IED ID | IndEnz0002005759 |
Enzyme Type ID | protease005759 |
Protein Name |
Kallikrein-7 hK7 EC 3.4.21.117 Serine protease 6 Stratum corneum chymotryptic enzyme hSCCE |
Gene Name | KLK7 PRSS6 SCCE |
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 | MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR |
Enzyme Length | 253 |
Uniprot Accession Number | P49862 |
Absorption | |
Active Site | ACT_SITE 70; /note=Charge relay system; /evidence=ECO:0000269|PubMed:17909180; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000269|PubMed:17909180; ACT_SITE 205; /note=Charge relay system; /evidence=ECO:0000269|PubMed:17909180 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by Zn2+ and Cu2+ at low micromolar concentrations. Inhibited by SERPINA12. {ECO:0000269|PubMed:23370777}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of proteins with aromatic side chains in the P1 position.; EC=3.4.21.117; |
DNA Binding | |
EC Number | 3.4.21.117 |
Enzyme Function | FUNCTION: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines. {ECO:0000269|PubMed:23370777}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (1); Beta strand (16); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (5); Mutagenesis (2); Propeptide (1); Sequence conflict (1); Signal peptide (1); Site (1); Turn (1) |
Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
Interact With | |
Induction | INDUCTION: By estrogens and glucocorticoids in a breast carcinoma cell line. {ECO:0000269|PubMed:10974542}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12738725}. Note=In ovarian carcinoma, secreted and also observed at the apical membrane and in cytoplasm at the invasive front. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:8034709 |
Structure 3D | X-ray crystallography (12) |
Cross Reference PDB | 2QXG; 2QXH; 2QXI; 2QXJ; 3BSQ; 5FAH; 5Y9L; 5YJK; 6SHH; 6SHI; 6SJU; 6Y4S; |
Mapped Pubmed ID | 14691584; 14972646; 15140227; 15191543; 15297163; 15675955; 15766562; 16628198; 17012259; 17332331; 17354228; 17989887; 18163887; 18325919; 18343220; 18774391; 18953252; 18976018; 19085836; 19091121; 19118981; 19423540; 19453546; 19558318; 19921697; 20090765; 20406964; 20424135; 20438785; 20544292; 20944116; 21168996; 21520985; 21548205; 21616098; 21868565; 22521249; 22573795; 22825846; 23224034; 23413953; 23495698; 25153388; 25182706; 25448018; 25477184; 25640309; 26022646; 26231762; 27279059; 27478344; 27769847; 27775713; 28479159; 28636767; 29102227; 29319165; 29498930; 29779317; 30644845; 30705123; 31883963; 32323843; 32374603; 33276948; 33588911; |
Motif | |
Gene Encoded By | |
Mass | 27,525 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.117; |