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNADSLNRNIRAKRATHPVHNRGEFSVCDSVSVWVANKTTATDIRGNVVTVMVDVKLNNNVYRQYFFETKCKNPSPVSSGCRGIDAKHWNSYCTTTDTFVRALTMEGNQASWRFIRIDTACVCVISRKNDNFG
Enzyme Length 244
Uniprot Accession Number P25428
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). It promotes neurite outgrowth in rat PC12 pheochromocytoma cells (PubMed:19463841). {ECO:0000250|UniProtKB:P61898, ECO:0000250|UniProtKB:P61899, ECO:0000269|PubMed:19463841}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Disulfide bond (3); Glycosylation (1); Propeptide (1); Sequence conflict (1); Signal peptide (1)
Keywords Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19463841}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:19463841, ECO:0000269|PubMed:4017541}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,318
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda