| IED ID | IndEnz0002015752 |
| Enzyme Type ID | protease015752 |
| Protein Name |
Kallikrein-14 EC 3.4.21.- Glandular kallikrein KLK14 mGK14 Kallikrein related-peptidase 14 |
| Gene Name | Klk14 Gk14 |
| 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 | MFLLLIILQALAVAIAQSQGDHKIIGGYRCVRNSQPWQVALQAGPGHRFLCGGVLLSDQWVITAAHCARPILHVALGKHNIRRWEATQQVVRVARQVPHPQYQPQAHDNDLMLLKLQKKVRLGRAVKTISVASSCASPGTPCRVSGWGTIASPIARYPTALQCVNVNIMSEQACHRAYPGIITSGMVCAGVPEGGKDSCQGDSGGPLVCGGQLQGLVSWGMERCAMPGYPGVYANLCNYHSWIQRTMQSN |
| Enzyme Length | 250 |
| Uniprot Accession Number | Q8CGR5 |
| Absorption | |
| Active Site | ACT_SITE 66; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 203; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA1, SERPINC1, SERPINE1, SERPINF2, aprotinin, soybean, trypsin inhibitor and leupeptin. Inhibited by serine protease inhibitor SPINK5. Has an autoproteolytic activity which may have a regulatory effect. Activated by citrate and inhibited by zinc and to a lower extent by manganese (By similarity). {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumor progression including growth, invasion and angiogenesis (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Domain (1); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage of the activation peptide produces the active enzyme. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12399446; 15192120; 15203212; 15331780; 16602821; 19906978; 21267068; 21677750; 24014879; 24194600; 27626380; 28700664; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,016 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |