| IED ID | IndEnz0002015374 |
| Enzyme Type ID | protease015374 |
| Protein Name |
Leukocyte elastase inhibitor LEI Leukocyte neutral proteinase inhibitor LNPI Serpin B1 |
| Gene Name | SERPINB1 ELANH2 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MEQLSAANTRFALDLFRALNESNPAGNIFISPFSISSALAMILLGTRGNTEAQMSKALHFDTVKDIHSRFQSLNADINKCGASYILKLANRLFGEKTYHFLPEFLASTQKTYGAELASVDFLRASEEARKAINEWVKEQTEGKIPELLASGVVDSATKLVLVNAIYFKGSWQEKFMTEATKDAPFRLNKKDSKTVKMMYQKKKFPFGYIKELKCRVLELPYQGKDLSMVILLPDSIEDESTGLRKIEQHLTLEKLNEWTKPDNLELLEVNVHLPRFRLEESYDLNAPLARLGVQDLFGSRADLTGMSEARDLFISKVVHKAFVEVNEEGTEAAAATAGIAVFAMLMPEEDFIADHPFIFFIRHNPSSNILFLGRLSSP |
| Enzyme Length | 378 |
| Uniprot Accession Number | P80229 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis. Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes but when released from granules, these potent enzymes also destroy host proteins and contribute to mortality. Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Acts also as a potent intracellular inhibitor of GZMH by directly blocking its proteolytic activity. During inflammation, limits the activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation. When secreted, promotes the proliferation of beta-cells via its protease inhibitory function. {ECO:0000250|UniProtKB:P30740}.; FUNCTION: May be cleaved leading to a loss of its anti-protease activity and to the appearance of an endonuclease activity. However no catalytic site was identified. {ECO:0000269|PubMed:9584202}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Modified residue (3); Region (1); Site (1) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Disulfide bond;Endosome;Lysosome;Phosphoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P30740}. Cytoplasm {ECO:0000250|UniProtKB:P30740}. Cytolytic granule {ECO:0000250|UniProtKB:P30740}. Early endosome {ECO:0000250|UniProtKB:P30740}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P30740; MOD_RES 137; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P30740; MOD_RES 299; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P30740 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,513 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |