IED ID | IndEnz0002007689 |
Enzyme Type ID | protease007689 |
Protein Name |
Myeloblastin EC 3.4.21.76 AGP7 C-ANCA antigen Leukocyte proteinase 3 PR-3 PR3 Neutrophil proteinase 4 NP-4 P29 Wegener autoantigen |
Gene Name | PRTN3 MBN |
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 | MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLRRVEAKGRP |
Enzyme Length | 256 |
Uniprot Accession Number | P24158 |
Absorption | |
Active Site | ACT_SITE 71; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 118; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 203; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF) and diisopropyl fluorophosphate (DFP). {ECO:0000269|PubMed:3198760}. |
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:0000269|PubMed:2033050, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}; |
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) (PubMed:3198760, PubMed:2033050, PubMed:28240246). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration (PubMed:23202369). May play a role in neutrophil transendothelial migration, probably when associated with CD177 (PubMed:22266279). {ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:23202369, ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:3198760}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:3198760}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (17); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Frameshift (1); Glycosylation (2); Helix (4); Natural variant (3); Propeptide (2); Sequence conflict (9); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Cell membrane;Collagen degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
Interact With | P24001-4 |
Induction | INDUCTION: Induced during CSF3/G-CSF-mediated neutrophil differentiation. {ECO:0000269|PubMed:18462208}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245, ECO:0000305|PubMed:17244676}. Secreted {ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:28240246}. Cell membrane {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246}; Peripheral membrane protein {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246}; Extracellular side {ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246}. Membrane raft {ECO:0000269|PubMed:21193407}; Peripheral membrane protein {ECO:0000269|PubMed:21193407}; Extracellular side {ECO:0000269|PubMed:21193407}. Note=Localizes predominantly to azurophil granules (primary secretory granules) in neutrophils (PubMed:2033050, PubMed:3198760, PubMed:7897245, PubMed:18462208). Secreted upon neutrophil stimulation by TNF-alpha, lipopolysaccharide (LPS), fMLP and CXCL8/IL8 or during neutrophil transmigration (PubMed:22266279, PubMed:28240246). Following secretion tethered to the cell membrane by CD177 (PubMed:18462208, PubMed:22266279). {ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:2033050, ECO:0000269|PubMed:22266279, ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:3198760, ECO:0000269|PubMed:7897245}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1FUJ; |
Mapped Pubmed ID | 11035113; 11115080; 11389039; 11714826; 12067299; 12114510; 12135665; 12140766; 12191967; 12200377; 12354776; 12393722; 12444202; 12506139; 12538645; 12832446; 12894870; 12960243; 14525959; 14675038; 15331626; 15527767; 15686586; 15879139; 15916759; 15975933; 16167885; 16263417; 16488976; 16598772; 16792675; 16799473; 17088257; 17158864; 17174955; 17412886; 17452051; 17534941; 17634439; 17681950; 17712045; 17785293; 18021746; 18023421; 18076025; 18596726; 18854317; 19185066; 19447886; 19490915; 19494315; 19913121; 20059480; 20155833; 20412702; 20412704; 20423453; 20491791; 20592714; 20628086; 20828556; 21193404; 21470489; 21700341; 22138257; 22210048; 22270365; 22510451; 22791638; 22810585; 22844112; 22936713; 22952809; 23380137; 23911525; 23957616; 24052258; 24271323; 24291125; 24719228; 24929239; 24949444; 25092677; 25180606; 25416382; 25461407; 25461571; 25788529; 25927497; 26436651; 26873743; 26939803; 26961880; 27559009; 27752292; 27821628; 28029757; 28339364; 28428279; 28546501; 29079698; 29132840; 29621735; 30021768; 30236095; 30880498; 30938436; 31125555; 31490025; 31963828; 31995266; 32303641; 32794199; 33023023; 33679731; 34292081; 8692836; |
Motif | |
Gene Encoded By | |
Mass | 27,807 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.21.76; |