| IED ID | IndEnz0002002990 |
| Enzyme Type ID | protease002990 |
| Protein Name |
Kallikrein-4 EC 3.4.21.- Enamel matrix serine proteinase 1 Kallikrein-like protein 1 Serine protease 17 |
| Gene Name | Klk4 EMSP1 KLK-L1 Prss17 |
| 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 | MMVTARTPWGWFLGCLILEVTGASASSVSSRIIQGQDCSPHSQPWQAALFSEDGFFCSGVLVHPQWVLSAAHCLQESYIVGLGLHNLKGSQEPGSRMLEAHLSIQHPNFNDPSFANDLMLIKLNESVIESNTIRSIPVATQCPTPGDTCLVSGWGQLKNGKLPSLLQCVNLSVASEETCRLLYDPVYHLSMFCAGGGQDQKDSCNGDSGGPIVCNRSLQGLVSMGQGKCGQPGIPSVYTNLCKFTNWIQTIIQTN |
| Enzyme Length | 255 |
| Uniprot Accession Number | Q9Z0M1 |
| Absorption | |
| Active Site | ACT_SITE 72; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 117; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 208; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Has a major role in enamel formation. Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix. {ECO:0000269|PubMed:19578120}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Metal binding (2); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Biomineralization;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. The N-glycan structures are of complex diantennary or triantennary type, which may be further modified with up to 2 sialic acid residues. {ECO:0000269|PubMed:22243251}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10673550; 12206593; 12466851; 15192120; 15203212; 15331780; 18714142; 19407151; 20487000; 21267068; 21285247; 21454549; 21546759; 22243238; 22243248; 22351765; 24194600; 24278477; 26620968; 27066511; 27626380; 28174279; 28650075; 29288201; 29684584; 32674056; 34722506; 34781073; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,488 |
| Kinetics | |
| Metal Binding | METAL 41; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q9Y5K2; METAL 92; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q9Y5K2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B12; |