| IED ID | IndEnz0002001428 |
| Enzyme Type ID | protease001428 |
| Protein Name |
Serine protease 57 EC 3.4.21.- Neutrophil serine protease 4 NSP4 Serine protease 1-like protein 1 |
| Gene Name | PRSS57 PRSSL1 UNQ782/PRO1599 |
| 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 | MGLGLRGWGRPLLTVATALMLPVKPPAGSWGAQIIGGHEVTPHSRPYMASVRFGGQHHCGGFLLRARWVVSAAHCFSHRDLRTGLVVLGAHVLSTAEPTQQVFGIDALTTHPDYHPMTHANDICLLRLNGSAVLGPAVGLLRPPGRRARPPTAGTRCRVAGWGFVSDFEELPPGLMEAKVRVLDPDVCNSSWKGHLTLTMLCTRSGDSHRRGFCSADSGGPLVCRNRAHGLVSFSGLWCGDPKTPDVYTQVSAFVAWIWDVVRRSSPQPGPLPGTTRPPGEAA |
| Enzyme Length | 283 |
| Uniprot Accession Number | Q6UWY2 |
| Absorption | |
| Active Site | ACT_SITE 74; /note=Charge relay system; /evidence=ECO:0000305|PubMed:25156428; ACT_SITE 122; /note=Charge relay system; /evidence=ECO:0000305|PubMed:25156428; ACT_SITE 218; /note=Charge relay system; /evidence=ECO:0000305|PubMed:25156428 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPINA1, SERPINC1 and SERPING1. {ECO:0000269|PubMed:22474388}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease that cleaves preferentially after Arg residues (PubMed:22474388, PubMed:23904161, PubMed:25156428). Can also cleave after citrulline (deimidated arginine) and methylarginine residues (PubMed:25156428). {ECO:0000269|PubMed:22474388, ECO:0000269|PubMed:23904161, ECO:0000269|PubMed:25156428}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Helix (5); Mutagenesis (3); Natural variant (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Disulfide bond;Glycoprotein;Heparin-binding;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic granule lumen {ECO:0000269|PubMed:22474388, ECO:0000269|PubMed:23904161}. Secreted {ECO:0000269|PubMed:22474388, ECO:0000269|PubMed:23904161}. Note=Stored in cytoplasmic granules and secreted as active enzyme in response to stimulation of neutrophils. {ECO:0000269|PubMed:22474388}. |
| Modified Residue | |
| Post Translational Modification | PTM: After cleavage of the signal peptide, the N-terminus is probably further processed by CTSC (PubMed:22474388, PubMed:23904161). Processing by CTSC is probably required for accumulation in cytoplasmic granules; in the absence of CTSC the protein does not accumulate (PubMed:23904161). {ECO:0000269|PubMed:23904161, ECO:0000305|PubMed:22474388}.; PTM: N-glycosylated. {ECO:0000269|PubMed:23904161}. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:22474388 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4Q7X; 4Q7Y; 4Q7Z; 4Q80; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,334 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |