| IED ID | IndEnz0002001509 |
| Enzyme Type ID | protease001509 |
| Protein Name |
Antileukoproteinase ALP BLPI HUSI-1 Mucus proteinase inhibitor MPI Protease inhibitor WAP4 Secretory leukocyte protease inhibitor Seminal proteinase inhibitor WAP four-disulfide core domain protein 4 |
| Gene Name | SLPI WAP4 WFDC4 |
| 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 | MKSSGLFPFLVLLALGTLAPWAVEGSGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKA |
| Enzyme Length | 132 |
| Uniprot Accession Number | P03973 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:3533531, PubMed:3462719, PubMed:2039600, PubMed:2110563, PubMed:10702419, PubMed:24121345). Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:10702419, PubMed:24352879). Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (PubMed:24352879). {ECO:0000250|UniProtKB:P97430, ECO:0000269|PubMed:10702419, ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:2110563, ECO:0000269|PubMed:24121345, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3533531, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Chain (1); Disulfide bond (8); Domain (2); Helix (1); Mutagenesis (7); Region (1); Signal peptide (1); Site (1) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Direct protein sequencing;Disulfide bond;Immunity;Innate immunity;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal |
| Interact With | Q9BXU9; Q96Q77; Q12805; Q8IZU0; P49639; O43561-2; Q13064; P41271-2; Q96HA8; Q8WWB5; O43765; Q96EQ0; Q96QK8; Q9UMX0; Q9UHD9 |
| Induction | INDUCTION: Down-regulated in response to low ELANE activity. Up-regulated by ELANE treatment in bone marrow cells. {ECO:0000269|PubMed:24352879}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence="ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543" |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2Z7F; 4DOQ; |
| Mapped Pubmed ID | 11667971; 11759111; 11817677; 11868825; 12023766; 12023969; 12183536; 12351521; 12732717; 12934194; 14743216; 15015603; 15020232; 15039315; 15039364; 15155685; 15167969; 15248236; 15315966; 15492784; 15650263; 15812165; 16015083; 16336202; 16384861; 16776851; 17371258; 17878156; 17964057; 18075823; 18173453; 18285402; 18425362; 18667508; 18688858; 18953959; 18976018; 19039956; 19095674; 19154415; 19254589; 19271144; 19333378; 19900269; 20047904; 20068074; 20378727; 21335488; 21377455; 21503571; 21641406; 21676452; 21687932; 21940052; 21994455; 22493362; 22537232; 22786767; 23650620; 23996702; 24023032; 24073410; 24121782; 24282288; 24606882; 24764155; 25041028; 25056659; 25319722; 25416956; 25559229; 25814554; 25917460; 26121748; 26239418; 26376365; 26555393; 26876202; 27238568; 28031424; 28255192; 28450389; 28606626; 28637988; 29436667; 29892293; 30180755; 31019507; 31476404; 31843555; 31925640; 32871084; 33016205; 33101778; 33147448; 33157500; 33387869; 33485930; 33506054; 34155270; 34214131; 34580954; |
| Motif | |
| Gene Encoded By | |
| Mass | 14,326 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |