Detail Information for IndEnz0002010546
IED ID IndEnz0002010546
Enzyme Type ID protease010546
Protein Name Myeloblastin
EC 3.4.21.76
Proteinase 3
PR-3
Gene Name Prtn3
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSGSYPSPKGIHPFLLLALVVGGAVQASKIVGGHEARPHSRPYVASLQLSRFPGSHFCGGTLIHPRFVLTAAHCLQDISWQLVTVVLGAHDLLSSEPEQQKFTISQVFQNNYNPEENLNDVLLLQLNRTASLGKEVAVASLPQQDQTLSQGTQCLAMGWGRLGTQAPTPRVLQELNVTVVTFLCREHNVCTLVPRRAAGICFGDSGGPLICNGILHGVDSFVIRECASLQFPDFFARVSMYVDWIQNVLRGAEP
Enzyme Length 254
Uniprot Accession Number Q61096
Absorption
Active Site ACT_SITE 73; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 205; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.; EC=3.4.21.76; Evidence={ECO:0000250|UniProtKB:P24158};
DNA Binding
EC Number 3.4.21.76
Enzyme Function FUNCTION: Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177. {ECO:0000250|UniProtKB:P24158}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (2); Sequence conflict (1); Signal peptide (1)
Keywords Cell membrane;Collagen degradation;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P24158}. Secreted {ECO:0000250|UniProtKB:P24158}. Cell membrane {ECO:0000250|UniProtKB:P24158}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24158}; Extracellular side {ECO:0000250|UniProtKB:P24158}. Membrane raft {ECO:0000250|UniProtKB:P24158}; Peripheral membrane protein {ECO:0000250|UniProtKB:P24158}; Extracellular side {ECO:0000250|UniProtKB:P24158}. Note=Localizes predominantly to azurophil granules (primary secretory granules) in neutrophils. Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration. Following secretion tethered to the cell membrane by CD177. {ECO:0000250|UniProtKB:P24158}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10037495; 10051312; 11290610; 12189154; 14610273; 15150076; 15919778; 16182289; 18023421; 18166659; 18568075; 19494315; 19833730; 20015271; 21160041; 21464320; 21677750; 22213227; 25180606; 25331958; 26185250; 26436651; 30392974; 32002713; 8996238; 9611252;
Motif
Gene Encoded By
Mass 27,626
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.76;