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; |