| IED ID | IndEnz0002015887 |
| Enzyme Type ID | protease015887 |
| Protein Name |
Kallikrein-8 mK8 EC 3.4.21.118 Neuropsin NP Serine protease 19 |
| Gene Name | Klk8 Nrpn Prss19 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGRPPPCAIQPWILLLLFMGAWAGLTRAQGSKILEGRECIPHSQPWQAALFQGERLICGGVLVGDRWVLTAAHCKKQKYSVRLGDHSLQSRDQPEQEIQVAQSIQHPCYNNSNPEDHSHDIMLIRLQNSANLGDKVKPVQLANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCDGMLQGITSWGSDPCGKPEKPGVYTKICRYTTWIKKTMDNRD |
| Enzyme Length | 260 |
| Uniprot Accession Number | Q61955 |
| 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 | ACTIVITY REGULATION: Strongly inhibited by diisopropyl fluorophosphate, leupeptin and (4-amidinophenyl)methanesulfonyl 1-fluoride. {ECO:0000269|PubMed:9556608}. |
| 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. {ECO:0000269|PubMed:10762375, ECO:0000269|PubMed:11880192, ECO:0000269|PubMed:12944500, ECO:0000269|PubMed:16308352, ECO:0000269|PubMed:16537644, ECO:0000269|PubMed:17182622, ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:9556608}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (3); Propeptide (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: By chemical/incision-induced brain injury which leads to increased expression in axon fiber bundles of the peri-lesioned region, by electrically-induced seizure (kindling) in brain, by UV irradiation in skin and by incisional and chemically-induced skin wounding which causes epidermal proliferation and hyperkeratosis. Induced by chemically-induced oxidative stress which leads to increased expression in the hippocampal pyramidal neurons 2 hours after treatment. Levels then decrease, drop to 60% of pretreated control levels at day 7 when avoidance learning is impaired and return to control levels at day 30. Also induced by spinal crush injury which leads to increased expression in spinal cord white matter adjacent to the lesion. Expression increases between days 1-14 post-injury with a peak at day 4. {ECO:0000269|PubMed:10196465, ECO:0000269|PubMed:10421059, ECO:0000269|PubMed:11274744, ECO:0000269|PubMed:14616360, ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:8864305, ECO:0000269|PubMed:9374276, ECO:0000269|PubMed:9749739}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Shows a cytoplasmic distribution in the keratinocytes. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1NPM; |
| Mapped Pubmed ID | 11854276; 11950511; 12390870; 12646205; 15192120; 15203212; 15378660; 15920728; 16602821; 18216192; 18329042; 18513120; 18973680; 19592578; 20152175; 20180635; 21267068; 21508957; 21646406; 21677750; 22358061; 22520925; 22972991; 27701413; 28267150; 29967374; 31103466; 33754057; 9487112; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,524 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:9556608}; KM=540 uM for Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:9556608}; KM=280 uM for D-Val-Leu-Arg-MCA {ECO:0000269|PubMed:9556608}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.118; |