| IED ID | IndEnz0002004143 |
| Enzyme Type ID | protease004143 |
| Protein Name |
Kallikrein-14 hK14 EC 3.4.21.- Kallikrein-like protein 6 KLK-L6 |
| Gene Name | KLK14 KLKL6 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSLRVLGSGTWPSAPKMFLLLTALQVLAIAMTQSQEDENKIIGGHTCTRSSQPWQAALLAGPRRRFLCGGALLSGQWVITAAHCGRPILQVALGKHNLRRWEATQQVLRVVRQVTHPNYNSRTHDNDLMLLQLQQPARIGRAVRPIEVTQACASPGTSCRVSGWGTISSPIARYPASLQCVNINISPDEVCQKAYPRTITPGMVCAGVPQGGKDSCQGDSGGPLVCRGQLQGLVSWGMERCALPGYPGVYTNLCKYRSWIEETMRDK |
| Enzyme Length | 267 |
| Uniprot Accession Number | Q9P0G3 |
| Absorption | |
| Active Site | ACT_SITE 83; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 127; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 220; /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. {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383, ECO:0000269|PubMed:17158887}. |
| 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. {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16885167, ECO:0000269|PubMed:17158887, ECO:0000269|PubMed:17625593, ECO:0000269|PubMed:18056261, ECO:0000269|PubMed:18482984}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Domain (1); Erroneous gene model prediction (4); Erroneous initiation (1); Natural variant (3); Propeptide (1); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated by steroid hormone. {ECO:0000269|PubMed:12645335}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16456535, ECO:0000269|PubMed:17110383}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage of the activation peptide produces the active enzyme. {ECO:0000269|PubMed:17110383}. |
| Signal Peptide | SIGNAL 1..34 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12439719; 12858357; 16434994; 18497543; 18627302; 19147544; 19383315; 19558318; 20155713; 20424135; 20667819; 21057706; 22505522; 22505523; 22505524; 23224034; 27533117; 29546479; 31630475; 32169475; 32575583; |
| Motif | |
| Gene Encoded By | |
| Mass | 29,122 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for S-2288 {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.2 mM for S-2222 {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.2 mM for S-2302 {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.7 mM for S-2586 {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.045 mM for Gln-Ala-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.043 mM for Val-Pro-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.09 mM for Pro-Phe-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.278 mM for Phe-Ser-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.0577 mM for Leu-Gly-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.139 mM for Gln-Gly-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.173 mM for Gly-Pro-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.0268 mM for Gln-Arg-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.130 mM for Gly-Gly-Arg synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; KM=0.578 mM for Val-Leu-Lys synthetic peptide {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383}; Note=Has a higher catalytic efficiency for the trypsin-like enzyme substrates S-2288, S-2222 and S-2302 compared to S-2586 a chymotrypsin-like enzyme substrate. Has a lower catalytic activity compared to trypsin towards S-2288, S-2222 and S-2302. Cleaves preferentially after Arg residues.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B45; |