Detail Information for IndEnz0002015813
IED ID IndEnz0002015813
Enzyme Type ID protease015813
Protein Name Venom nerve growth factor
v-NGF
vNGF
Fragment
Gene Name
Organism Echis ocellatus (Ocellated saw-scaled 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) Echis Echis ocellatus (Ocellated saw-scaled viper)
Enzyme Sequence MSMLCYTLIIAFLIGIWAAPKSEDNVSLGSPATPDISDTSCAKTHEALKTSQNTDQHSPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNADSLNRNIRAKRGIHPVHNQGEFSVCDSVNVWVANKTTATDIKGNEVTVMVNVKP
Enzyme Length 168
Uniprot Accession Number P0DMD1
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). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Glycosylation (2); Non-terminal residue (1); Propeptide (1); Region (1); Signal peptide (1)
Keywords Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Growth factor;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 18,478
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda