| IED ID | IndEnz0002006645 |
| Enzyme Type ID | protease006645 |
| Protein Name |
Kallikrein-4 EC 3.4.21.- Enamel matrix serine proteinase 1 Kallikrein-like protein 1 KLK-L1 Prostase Serine protease 17 |
| Gene Name | KLK4 EMSP1 PRSS17 PSTS |
| 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 | MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS |
| Enzyme Length | 254 |
| Uniprot Accession Number | Q9Y5K2 |
| Absorption | |
| Active Site | ACT_SITE 71; /note=Charge relay system; /evidence=ECO:0000269|PubMed:16950394; ACT_SITE 116; /note=Charge relay system; /evidence=ECO:0000269|PubMed:16950394; ACT_SITE 207; /note=Charge relay system; /evidence=ECO:0000269|PubMed:16950394 |
| 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 (PubMed:15235027). Required during the maturation stage of tooth development for clearance of enamel proteins and normal structural patterning of the crystalline matrix (By similarity). {ECO:0000250|UniProtKB:Q9Z0M1, ECO:0000269|PubMed:15235027}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (16); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (5); Metal binding (2); Natural variant (3); Propeptide (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Amelogenesis imperfecta;Biomineralization;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zinc;Zymogen |
| Interact With | P20155; Q06418 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| 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:0000250|UniProtKB:Q9Z0M1}. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (13) |
| Cross Reference PDB | 2BDG; 2BDH; 2BDI; 4K1E; 4K8Y; 4KEL; 4KGA; 6KBR; 6NVB; 6O21; 7JQK; 7JQN; 7JQO; |
| Mapped Pubmed ID | 12077288; 15059887; 16172196; 16322328; 16497155; 16704423; 16800736; 17221837; 17545602; 18221492; 18308730; 18567807; 18687310; 18714142; 19190825; 19372141; 19423540; 19795418; 19966041; 20009893; 20056842; 20180634; 20406964; 20406994; 20424135; 20460480; 21874303; 22970239; 23201139; 23355523; 23798432; 24405067; 24854539; 25153390; 25153393; 25416956; 25563717; 25724897; 25862839; 26124219; 26420451; 26546590; 26620968; 27378148; 27767076; 28150891; 28445870; 28510269; 28743213; 29229389; 29795101; 29975661; 30055641; 30644845; 30811511; 30945557; 31058493; 31264534; 31265790; 31391482; 31397325; 31829025; 31868942; 34342281; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,032 |
| Kinetics | |
| Metal Binding | METAL 40; /note=Zinc; /evidence=ECO:0000269|PubMed:16950394; METAL 91; /note=Zinc; /evidence=ECO:0000269|PubMed:16950394 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B12; |