IED ID | IndEnz0002003597 |
Enzyme Type ID | protease003597 |
Protein Name |
Kallikrein-8 EC 3.4.21.118 Brain serine protease 1 Neuropsin NP Serine protease 19 |
Gene Name | Klk8 Bsp1 Nrpn Prss19 |
Organism | Rattus norvegicus (Rat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MGRPPPCAIQTWILLFLLMGAWAGLTRAQGSKILEGQECKPHSQPWQTALFQGERLVCGGVLVGDRWVLTAAHCKKDKYSVRLGDHSLQKRDEPEQEIQVARSIQHPCFNSSNPEDHSHDIMLIRLQNSANLGDKVKPIELANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCNGVLQGITTWGSDPCGKPEKPGVYTKICRYTNWIKKTMGKRD |
Enzyme Length | 260 |
Uniprot Accession Number | O88780 |
Absorption | |
Active Site | ACT_SITE 73; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 212; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.; EC=3.4.21.118; |
DNA Binding | |
EC Number | 3.4.21.118 |
Enzyme Function | FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
Keywords | Cytoplasm;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shows a cytoplasmic distribution in the keratinocytes. {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 28,510 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.118; |