Detail Information for IndEnz0002002600
IED ID IndEnz0002002600
Enzyme Type ID protease002600
Protein Name Leukocyte elastase inhibitor
LEI
Serpin B1
Gene Name SERPINB1 ELANH2
Organism Equus caballus (Horse)
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 Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse)
Enzyme Sequence MEQLSTANTHFAVDLFRALNESDPTGNIFISPLSISSALAMIFLGTRGNTAAQVSKALYFDTVEDIHSRFQSLNADINKPGAPYILKLANRLYGEKTYNFLADFLASTQKMYGAELASVDFQQAPEDARKEINEWVKGQTEGKIPELLVKGMVDNMTKLVLVNAIYFKGNWQEKFMKEATRDAPFRLNKKDTKTVKMMYQKKKFPYNYIEDLKCRVLELPYQGKELSMIILLPDDIEDESTGLEKIEKQLTLEKLREWTKPENLYLAEVNVHLPRFKLEESYDLTSHLARLGVQDLFNRGKADLSGMSGARDLFVSKIIHKSFVDLNEEGTEAAAATAGTIMLAMLMPEENFNADHPFIFFIRHNPSANILFLGRFSSP
Enzyme Length 379
Uniprot Accession Number P05619
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}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (19); Chain (1); Helix (15); Modified residue (3); Region (1); Site (1); Turn (4)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Endosome;Lysosome;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 177; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P30740
Post Translational Modification PTM: The N-terminus is blocked.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1HLE;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 43,006
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda